[{"oa":1,"publisher":"Taylor & Francis","quality_controlled":"1","acknowledgement":"We thank members of the Hetzer lab for critical review of the manuscript; Novogene for mRNA library preparation and sequencing; the Next-Generation Sequencing Core Facility at the Salk Institute, with funding from NIH-NCI CCSG: P30 014195, the Chapman Foundation, and the Helmsley Charitable Trust, for sequencing Cut&Run libraries; and the Waitt Advanced Biophotonics Core Facility at the Salk Institute, with funding from NIH-NCI CCSG: P30 014195, the Waitt Foundation, and the Chan-Zuckerberg Initiative Imaging Scientist Award, for electron microscopy sample preparation and imaging.","date_created":"2023-04-30T22:01:06Z","date_published":"2023-04-18T00:00:00Z","doi":"10.1080/19491034.2023.2202548","year":"2023","has_accepted_license":"1","isi":1,"publication":"Nucleus","day":"18","article_number":"2202548","article_processing_charge":"No","external_id":{"isi":["000971629400001"],"pmid":["37071033"]},"author":[{"full_name":"Kaneshiro, Jeanae M.","last_name":"Kaneshiro","first_name":"Jeanae M."},{"last_name":"Capitanio","full_name":"Capitanio, Juliana S.","first_name":"Juliana S."},{"last_name":"Hetzer","full_name":"Hetzer, Martin W","orcid":"0000-0002-2111-992X","first_name":"Martin W","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed"}],"title":"Lamin B1 overexpression alters chromatin organization and gene expression","citation":{"chicago":"Kaneshiro, Jeanae M., Juliana S. Capitanio, and Martin Hetzer. “Lamin B1 Overexpression Alters Chromatin Organization and Gene Expression.” Nucleus. Taylor & Francis, 2023. https://doi.org/10.1080/19491034.2023.2202548.","ista":"Kaneshiro JM, Capitanio JS, Hetzer M. 2023. Lamin B1 overexpression alters chromatin organization and gene expression. Nucleus. 14(1), 2202548.","mla":"Kaneshiro, Jeanae M., et al. “Lamin B1 Overexpression Alters Chromatin Organization and Gene Expression.” Nucleus, vol. 14, no. 1, 2202548, Taylor & Francis, 2023, doi:10.1080/19491034.2023.2202548.","apa":"Kaneshiro, J. M., Capitanio, J. S., & Hetzer, M. (2023). Lamin B1 overexpression alters chromatin organization and gene expression. Nucleus. Taylor & Francis. https://doi.org/10.1080/19491034.2023.2202548","ama":"Kaneshiro JM, Capitanio JS, Hetzer M. Lamin B1 overexpression alters chromatin organization and gene expression. Nucleus. 2023;14(1). doi:10.1080/19491034.2023.2202548","short":"J.M. Kaneshiro, J.S. Capitanio, M. Hetzer, Nucleus 14 (2023).","ieee":"J. M. Kaneshiro, J. S. Capitanio, and M. Hetzer, “Lamin B1 overexpression alters chromatin organization and gene expression,” Nucleus, vol. 14, no. 1. Taylor & Francis, 2023."},"user_id":"4359f0d1-fa6c-11eb-b949-802e58b17ae8","scopus_import":"1","intvolume":" 14","month":"04","abstract":[{"text":"Peripheral heterochromatin positioning depends on nuclear envelope associated proteins and repressive histone modifications. Here we show that overexpression (OE) of Lamin B1 (LmnB1) leads to the redistribution of peripheral heterochromatin into heterochromatic foci within the nucleoplasm. These changes represent a perturbation of heterochromatin binding at the nuclear periphery (NP) through a mechanism independent from altering other heterochromatin anchors or histone post-translational modifications. We further show that LmnB1 OE alters gene expression. These changes do not correlate with different levels of H3K9me3, but a significant number of the misregulated genes were likely mislocalized away from the NP upon LmnB1 OE. We also observed an enrichment of developmental processes amongst the upregulated genes. ~74% of these genes were normally repressed in our cell type, suggesting that LmnB1 OE promotes gene de-repression. This demonstrates a broader consequence of LmnB1 OE on cell fate, and highlights the importance of maintaining proper levels of LmnB1.","lang":"eng"}],"pmid":1,"oa_version":"Published Version","license":"https://creativecommons.org/licenses/by-nc/4.0/","volume":14,"issue":"1","publication_status":"published","publication_identifier":{"issn":["1949-1034"],"eissn":["1949-1042"]},"language":[{"iso":"eng"}],"file":[{"file_name":"2023_Nucleus_Kaneshiro.pdf","date_created":"2023-05-02T07:24:55Z","creator":"dernst","file_size":3811113,"date_updated":"2023-05-02T07:24:55Z","success":1,"file_id":"12884","checksum":"8e707eda84f64dbad7f03545ae0a83ef","relation":"main_file","access_level":"open_access","content_type":"application/pdf"}],"tmp":{"legal_code_url":"https://creativecommons.org/licenses/by-nc/4.0/legalcode","image":"/images/cc_by_nc.png","name":"Creative Commons Attribution-NonCommercial 4.0 International (CC BY-NC 4.0)","short":"CC BY-NC (4.0)"},"article_type":"original","type":"journal_article","status":"public","_id":"12880","file_date_updated":"2023-05-02T07:24:55Z","department":[{"_id":"MaHe"}],"date_updated":"2023-08-01T14:18:46Z","ddc":["570"]},{"volume":12,"license":"https://creativecommons.org/licenses/by/4.0/","publication_identifier":{"eissn":["2050-084X"]},"publication_status":"published","file":[{"date_created":"2023-09-15T06:59:10Z","file_name":"2023_eLife_Cho.pdf","creator":"dernst","date_updated":"2023-09-15T06:59:10Z","file_size":3703097,"file_id":"14336","checksum":"db24bf3d595507387b48d3799c33e289","success":1,"access_level":"open_access","relation":"main_file","content_type":"application/pdf"}],"language":[{"iso":"eng"}],"scopus_import":"1","month":"09","intvolume":" 12","abstract":[{"text":"During apoptosis, caspases degrade 8 out of ~30 nucleoporins to irreversibly demolish the nuclear pore complex. However, for poorly understood reasons, caspases are also activated during cell differentiation. Here, we show that sublethal activation of caspases during myogenesis results in the transient proteolysis of four peripheral Nups and one transmembrane Nup. ‘Trimmed’ NPCs become nuclear export-defective, and we identified in an unbiased manner several classes of cytoplasmic, plasma membrane, and mitochondrial proteins that rapidly accumulate in the nucleus. NPC trimming by non-apoptotic caspases was also observed in neurogenesis and endoplasmic reticulum stress. Our results suggest that caspases can reversibly modulate nuclear transport activity, which allows them to function as agents of cell differentiation and adaptation at sublethal levels.","lang":"eng"}],"oa_version":"Published Version","pmid":1,"file_date_updated":"2023-09-15T06:59:10Z","department":[{"_id":"MaHe"}],"date_updated":"2023-09-15T07:07:10Z","ddc":["570"],"article_type":"original","type":"journal_article","tmp":{"legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","image":"/images/cc_by.png","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","short":"CC BY (4.0)"},"status":"public","_id":"14315","date_published":"2023-09-04T00:00:00Z","doi":"10.7554/eLife.89066","date_created":"2023-09-10T22:01:11Z","has_accepted_license":"1","year":"2023","day":"04","publication":"eLife","publisher":"eLife Sciences Publications","quality_controlled":"1","oa":1,"acknowledgement":"We thank the members of the Hetzer laboratory, Tony Hunter (Salk), Lorenzo Puri (Sanford Burnham Prebys), and Jongmin Kim (Massachusetts General Hospital) for the critical reading of the manuscript; Kenneth Diffenderfer and Aimee Pankonin (Stem Cell Core at the Salk Institute) for help with neurogenesis; Carol Marchetto and Fred Gage (Salk) for providing H9 embryonic stem cells; Lorenzo Puri, Alexandra Sacco, and Luca Caputo (Sanford Burnham Prebys) for helpful discussions and sharing mouse primary myoblasts. This work was supported by a Glenn Foundation for Medical Research Postdoctoral Fellowship in Aging Research (UHC), the NOMIS foundation (MWH), and the National Institutes of Health (R01 NS096786 to MWH and K01 AR080828 to UHC). This work was also supported by the Mass Spectrometry Core of the Salk Institute with funding from NIH-NCI CCSG: P30 014195 and the Helmsley Center for Genomic Medicine. We thank Jolene Diedrich and Antonio Pinto for technical support.","author":[{"first_name":"Ukrae H.","full_name":"Cho, Ukrae H.","last_name":"Cho"},{"last_name":"Hetzer","orcid":"0000-0002-2111-992X","full_name":"Hetzer, Martin W","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","first_name":"Martin W"}],"external_id":{"pmid":["37665327"]},"article_processing_charge":"Yes","title":"Caspase-mediated nuclear pore complex trimming in cell differentiation and endoplasmic reticulum stress","citation":{"chicago":"Cho, Ukrae H., and Martin Hetzer. “Caspase-Mediated Nuclear Pore Complex Trimming in Cell Differentiation and Endoplasmic Reticulum Stress.” ELife. eLife Sciences Publications, 2023. https://doi.org/10.7554/eLife.89066.","ista":"Cho UH, Hetzer M. 2023. Caspase-mediated nuclear pore complex trimming in cell differentiation and endoplasmic reticulum stress. eLife. 12, RP89066.","mla":"Cho, Ukrae H., and Martin Hetzer. “Caspase-Mediated Nuclear Pore Complex Trimming in Cell Differentiation and Endoplasmic Reticulum Stress.” ELife, vol. 12, RP89066, eLife Sciences Publications, 2023, doi:10.7554/eLife.89066.","ieee":"U. H. Cho and M. Hetzer, “Caspase-mediated nuclear pore complex trimming in cell differentiation and endoplasmic reticulum stress,” eLife, vol. 12. eLife Sciences Publications, 2023.","short":"U.H. Cho, M. Hetzer, ELife 12 (2023).","ama":"Cho UH, Hetzer M. Caspase-mediated nuclear pore complex trimming in cell differentiation and endoplasmic reticulum stress. eLife. 2023;12. doi:10.7554/eLife.89066","apa":"Cho, U. H., & Hetzer, M. (2023). Caspase-mediated nuclear pore complex trimming in cell differentiation and endoplasmic reticulum stress. ELife. eLife Sciences Publications. https://doi.org/10.7554/eLife.89066"},"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","article_number":"RP89066"},{"_id":"11051","status":"public","keyword":["Cell Biology"],"type":"journal_article","article_type":"review","extern":"1","date_updated":"2022-07-18T08:58:33Z","oa_version":"None","pmid":1,"abstract":[{"lang":"eng","text":"Nuclear pore complexes (NPCs) bridge the nucleus and the cytoplasm and are indispensable for crucial cellular activities, such as bidirectional molecular trafficking and gene transcription regulation. The discovery of long-lived proteins (LLPs) in NPCs from postmitotic cells raises the exciting possibility that the maintenance of NPC integrity might play an inherent role in lifelong cell function. Age-dependent deterioration of NPCs and loss of nuclear integrity have been linked to age-related decline in postmitotic cell function and degenerative diseases. In this review, we discuss our current understanding of NPC maintenance in proliferating and postmitotic cells, and how malfunction of nucleoporins (Nups) might contribute to the pathogenesis of various neurodegenerative and cardiovascular diseases."}],"month":"03","intvolume":" 32","scopus_import":"1","language":[{"iso":"eng"}],"publication_identifier":{"issn":["0962-8924"]},"publication_status":"published","volume":32,"issue":"3","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","citation":{"ieee":"J. Liu and M. Hetzer, “Nuclear pore complex maintenance and implications for age-related diseases,” Trends in Cell Biology, vol. 32, no. 3. Elsevier, pp. P216-227, 2022.","short":"J. Liu, M. Hetzer, Trends in Cell Biology 32 (2022) P216-227.","ama":"Liu J, Hetzer M. Nuclear pore complex maintenance and implications for age-related diseases. Trends in Cell Biology. 2022;32(3):P216-227. doi:10.1016/j.tcb.2021.10.001","apa":"Liu, J., & Hetzer, M. (2022). Nuclear pore complex maintenance and implications for age-related diseases. Trends in Cell Biology. Elsevier. https://doi.org/10.1016/j.tcb.2021.10.001","mla":"Liu, Jinqiang, and Martin Hetzer. “Nuclear Pore Complex Maintenance and Implications for Age-Related Diseases.” Trends in Cell Biology, vol. 32, no. 3, Elsevier, 2022, pp. P216-227, doi:10.1016/j.tcb.2021.10.001.","ista":"Liu J, Hetzer M. 2022. Nuclear pore complex maintenance and implications for age-related diseases. Trends in Cell Biology. 32(3), P216-227.","chicago":"Liu, Jinqiang, and Martin Hetzer. “Nuclear Pore Complex Maintenance and Implications for Age-Related Diseases.” Trends in Cell Biology. Elsevier, 2022. https://doi.org/10.1016/j.tcb.2021.10.001."},"title":"Nuclear pore complex maintenance and implications for age-related diseases","author":[{"last_name":"Liu","full_name":"Liu, Jinqiang","first_name":"Jinqiang"},{"last_name":"HETZER","orcid":"0000-0002-2111-992X","full_name":"HETZER, Martin W","first_name":"Martin W","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed"}],"article_processing_charge":"No","external_id":{"pmid":["34782239"]},"publisher":"Elsevier","quality_controlled":"1","day":"01","publication":"Trends in Cell Biology","year":"2022","doi":"10.1016/j.tcb.2021.10.001","date_published":"2022-03-01T00:00:00Z","date_created":"2022-04-07T07:43:01Z","page":"P216-227"},{"_id":"11053","status":"public","keyword":["Geriatrics and Gerontology","Aging"],"type":"journal_article","article_type":"original","extern":"1","date_updated":"2022-07-18T08:27:24Z","pmid":1,"oa_version":"Published Version","abstract":[{"lang":"eng","text":"Understanding basic mechanisms of aging holds great promise for developing interventions that prevent or delay many age-related declines and diseases simultaneously to increase human healthspan. However, a major confounding factor in aging research is the heterogeneity of the aging process itself. At the organismal level, it is clear that chronological age does not always predict biological age or susceptibility to frailty or pathology. While genetics and environment are major factors driving variable rates of aging, additional complexity arises because different organs, tissues, and cell types are intrinsically heterogeneous and exhibit different aging trajectories normally or in response to the stresses of the aging process (e.g., damage accumulation). Tackling the heterogeneity of aging requires new and specialized tools (e.g., single-cell analyses, mass spectrometry-based approaches, and advanced imaging) to identify novel signatures of aging across scales. Cutting-edge computational approaches are then needed to integrate these disparate datasets and elucidate network interactions between known aging hallmarks. There is also a need for improved, human cell-based models of aging to ensure that basic research findings are relevant to human aging and healthspan interventions. The San Diego Nathan Shock Center (SD-NSC) provides access to cutting-edge scientific resources to facilitate the study of the heterogeneity of aging in general and to promote the use of novel human cell models of aging. The center also has a robust Research Development Core that funds pilot projects on the heterogeneity of aging and organizes innovative training activities, including workshops and a personalized mentoring program, to help investigators new to the aging field succeed. Finally, the SD-NSC participates in outreach activities to educate the general community about the importance of aging research and promote the need for basic biology of aging research in particular."}],"month":"10","intvolume":" 43","scopus_import":"1","main_file_link":[{"open_access":"1","url":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8599742/"}],"language":[{"iso":"eng"}],"publication_identifier":{"issn":["2509-2715","2509-2723"]},"publication_status":"published","volume":43,"issue":"5","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","citation":{"mla":"Shadel, Gerald S., et al. “The San Diego Nathan Shock Center: Tackling the Heterogeneity of Aging.” GeroScience, vol. 43, no. 5, Springer Nature, 2021, pp. 2139–48, doi:10.1007/s11357-021-00426-x.","ieee":"G. S. Shadel et al., “The San Diego Nathan Shock Center: Tackling the heterogeneity of aging,” GeroScience, vol. 43, no. 5. Springer Nature, pp. 2139–2148, 2021.","short":"G.S. Shadel, P.D. Adams, W.T. Berggren, J.K. Diedrich, K.E. Diffenderfer, F.H. Gage, N. Hah, M. Hansen, M. Hetzer, A.J.A. Molina, U. Manor, K. Marek, D.D. O’Keefe, A.F.M. Pinto, A. Sacco, T.O. Sharpee, M.N. Shokriev, S. Zambetti, GeroScience 43 (2021) 2139–2148.","apa":"Shadel, G. S., Adams, P. D., Berggren, W. T., Diedrich, J. K., Diffenderfer, K. E., Gage, F. H., … Zambetti, S. (2021). The San Diego Nathan Shock Center: Tackling the heterogeneity of aging. GeroScience. Springer Nature. https://doi.org/10.1007/s11357-021-00426-x","ama":"Shadel GS, Adams PD, Berggren WT, et al. The San Diego Nathan Shock Center: Tackling the heterogeneity of aging. GeroScience. 2021;43(5):2139-2148. doi:10.1007/s11357-021-00426-x","chicago":"Shadel, Gerald S., Peter D. Adams, W. Travis Berggren, Jolene K. Diedrich, Kenneth E. Diffenderfer, Fred H. Gage, Nasun Hah, et al. “The San Diego Nathan Shock Center: Tackling the Heterogeneity of Aging.” GeroScience. Springer Nature, 2021. https://doi.org/10.1007/s11357-021-00426-x.","ista":"Shadel GS, Adams PD, Berggren WT, Diedrich JK, Diffenderfer KE, Gage FH, Hah N, Hansen M, Hetzer M, Molina AJA, Manor U, Marek K, O’Keefe DD, Pinto AFM, Sacco A, Sharpee TO, Shokriev MN, Zambetti S. 2021. The San Diego Nathan Shock Center: Tackling the heterogeneity of aging. GeroScience. 43(5), 2139–2148."},"title":"The San Diego Nathan Shock Center: Tackling the heterogeneity of aging","author":[{"first_name":"Gerald S.","last_name":"Shadel","full_name":"Shadel, Gerald S."},{"last_name":"Adams","full_name":"Adams, Peter D.","first_name":"Peter D."},{"full_name":"Berggren, W. Travis","last_name":"Berggren","first_name":"W. Travis"},{"first_name":"Jolene K.","full_name":"Diedrich, Jolene K.","last_name":"Diedrich"},{"last_name":"Diffenderfer","full_name":"Diffenderfer, Kenneth E.","first_name":"Kenneth E."},{"first_name":"Fred H.","full_name":"Gage, Fred H.","last_name":"Gage"},{"full_name":"Hah, Nasun","last_name":"Hah","first_name":"Nasun"},{"last_name":"Hansen","full_name":"Hansen, Malene","first_name":"Malene"},{"first_name":"Martin W","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","full_name":"HETZER, Martin W","orcid":"0000-0002-2111-992X","last_name":"HETZER"},{"first_name":"Anthony J. A.","full_name":"Molina, Anthony J. A.","last_name":"Molina"},{"first_name":"Uri","full_name":"Manor, Uri","last_name":"Manor"},{"first_name":"Kurt","last_name":"Marek","full_name":"Marek, Kurt"},{"first_name":"David D.","full_name":"O’Keefe, David D.","last_name":"O’Keefe"},{"first_name":"Antonio F. M.","full_name":"Pinto, Antonio F. M.","last_name":"Pinto"},{"first_name":"Alessandra","last_name":"Sacco","full_name":"Sacco, Alessandra"},{"last_name":"Sharpee","full_name":"Sharpee, Tatyana O.","first_name":"Tatyana O."},{"full_name":"Shokriev, Maxim N.","last_name":"Shokriev","first_name":"Maxim N."},{"first_name":"Stefania","last_name":"Zambetti","full_name":"Zambetti, Stefania"}],"article_processing_charge":"No","external_id":{"pmid":["34370163"]},"quality_controlled":"1","publisher":"Springer Nature","oa":1,"day":"01","publication":"GeroScience","year":"2021","date_published":"2021-10-01T00:00:00Z","doi":"10.1007/s11357-021-00426-x","date_created":"2022-04-07T07:43:25Z","page":"2139-2148"},{"year":"2021","day":"08","publication":"Developmental Cell","page":"P2952-2965.e9","doi":"10.1016/j.devcel.2021.10.008","date_published":"2021-11-08T00:00:00Z","date_created":"2022-04-07T07:43:14Z","publisher":"Elsevier","quality_controlled":"1","citation":{"chicago":"Krishna, Shefali, Rafael Arrojo e Drigo, Juliana S. Capitanio, Ranjan Ramachandra, Mark Ellisman, and Martin Hetzer. “Identification of Long-Lived Proteins in the Mitochondria Reveals Increased Stability of the Electron Transport Chain.” Developmental Cell. Elsevier, 2021. https://doi.org/10.1016/j.devcel.2021.10.008.","ista":"Krishna S, Arrojo e Drigo R, Capitanio JS, Ramachandra R, Ellisman M, Hetzer M. 2021. Identification of long-lived proteins in the mitochondria reveals increased stability of the electron transport chain. Developmental Cell. 56(21), P2952–2965.e9.","mla":"Krishna, Shefali, et al. “Identification of Long-Lived Proteins in the Mitochondria Reveals Increased Stability of the Electron Transport Chain.” Developmental Cell, vol. 56, no. 21, Elsevier, 2021, p. P2952–2965.e9, doi:10.1016/j.devcel.2021.10.008.","apa":"Krishna, S., Arrojo e Drigo, R., Capitanio, J. S., Ramachandra, R., Ellisman, M., & Hetzer, M. (2021). Identification of long-lived proteins in the mitochondria reveals increased stability of the electron transport chain. Developmental Cell. Elsevier. https://doi.org/10.1016/j.devcel.2021.10.008","ama":"Krishna S, Arrojo e Drigo R, Capitanio JS, Ramachandra R, Ellisman M, Hetzer M. Identification of long-lived proteins in the mitochondria reveals increased stability of the electron transport chain. Developmental Cell. 2021;56(21):P2952-2965.e9. doi:10.1016/j.devcel.2021.10.008","short":"S. Krishna, R. Arrojo e Drigo, J.S. Capitanio, R. Ramachandra, M. Ellisman, M. Hetzer, Developmental Cell 56 (2021) P2952–2965.e9.","ieee":"S. Krishna, R. Arrojo e Drigo, J. S. Capitanio, R. Ramachandra, M. Ellisman, and M. Hetzer, “Identification of long-lived proteins in the mitochondria reveals increased stability of the electron transport chain,” Developmental Cell, vol. 56, no. 21. Elsevier, p. P2952–2965.e9, 2021."},"user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","author":[{"first_name":"Shefali","last_name":"Krishna","full_name":"Krishna, Shefali"},{"last_name":"Arrojo e Drigo","full_name":"Arrojo e Drigo, Rafael","first_name":"Rafael"},{"last_name":"Capitanio","full_name":"Capitanio, Juliana S.","first_name":"Juliana S."},{"full_name":"Ramachandra, Ranjan","last_name":"Ramachandra","first_name":"Ranjan"},{"full_name":"Ellisman, Mark","last_name":"Ellisman","first_name":"Mark"},{"id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","first_name":"Martin W","full_name":"HETZER, Martin W","orcid":"0000-0002-2111-992X","last_name":"HETZER"}],"article_processing_charge":"No","external_id":{"pmid":["34715012"]},"title":"Identification of long-lived proteins in the mitochondria reveals increased stability of the electron transport chain","publication_identifier":{"issn":["1534-5807"]},"publication_status":"published","language":[{"iso":"eng"}],"volume":56,"issue":"21","abstract":[{"lang":"eng","text":"In order to combat molecular damage, most cellular proteins undergo rapid turnover. We have previously identified large nuclear protein assemblies that can persist for years in post-mitotic tissues and are subject to age-related decline. Here, we report that mitochondria can be long lived in the mouse brain and reveal that specific mitochondrial proteins have half-lives longer than the average proteome. These mitochondrial long-lived proteins (mitoLLPs) are core components of the electron transport chain (ETC) and display increased longevity in respiratory supercomplexes. We find that COX7C, a mitoLLP that forms a stable contact site between complexes I and IV, is required for complex IV and supercomplex assembly. Remarkably, even upon depletion of COX7C transcripts, ETC function is maintained for days, effectively uncoupling mitochondrial function from ongoing transcription of its mitoLLPs. Our results suggest that modulating protein longevity within the ETC is critical for mitochondrial proteome maintenance and the robustness of mitochondrial function."}],"oa_version":"None","pmid":1,"scopus_import":"1","month":"11","intvolume":" 56","date_updated":"2022-07-18T08:26:38Z","extern":"1","_id":"11052","type":"journal_article","article_type":"original","status":"public","keyword":["Developmental Biology","Cell Biology","General Biochemistry","Genetics and Molecular Biology","Molecular Biology"]},{"_id":"11056","status":"public","keyword":["General Biochemistry","Genetics and Molecular Biology","Biomedical Engineering","Biomaterials"],"type":"journal_article","article_type":"original","tmp":{"short":"CC BY-NC-ND (4.0)","name":"Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International (CC BY-NC-ND 4.0)","legal_code_url":"https://creativecommons.org/licenses/by-nc-nd/4.0/legalcode","image":"/images/cc_by_nc_nd.png"},"extern":"1","ddc":["570"],"date_updated":"2022-07-18T08:30:48Z","file_date_updated":"2022-04-08T07:06:05Z","oa_version":"Published Version","pmid":1,"abstract":[{"text":"Aging of the circulatory system correlates with the pathogenesis of a large spectrum of diseases. However, it is largely unknown which factors drive the age-dependent or pathological decline of the vasculature and how vascular defects relate to tissue aging. The goal of the study is to design a multianalytical approach to identify how the cellular microenvironment (i.e., fibroblasts) and serum from healthy donors of different ages or Alzheimer disease (AD) patients can modulate the functionality of organ-specific vascular endothelial cells (VECs). Long-living human microvascular networks embedding VECs and fibroblasts from skin biopsies are generated. RNA-seq, secretome analyses, and microfluidic assays demonstrate that fibroblasts from young donors restore the functionality of aged endothelial cells, an effect also achieved by serum from young donors. New biomarkers of vascular aging are validated in human biopsies and it is shown that young serum induces angiopoietin-like-4, which can restore compromised vascular barriers. This strategy is then employed to characterize transcriptional/functional changes induced on the blood–brain barrier by AD serum, demonstrating the importance of PTP4A3 in the regulation of permeability. Features of vascular degeneration during aging and AD are recapitulated, and a tool to identify novel biomarkers that can be exploited to develop future therapeutics modulating vascular function is established.","lang":"eng"}],"month":"05","intvolume":" 4","scopus_import":"1","file":[{"relation":"main_file","access_level":"open_access","content_type":"application/pdf","success":1,"checksum":"5584d9a1609812dc75c02ce1e35d2ec0","file_id":"11134","creator":"dernst","file_size":2490829,"date_updated":"2022-04-08T07:06:05Z","file_name":"2020_AdvancedBiosystems_Bersini.pdf","date_created":"2022-04-08T07:06:05Z"}],"language":[{"iso":"eng"}],"publication_identifier":{"issn":["2366-7478","2366-7478"]},"publication_status":"published","volume":4,"issue":"5","license":"https://creativecommons.org/licenses/by-nc-nd/4.0/","article_number":"2000044","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","citation":{"chicago":"Bersini, Simone, Rafael Arrojo e Drigo, Ling Huang, Maxim N. Shokhirev, and Martin Hetzer. “Transcriptional and Functional Changes of the Human Microvasculature during Physiological Aging and Alzheimer Disease.” Advanced Biosystems. Wiley, 2020. https://doi.org/10.1002/adbi.202000044.","ista":"Bersini S, Arrojo e Drigo R, Huang L, Shokhirev MN, Hetzer M. 2020. Transcriptional and functional changes of the human microvasculature during physiological aging and Alzheimer disease. Advanced Biosystems. 4(5), 2000044.","mla":"Bersini, Simone, et al. “Transcriptional and Functional Changes of the Human Microvasculature during Physiological Aging and Alzheimer Disease.” Advanced Biosystems, vol. 4, no. 5, 2000044, Wiley, 2020, doi:10.1002/adbi.202000044.","ieee":"S. Bersini, R. Arrojo e Drigo, L. Huang, M. N. Shokhirev, and M. Hetzer, “Transcriptional and functional changes of the human microvasculature during physiological aging and Alzheimer disease,” Advanced Biosystems, vol. 4, no. 5. Wiley, 2020.","short":"S. Bersini, R. Arrojo e Drigo, L. Huang, M.N. Shokhirev, M. Hetzer, Advanced Biosystems 4 (2020).","ama":"Bersini S, Arrojo e Drigo R, Huang L, Shokhirev MN, Hetzer M. Transcriptional and functional changes of the human microvasculature during physiological aging and Alzheimer disease. Advanced Biosystems. 2020;4(5). doi:10.1002/adbi.202000044","apa":"Bersini, S., Arrojo e Drigo, R., Huang, L., Shokhirev, M. N., & Hetzer, M. (2020). Transcriptional and functional changes of the human microvasculature during physiological aging and Alzheimer disease. Advanced Biosystems. Wiley. https://doi.org/10.1002/adbi.202000044"},"title":"Transcriptional and functional changes of the human microvasculature during physiological aging and Alzheimer disease","author":[{"full_name":"Bersini, Simone","last_name":"Bersini","first_name":"Simone"},{"full_name":"Arrojo e Drigo, Rafael","last_name":"Arrojo e Drigo","first_name":"Rafael"},{"full_name":"Huang, Ling","last_name":"Huang","first_name":"Ling"},{"first_name":"Maxim N.","full_name":"Shokhirev, Maxim N.","last_name":"Shokhirev"},{"full_name":"HETZER, Martin W","orcid":"0000-0002-2111-992X","last_name":"HETZER","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","first_name":"Martin W"}],"article_processing_charge":"No","external_id":{"pmid":["32402127"]},"publisher":"Wiley","quality_controlled":"1","oa":1,"day":"01","publication":"Advanced Biosystems","has_accepted_license":"1","year":"2020","date_published":"2020-05-01T00:00:00Z","doi":"10.1002/adbi.202000044","date_created":"2022-04-07T07:43:57Z"},{"intvolume":" 9","month":"09","scopus_import":"1","pmid":1,"oa_version":"Published Version","abstract":[{"text":"Vascular dysfunctions are a common feature of multiple age-related diseases. However, modeling healthy and pathological aging of the human vasculature represents an unresolved experimental challenge. Here, we generated induced vascular endothelial cells (iVECs) and smooth muscle cells (iSMCs) by direct reprogramming of healthy human fibroblasts from donors of different ages and Hutchinson-Gilford Progeria Syndrome (HGPS) patients. iVECs induced from old donors revealed upregulation of GSTM1 and PALD1, genes linked to oxidative stress, inflammation and endothelial junction stability, as vascular aging markers. A functional assay performed on PALD1 KD VECs demonstrated a recovery in vascular permeability. We found that iSMCs from HGPS donors overexpressed bone morphogenetic protein (BMP)−4, which plays a key role in both vascular calcification and endothelial barrier damage observed in HGPS. Strikingly, BMP4 concentrations are higher in serum from HGPS vs. age-matched mice. Furthermore, targeting BMP4 with blocking antibody recovered the functionality of the vascular barrier in vitro, hence representing a potential future therapeutic strategy to limit cardiovascular dysfunction in HGPS. These results show that iVECs and iSMCs retain disease-related signatures, allowing modeling of vascular aging and HGPS in vitro.","lang":"eng"}],"volume":9,"language":[{"iso":"eng"}],"file":[{"date_created":"2022-04-08T06:53:10Z","file_name":"2020_eLife_Bersini.pdf","date_updated":"2022-04-08T06:53:10Z","file_size":4399825,"creator":"dernst","checksum":"f8b3821349a194050be02570d8fe7d4b","file_id":"11132","success":1,"content_type":"application/pdf","access_level":"open_access","relation":"main_file"}],"publication_status":"published","publication_identifier":{"issn":["2050-084X"]},"keyword":["General Immunology and Microbiology","General Biochemistry","Genetics and Molecular Biology","General Medicine","General Neuroscience"],"status":"public","tmp":{"legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","image":"/images/cc_by.png","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","short":"CC BY (4.0)"},"article_type":"original","type":"journal_article","_id":"11055","file_date_updated":"2022-04-08T06:53:10Z","ddc":["570"],"extern":"1","date_updated":"2022-07-18T08:30:37Z","oa":1,"publisher":"eLife Sciences Publications","quality_controlled":"1","date_created":"2022-04-07T07:43:48Z","doi":"10.7554/elife.54383","date_published":"2020-09-08T00:00:00Z","publication":"eLife","day":"08","year":"2020","has_accepted_license":"1","article_number":"e54383","title":"Direct reprogramming of human smooth muscle and vascular endothelial cells reveals defects associated with aging and Hutchinson-Gilford progeria syndrome","external_id":{"pmid":["32896271"]},"article_processing_charge":"No","author":[{"full_name":"Bersini, Simone","last_name":"Bersini","first_name":"Simone"},{"first_name":"Roberta","last_name":"Schulte","full_name":"Schulte, Roberta"},{"first_name":"Ling","last_name":"Huang","full_name":"Huang, Ling"},{"first_name":"Hannah","full_name":"Tsai, Hannah","last_name":"Tsai"},{"id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","first_name":"Martin W","orcid":"0000-0002-2111-992X","full_name":"HETZER, Martin W","last_name":"HETZER"}],"user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","citation":{"short":"S. Bersini, R. Schulte, L. Huang, H. Tsai, M. Hetzer, ELife 9 (2020).","ieee":"S. Bersini, R. Schulte, L. Huang, H. Tsai, and M. Hetzer, “Direct reprogramming of human smooth muscle and vascular endothelial cells reveals defects associated with aging and Hutchinson-Gilford progeria syndrome,” eLife, vol. 9. eLife Sciences Publications, 2020.","ama":"Bersini S, Schulte R, Huang L, Tsai H, Hetzer M. Direct reprogramming of human smooth muscle and vascular endothelial cells reveals defects associated with aging and Hutchinson-Gilford progeria syndrome. eLife. 2020;9. doi:10.7554/elife.54383","apa":"Bersini, S., Schulte, R., Huang, L., Tsai, H., & Hetzer, M. (2020). Direct reprogramming of human smooth muscle and vascular endothelial cells reveals defects associated with aging and Hutchinson-Gilford progeria syndrome. ELife. eLife Sciences Publications. https://doi.org/10.7554/elife.54383","mla":"Bersini, Simone, et al. “Direct Reprogramming of Human Smooth Muscle and Vascular Endothelial Cells Reveals Defects Associated with Aging and Hutchinson-Gilford Progeria Syndrome.” ELife, vol. 9, e54383, eLife Sciences Publications, 2020, doi:10.7554/elife.54383.","ista":"Bersini S, Schulte R, Huang L, Tsai H, Hetzer M. 2020. Direct reprogramming of human smooth muscle and vascular endothelial cells reveals defects associated with aging and Hutchinson-Gilford progeria syndrome. eLife. 9, e54383.","chicago":"Bersini, Simone, Roberta Schulte, Ling Huang, Hannah Tsai, and Martin Hetzer. “Direct Reprogramming of Human Smooth Muscle and Vascular Endothelial Cells Reveals Defects Associated with Aging and Hutchinson-Gilford Progeria Syndrome.” ELife. eLife Sciences Publications, 2020. https://doi.org/10.7554/elife.54383."}},{"abstract":[{"text":"In recent years, the nuclear pore complex (NPC) has emerged as a key player in genome regulation and cellular homeostasis. New discoveries have revealed that the NPC has multiple cellular functions besides mediating the molecular exchange between the nucleus and the cytoplasm. In this review, we discuss non-transport aspects of the NPC focusing on the NPC-genome interaction, the extreme longevity of the NPC proteins, and NPC dysfunction in age-related diseases. The examples summarized herein demonstrate that the NPC, which first evolved to enable the biochemical communication between the nucleus and the cytoplasm, now doubles as the gatekeeper of cellular identity and aging.","lang":"eng"}],"oa_version":"Published Version","pmid":1,"scopus_import":"1","main_file_link":[{"open_access":"1","url":"https://doi.org/10.1016/j.neuron.2020.05.031"}],"month":"06","intvolume":" 106","publication_identifier":{"issn":["0896-6273"]},"publication_status":"published","language":[{"iso":"eng"}],"issue":"6","volume":106,"_id":"11054","type":"journal_article","article_type":"review","status":"public","keyword":["General Neuroscience"],"date_updated":"2022-07-18T08:29:35Z","extern":"1","publisher":"Elsevier","quality_controlled":"1","oa":1,"year":"2020","day":"17","publication":"Neuron","page":"899-911","doi":"10.1016/j.neuron.2020.05.031","date_published":"2020-06-17T00:00:00Z","date_created":"2022-04-07T07:43:36Z","citation":{"chicago":"Cho, Ukrae H., and Martin Hetzer. “Nuclear Periphery Takes Center Stage: The Role of Nuclear Pore Complexes in Cell Identity and Aging.” Neuron. Elsevier, 2020. https://doi.org/10.1016/j.neuron.2020.05.031.","ista":"Cho UH, Hetzer M. 2020. Nuclear periphery takes center stage: The role of nuclear pore complexes in cell identity and aging. Neuron. 106(6), 899–911.","mla":"Cho, Ukrae H., and Martin Hetzer. “Nuclear Periphery Takes Center Stage: The Role of Nuclear Pore Complexes in Cell Identity and Aging.” Neuron, vol. 106, no. 6, Elsevier, 2020, pp. 899–911, doi:10.1016/j.neuron.2020.05.031.","ama":"Cho UH, Hetzer M. Nuclear periphery takes center stage: The role of nuclear pore complexes in cell identity and aging. Neuron. 2020;106(6):899-911. doi:10.1016/j.neuron.2020.05.031","apa":"Cho, U. H., & Hetzer, M. (2020). Nuclear periphery takes center stage: The role of nuclear pore complexes in cell identity and aging. Neuron. Elsevier. https://doi.org/10.1016/j.neuron.2020.05.031","ieee":"U. H. Cho and M. Hetzer, “Nuclear periphery takes center stage: The role of nuclear pore complexes in cell identity and aging,” Neuron, vol. 106, no. 6. Elsevier, pp. 899–911, 2020.","short":"U.H. Cho, M. Hetzer, Neuron 106 (2020) 899–911."},"user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","author":[{"first_name":"Ukrae H.","last_name":"Cho","full_name":"Cho, Ukrae H."},{"first_name":"Martin W","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","last_name":"HETZER","orcid":"0000-0002-2111-992X","full_name":"HETZER, Martin W"}],"article_processing_charge":"No","external_id":{"pmid":["32553207"]},"title":"Nuclear periphery takes center stage: The role of nuclear pore complexes in cell identity and aging"},{"author":[{"full_name":"Kang, Hyeseon","last_name":"Kang","first_name":"Hyeseon"},{"first_name":"Maxim N.","full_name":"Shokhirev, Maxim N.","last_name":"Shokhirev"},{"full_name":"Xu, Zhichao","last_name":"Xu","first_name":"Zhichao"},{"full_name":"Chandran, Sahaana","last_name":"Chandran","first_name":"Sahaana"},{"full_name":"Dixon, Jesse R.","last_name":"Dixon","first_name":"Jesse R."},{"full_name":"HETZER, Martin W","orcid":"0000-0002-2111-992X","last_name":"HETZER","first_name":"Martin W","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed"}],"external_id":{"pmid":["32499403"]},"article_processing_charge":"No","title":"Dynamic regulation of histone modifications and long-range chromosomal interactions during postmitotic transcriptional reactivation","citation":{"mla":"Kang, Hyeseon, et al. “Dynamic Regulation of Histone Modifications and Long-Range Chromosomal Interactions during Postmitotic Transcriptional Reactivation.” Genes & Development, vol. 34, no. 13–14, Cold Spring Harbor Laboratory Press, 2020, pp. 913–30, doi:10.1101/gad.335794.119.","ama":"Kang H, Shokhirev MN, Xu Z, Chandran S, Dixon JR, Hetzer M. Dynamic regulation of histone modifications and long-range chromosomal interactions during postmitotic transcriptional reactivation. Genes & Development. 2020;34(13-14):913-930. doi:10.1101/gad.335794.119","apa":"Kang, H., Shokhirev, M. N., Xu, Z., Chandran, S., Dixon, J. R., & Hetzer, M. (2020). Dynamic regulation of histone modifications and long-range chromosomal interactions during postmitotic transcriptional reactivation. Genes & Development. Cold Spring Harbor Laboratory Press. https://doi.org/10.1101/gad.335794.119","ieee":"H. Kang, M. N. Shokhirev, Z. Xu, S. Chandran, J. R. Dixon, and M. Hetzer, “Dynamic regulation of histone modifications and long-range chromosomal interactions during postmitotic transcriptional reactivation,” Genes & Development, vol. 34, no. 13–14. Cold Spring Harbor Laboratory Press, pp. 913–930, 2020.","short":"H. Kang, M.N. Shokhirev, Z. Xu, S. Chandran, J.R. Dixon, M. Hetzer, Genes & Development 34 (2020) 913–930.","chicago":"Kang, Hyeseon, Maxim N. Shokhirev, Zhichao Xu, Sahaana Chandran, Jesse R. Dixon, and Martin Hetzer. “Dynamic Regulation of Histone Modifications and Long-Range Chromosomal Interactions during Postmitotic Transcriptional Reactivation.” Genes & Development. Cold Spring Harbor Laboratory Press, 2020. https://doi.org/10.1101/gad.335794.119.","ista":"Kang H, Shokhirev MN, Xu Z, Chandran S, Dixon JR, Hetzer M. 2020. Dynamic regulation of histone modifications and long-range chromosomal interactions during postmitotic transcriptional reactivation. Genes & Development. 34(13–14), 913–930."},"user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","page":"913-930","date_published":"2020-04-28T00:00:00Z","doi":"10.1101/gad.335794.119","date_created":"2022-04-07T07:44:09Z","has_accepted_license":"1","year":"2020","day":"28","publication":"Genes & Development","quality_controlled":"1","publisher":"Cold Spring Harbor Laboratory Press","oa":1,"file_date_updated":"2022-04-08T07:12:33Z","date_updated":"2022-07-18T08:31:08Z","extern":"1","ddc":["570"],"article_type":"original","type":"journal_article","tmp":{"legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","image":"/images/cc_by.png","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","short":"CC BY (4.0)"},"status":"public","keyword":["Developmental Biology","Genetics"],"_id":"11057","volume":34,"issue":"13-14","publication_identifier":{"issn":["0890-9369","1549-5477"]},"publication_status":"published","file":[{"date_updated":"2022-04-08T07:12:33Z","file_size":4406772,"creator":"dernst","date_created":"2022-04-08T07:12:33Z","file_name":"2020_GenesDevelopment_Kang.pdf","content_type":"application/pdf","access_level":"open_access","relation":"main_file","checksum":"84e92d40e67936c739628315c238daf9","file_id":"11136","success":1}],"language":[{"iso":"eng"}],"scopus_import":"1","month":"04","intvolume":" 34","abstract":[{"lang":"eng","text":"During mitosis, transcription of genomic DNA is dramatically reduced, before it is reactivated during nuclear reformation in anaphase/telophase. Many aspects of the underlying principles that mediate transcriptional memory and reactivation in the daughter cells remain unclear. Here, we used ChIP-seq on synchronized cells at different stages after mitosis to generate genome-wide maps of histone modifications. Combined with EU-RNA-seq and Hi-C analyses, we found that during prometaphase, promoters, enhancers, and insulators retain H3K4me3 and H3K4me1, while losing H3K27ac. Enhancers globally retaining mitotic H3K4me1 or locally retaining mitotic H3K27ac are associated with cell type-specific genes and their transcription factors for rapid transcriptional activation. As cells exit mitosis, promoters regain H3K27ac, which correlates with transcriptional reactivation. Insulators also gain H3K27ac and CCCTC-binding factor (CTCF) in anaphase/telophase. This increase of H3K27ac in anaphase/telophase is required for posttranscriptional activation and may play a role in the establishment of topologically associating domains (TADs). Together, our results suggest that the genome is reorganized in a sequential order, in which histone methylations occur first in prometaphase, histone acetylation, and CTCF in anaphase/telophase, transcription in cytokinesis, and long-range chromatin interactions in early G1. We thus provide insights into the histone modification landscape that allows faithful reestablishment of the transcriptional program and TADs during cell division."}],"oa_version":"Published Version","pmid":1},{"file_date_updated":"2022-04-08T07:33:01Z","date_updated":"2022-07-18T08:31:20Z","extern":"1","ddc":["570"],"article_type":"original","type":"journal_article","tmp":{"legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","image":"/images/cc_by.png","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","short":"CC BY (4.0)"},"status":"public","keyword":["Health","Toxicology and Mutagenesis","Plant Science","Biochemistry","Genetics and Molecular Biology (miscellaneous)","Ecology"],"_id":"11058","volume":3,"issue":"1","publication_identifier":{"issn":["2575-1077"]},"publication_status":"published","file":[{"access_level":"open_access","relation":"main_file","content_type":"application/pdf","checksum":"3bf33e7e93bef7823287807206b69b38","file_id":"11137","success":1,"creator":"dernst","date_updated":"2022-04-08T07:33:01Z","file_size":2653960,"date_created":"2022-04-08T07:33:01Z","file_name":"2020_LifeScienceAlliance_Bersini.pdf"}],"language":[{"iso":"eng"}],"scopus_import":"1","month":"01","intvolume":" 3","abstract":[{"lang":"eng","text":"Nucleoporin 93 (Nup93) expression inversely correlates with the survival of triple-negative breast cancer patients. However, our knowledge of Nup93 function in breast cancer besides its role as structural component of the nuclear pore complex is not understood. Combination of functional assays and genetic analyses suggested that chromatin interaction of Nup93 partially modulates the expression of genes associated with actin cytoskeleton remodeling and epithelial to mesenchymal transition, resulting in impaired invasion of triple-negative, claudin-low breast cancer cells. Nup93 depletion induced stress fiber formation associated with reduced cell migration/proliferation and impaired expression of mesenchymal-like genes. Silencing LIMCH1, a gene responsible for actin cytoskeleton remodeling and up-regulated upon Nup93 depletion, partially restored the invasive phenotype of cancer cells. Loss of Nup93 led to significant defects in tumor establishment/propagation in vivo, whereas patient samples revealed that high Nup93 and low LIMCH1 expression correlate with late tumor stage. Our approach identified Nup93 as contributor of triple-negative, claudin-low breast cancer cell invasion and paves the way to study the role of nuclear envelope proteins during breast cancer tumorigenesis."}],"oa_version":"Published Version","pmid":1,"author":[{"full_name":"Bersini, Simone","last_name":"Bersini","first_name":"Simone"},{"last_name":"Lytle","full_name":"Lytle, Nikki K","first_name":"Nikki K"},{"last_name":"Schulte","full_name":"Schulte, Roberta","first_name":"Roberta"},{"first_name":"Ling","last_name":"Huang","full_name":"Huang, Ling"},{"last_name":"Wahl","full_name":"Wahl, Geoffrey M","first_name":"Geoffrey M"},{"first_name":"Martin W","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","full_name":"HETZER, Martin W","orcid":"0000-0002-2111-992X","last_name":"HETZER"}],"article_processing_charge":"No","external_id":{"pmid":["31959624"]},"title":"Nup93 regulates breast tumor growth by modulating cell proliferation and actin cytoskeleton remodeling","citation":{"mla":"Bersini, Simone, et al. “Nup93 Regulates Breast Tumor Growth by Modulating Cell Proliferation and Actin Cytoskeleton Remodeling.” Life Science Alliance, vol. 3, no. 1, e201900623, Life Science Alliance, 2020, doi:10.26508/lsa.201900623.","ama":"Bersini S, Lytle NK, Schulte R, Huang L, Wahl GM, Hetzer M. Nup93 regulates breast tumor growth by modulating cell proliferation and actin cytoskeleton remodeling. Life Science Alliance. 2020;3(1). doi:10.26508/lsa.201900623","apa":"Bersini, S., Lytle, N. K., Schulte, R., Huang, L., Wahl, G. M., & Hetzer, M. (2020). Nup93 regulates breast tumor growth by modulating cell proliferation and actin cytoskeleton remodeling. Life Science Alliance. Life Science Alliance. https://doi.org/10.26508/lsa.201900623","short":"S. Bersini, N.K. Lytle, R. Schulte, L. Huang, G.M. Wahl, M. Hetzer, Life Science Alliance 3 (2020).","ieee":"S. Bersini, N. K. Lytle, R. Schulte, L. Huang, G. M. Wahl, and M. Hetzer, “Nup93 regulates breast tumor growth by modulating cell proliferation and actin cytoskeleton remodeling,” Life Science Alliance, vol. 3, no. 1. Life Science Alliance, 2020.","chicago":"Bersini, Simone, Nikki K Lytle, Roberta Schulte, Ling Huang, Geoffrey M Wahl, and Martin Hetzer. “Nup93 Regulates Breast Tumor Growth by Modulating Cell Proliferation and Actin Cytoskeleton Remodeling.” Life Science Alliance. Life Science Alliance, 2020. https://doi.org/10.26508/lsa.201900623.","ista":"Bersini S, Lytle NK, Schulte R, Huang L, Wahl GM, Hetzer M. 2020. Nup93 regulates breast tumor growth by modulating cell proliferation and actin cytoskeleton remodeling. Life Science Alliance. 3(1), e201900623."},"user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","article_number":"e201900623","date_published":"2020-01-01T00:00:00Z","doi":"10.26508/lsa.201900623","date_created":"2022-04-07T07:44:18Z","has_accepted_license":"1","year":"2020","day":"01","publication":"Life Science Alliance","quality_controlled":"1","publisher":"Life Science Alliance","oa":1},{"scopus_import":"1","month":"02","intvolume":" 218","abstract":[{"text":"Many adult tissues contain postmitotic cells as old as the host organism. The only organelle that does not turn over in these cells is the nucleus, and its maintenance represents a formidable challenge, as it harbors regulatory proteins that persist throughout adulthood. Here we developed strategies to visualize two classes of such long-lived proteins, histones and nucleoporins, to understand the function of protein longevity in nuclear maintenance. Genome-wide mapping of histones revealed specific enrichment of long-lived variants at silent gene loci. Interestingly, nuclear pores are maintained by piecemeal replacement of subunits, resulting in mosaic complexes composed of polypeptides with vastly different ages. In contrast, nondividing quiescent cells remove old nuclear pores in an ESCRT-dependent manner. Our findings reveal distinct molecular strategies of nuclear maintenance, linking lifelong protein persistence to gene regulation and nuclear integrity.","lang":"eng"}],"oa_version":"Published Version","pmid":1,"issue":"2","volume":218,"license":"https://creativecommons.org/licenses/by-nc-sa/4.0/","publication_identifier":{"eissn":["1540-8140"],"issn":["0021-9525"]},"publication_status":"published","file":[{"content_type":"application/pdf","relation":"main_file","access_level":"open_access","success":1,"checksum":"7964ebbf833b0b35f9fba840eea9531d","file_id":"11139","file_size":2503838,"date_updated":"2022-04-08T08:26:32Z","creator":"dernst","file_name":"2019_JCB_Toyama.pdf","date_created":"2022-04-08T08:26:32Z"}],"language":[{"iso":"eng"}],"type":"journal_article","article_type":"original","tmp":{"name":"Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)","image":"/images/cc_by_nc_sa.png","legal_code_url":"https://creativecommons.org/licenses/by-nc-sa/4.0/legalcode","short":"CC BY-NC-SA (4.0)"},"status":"public","keyword":["Cell Biology"],"_id":"11061","file_date_updated":"2022-04-08T08:26:32Z","date_updated":"2022-07-18T08:31:52Z","extern":"1","ddc":["570"],"publisher":"Rockefeller University Press","quality_controlled":"1","oa":1,"page":"433-444","doi":"10.1083/jcb.201809123","date_published":"2019-02-04T00:00:00Z","date_created":"2022-04-07T07:45:11Z","has_accepted_license":"1","year":"2019","day":"04","publication":"Journal of Cell Biology","author":[{"first_name":"Brandon H.","last_name":"Toyama","full_name":"Toyama, Brandon H."},{"full_name":"Arrojo e Drigo, Rafael","last_name":"Arrojo e Drigo","first_name":"Rafael"},{"first_name":"Varda","last_name":"Lev-Ram","full_name":"Lev-Ram, Varda"},{"first_name":"Ranjan","last_name":"Ramachandra","full_name":"Ramachandra, Ranjan"},{"first_name":"Thomas J.","full_name":"Deerinck, Thomas J.","last_name":"Deerinck"},{"last_name":"Lechene","full_name":"Lechene, Claude","first_name":"Claude"},{"full_name":"Ellisman, Mark H.","last_name":"Ellisman","first_name":"Mark H."},{"full_name":"HETZER, Martin W","orcid":"0000-0002-2111-992X","last_name":"HETZER","first_name":"Martin W","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed"}],"external_id":{"pmid":["30552100"]},"article_processing_charge":"No","title":"Visualization of long-lived proteins reveals age mosaicism within nuclei of postmitotic cells","citation":{"mla":"Toyama, Brandon H., et al. “Visualization of Long-Lived Proteins Reveals Age Mosaicism within Nuclei of Postmitotic Cells.” Journal of Cell Biology, vol. 218, no. 2, Rockefeller University Press, 2019, pp. 433–44, doi:10.1083/jcb.201809123.","ieee":"B. H. Toyama et al., “Visualization of long-lived proteins reveals age mosaicism within nuclei of postmitotic cells,” Journal of Cell Biology, vol. 218, no. 2. Rockefeller University Press, pp. 433–444, 2019.","short":"B.H. Toyama, R. Arrojo e Drigo, V. Lev-Ram, R. Ramachandra, T.J. Deerinck, C. Lechene, M.H. Ellisman, M. Hetzer, Journal of Cell Biology 218 (2019) 433–444.","ama":"Toyama BH, Arrojo e Drigo R, Lev-Ram V, et al. Visualization of long-lived proteins reveals age mosaicism within nuclei of postmitotic cells. Journal of Cell Biology. 2019;218(2):433-444. doi:10.1083/jcb.201809123","apa":"Toyama, B. H., Arrojo e Drigo, R., Lev-Ram, V., Ramachandra, R., Deerinck, T. J., Lechene, C., … Hetzer, M. (2019). Visualization of long-lived proteins reveals age mosaicism within nuclei of postmitotic cells. Journal of Cell Biology. Rockefeller University Press. https://doi.org/10.1083/jcb.201809123","chicago":"Toyama, Brandon H., Rafael Arrojo e Drigo, Varda Lev-Ram, Ranjan Ramachandra, Thomas J. Deerinck, Claude Lechene, Mark H. Ellisman, and Martin Hetzer. “Visualization of Long-Lived Proteins Reveals Age Mosaicism within Nuclei of Postmitotic Cells.” Journal of Cell Biology. Rockefeller University Press, 2019. https://doi.org/10.1083/jcb.201809123.","ista":"Toyama BH, Arrojo e Drigo R, Lev-Ram V, Ramachandra R, Deerinck TJ, Lechene C, Ellisman MH, Hetzer M. 2019. Visualization of long-lived proteins reveals age mosaicism within nuclei of postmitotic cells. Journal of Cell Biology. 218(2), 433–444."},"user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd"},{"page":"343-351.e3","date_created":"2022-04-07T07:45:21Z","doi":"10.1016/j.cmet.2019.05.010","date_published":"2019-08-06T00:00:00Z","year":"2019","publication":"Cell Metabolism","day":"06","oa":1,"publisher":"Elsevier","quality_controlled":"1","external_id":{"pmid":["31178361"]},"article_processing_charge":"No","author":[{"last_name":"Arrojo e Drigo","full_name":"Arrojo e Drigo, Rafael","first_name":"Rafael"},{"last_name":"Lev-Ram","full_name":"Lev-Ram, Varda","first_name":"Varda"},{"full_name":"Tyagi, Swati","last_name":"Tyagi","first_name":"Swati"},{"first_name":"Ranjan","full_name":"Ramachandra, Ranjan","last_name":"Ramachandra"},{"first_name":"Thomas","full_name":"Deerinck, Thomas","last_name":"Deerinck"},{"first_name":"Eric","last_name":"Bushong","full_name":"Bushong, Eric"},{"first_name":"Sebastien","last_name":"Phan","full_name":"Phan, Sebastien"},{"last_name":"Orphan","full_name":"Orphan, Victoria","first_name":"Victoria"},{"first_name":"Claude","last_name":"Lechene","full_name":"Lechene, Claude"},{"last_name":"Ellisman","full_name":"Ellisman, Mark H.","first_name":"Mark H."},{"id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","first_name":"Martin W","full_name":"HETZER, Martin W","orcid":"0000-0002-2111-992X","last_name":"HETZER"}],"title":"Age mosaicism across multiple scales in adult tissues","citation":{"chicago":"Arrojo e Drigo, Rafael, Varda Lev-Ram, Swati Tyagi, Ranjan Ramachandra, Thomas Deerinck, Eric Bushong, Sebastien Phan, et al. “Age Mosaicism across Multiple Scales in Adult Tissues.” Cell Metabolism. Elsevier, 2019. https://doi.org/10.1016/j.cmet.2019.05.010.","ista":"Arrojo e Drigo R, Lev-Ram V, Tyagi S, Ramachandra R, Deerinck T, Bushong E, Phan S, Orphan V, Lechene C, Ellisman MH, Hetzer M. 2019. Age mosaicism across multiple scales in adult tissues. Cell Metabolism. 30(2), 343–351.e3.","mla":"Arrojo e Drigo, Rafael, et al. “Age Mosaicism across Multiple Scales in Adult Tissues.” Cell Metabolism, vol. 30, no. 2, Elsevier, 2019, p. 343–351.e3, doi:10.1016/j.cmet.2019.05.010.","short":"R. Arrojo e Drigo, V. Lev-Ram, S. Tyagi, R. Ramachandra, T. Deerinck, E. Bushong, S. Phan, V. Orphan, C. Lechene, M.H. Ellisman, M. Hetzer, Cell Metabolism 30 (2019) 343–351.e3.","ieee":"R. Arrojo e Drigo et al., “Age mosaicism across multiple scales in adult tissues,” Cell Metabolism, vol. 30, no. 2. Elsevier, p. 343–351.e3, 2019.","ama":"Arrojo e Drigo R, Lev-Ram V, Tyagi S, et al. Age mosaicism across multiple scales in adult tissues. Cell Metabolism. 2019;30(2):343-351.e3. doi:10.1016/j.cmet.2019.05.010","apa":"Arrojo e Drigo, R., Lev-Ram, V., Tyagi, S., Ramachandra, R., Deerinck, T., Bushong, E., … Hetzer, M. (2019). Age mosaicism across multiple scales in adult tissues. Cell Metabolism. Elsevier. https://doi.org/10.1016/j.cmet.2019.05.010"},"user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","volume":30,"issue":"2","publication_status":"published","publication_identifier":{"issn":["1550-4131"]},"language":[{"iso":"eng"}],"main_file_link":[{"url":"https://doi.org/10.1016/j.cmet.2019.05.010","open_access":"1"}],"scopus_import":"1","intvolume":" 30","month":"08","abstract":[{"text":"Most neurons are not replaced during an animal’s lifetime. This nondividing state is characterized by extreme longevity and age-dependent decline of key regulatory proteins. To study the lifespans of cells and proteins in adult tissues, we combined isotope labeling of mice with a hybrid imaging method (MIMS-EM). Using 15N mapping, we show that liver and pancreas are composed of cells with vastly different ages, many as old as the animal. Strikingly, we also found that a subset of fibroblasts and endothelial cells, both known for their replicative potential, are characterized by the absence of cell division during adulthood. In addition, we show that the primary cilia of beta cells and neurons contains different structural regions with vastly different lifespans. Based on these results, we propose that age mosaicism across multiple scales is a fundamental principle of adult tissue, cell, and protein complex organization.","lang":"eng"}],"pmid":1,"oa_version":"Published Version","date_updated":"2022-07-18T08:32:30Z","extern":"1","article_type":"original","type":"journal_article","keyword":["Cell Biology","Molecular Biology","Physiology"],"status":"public","_id":"11062"},{"year":"2019","publication":"Nature Reviews Genetics","day":"01","page":"39-50","date_created":"2022-04-07T07:44:45Z","date_published":"2019-01-01T00:00:00Z","doi":"10.1038/s41576-018-0063-5","quality_controlled":"1","publisher":"Springer Nature","citation":{"ista":"Buchwalter A, Kaneshiro JM, Hetzer M. 2019. Coaching from the sidelines: The nuclear periphery in genome regulation. Nature Reviews Genetics. 20(1), 39–50.","chicago":"Buchwalter, Abigail, Jeanae M. Kaneshiro, and Martin Hetzer. “Coaching from the Sidelines: The Nuclear Periphery in Genome Regulation.” Nature Reviews Genetics. Springer Nature, 2019. https://doi.org/10.1038/s41576-018-0063-5.","apa":"Buchwalter, A., Kaneshiro, J. M., & Hetzer, M. (2019). Coaching from the sidelines: The nuclear periphery in genome regulation. Nature Reviews Genetics. Springer Nature. https://doi.org/10.1038/s41576-018-0063-5","ama":"Buchwalter A, Kaneshiro JM, Hetzer M. Coaching from the sidelines: The nuclear periphery in genome regulation. Nature Reviews Genetics. 2019;20(1):39-50. doi:10.1038/s41576-018-0063-5","ieee":"A. Buchwalter, J. M. Kaneshiro, and M. Hetzer, “Coaching from the sidelines: The nuclear periphery in genome regulation,” Nature Reviews Genetics, vol. 20, no. 1. Springer Nature, pp. 39–50, 2019.","short":"A. Buchwalter, J.M. Kaneshiro, M. Hetzer, Nature Reviews Genetics 20 (2019) 39–50.","mla":"Buchwalter, Abigail, et al. “Coaching from the Sidelines: The Nuclear Periphery in Genome Regulation.” Nature Reviews Genetics, vol. 20, no. 1, Springer Nature, 2019, pp. 39–50, doi:10.1038/s41576-018-0063-5."},"user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","external_id":{"pmid":["30356165"]},"article_processing_charge":"No","author":[{"first_name":"Abigail","full_name":"Buchwalter, Abigail","last_name":"Buchwalter"},{"first_name":"Jeanae M.","full_name":"Kaneshiro, Jeanae M.","last_name":"Kaneshiro"},{"last_name":"HETZER","full_name":"HETZER, Martin W","orcid":"0000-0002-2111-992X","first_name":"Martin W","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed"}],"title":"Coaching from the sidelines: The nuclear periphery in genome regulation","publication_status":"published","publication_identifier":{"issn":["1471-0056"],"eissn":["1471-0064"]},"language":[{"iso":"eng"}],"issue":"1","volume":20,"abstract":[{"lang":"eng","text":"The genome is packaged and organized nonrandomly within the 3D space of the nucleus to promote efficient gene expression and to faithfully maintain silencing of heterochromatin. The genome is enclosed within the nucleus by the nuclear envelope membrane, which contains a set of proteins that actively participate in chromatin organization and gene regulation. Technological advances are providing views of genome organization at unprecedented resolution and are beginning to reveal the ways that cells co-opt the structures of the nuclear periphery for nuclear organization and gene regulation. These genome regulatory roles of proteins of the nuclear periphery have important influences on development, disease and ageing."}],"oa_version":"None","pmid":1,"scopus_import":"1","intvolume":" 20","month":"01","date_updated":"2022-07-18T08:31:42Z","extern":"1","_id":"11059","article_type":"review","type":"journal_article","keyword":["Genetics (clinical)","Genetics","Molecular Biology"],"status":"public"},{"tmp":{"legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","image":"/images/cc_by.png","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","short":"CC BY (4.0)"},"type":"journal_article","article_type":"original","keyword":["General Immunology and Microbiology","General Biochemistry","Genetics and Molecular Biology","General Medicine","General Neuroscience"],"status":"public","_id":"11060","file_date_updated":"2022-04-08T08:18:01Z","date_updated":"2023-05-31T06:36:22Z","ddc":["570"],"extern":"1","scopus_import":"1","intvolume":" 8","month":"10","abstract":[{"lang":"eng","text":"The inner nuclear membrane (INM) is a subdomain of the endoplasmic reticulum (ER) that is gated by the nuclear pore complex. It is unknown whether proteins of the INM and ER are degraded through shared or distinct pathways in mammalian cells. We applied dynamic proteomics to profile protein half-lives and report that INM and ER residents turn over at similar rates, indicating that the INM’s unique topology is not a barrier to turnover. Using a microscopy approach, we observed that the proteasome can degrade INM proteins in situ. However, we also uncovered evidence for selective, vesicular transport-mediated turnover of a single INM protein, emerin, that is potentiated by ER stress. Emerin is rapidly cleared from the INM by a mechanism that requires emerin’s LEM domain to mediate vesicular trafficking to lysosomes. This work demonstrates that the INM can be dynamically remodeled in response to environmental inputs."}],"oa_version":"Published Version","pmid":1,"volume":8,"related_material":{"record":[{"relation":"research_data","id":"13079","status":"public"}]},"publication_status":"published","publication_identifier":{"issn":["2050-084X"]},"language":[{"iso":"eng"}],"file":[{"file_name":"2019_eLife_Buchwalter.pdf","date_created":"2022-04-08T08:18:01Z","file_size":6984654,"date_updated":"2022-04-08T08:18:01Z","creator":"dernst","success":1,"file_id":"11138","checksum":"1e8672a1e9c3dc0a2d3d0dad89673616","content_type":"application/pdf","relation":"main_file","access_level":"open_access"}],"article_number":"e49796","external_id":{"pmid":["31599721"]},"article_processing_charge":"No","author":[{"full_name":"Buchwalter, Abigail","last_name":"Buchwalter","first_name":"Abigail"},{"first_name":"Roberta","last_name":"Schulte","full_name":"Schulte, Roberta"},{"full_name":"Tsai, Hsiao","last_name":"Tsai","first_name":"Hsiao"},{"last_name":"Capitanio","full_name":"Capitanio, Juliana","first_name":"Juliana"},{"orcid":"0000-0002-2111-992X","full_name":"HETZER, Martin W","last_name":"HETZER","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","first_name":"Martin W"}],"title":"Selective clearance of the inner nuclear membrane protein emerin by vesicular transport during ER stress","citation":{"ista":"Buchwalter A, Schulte R, Tsai H, Capitanio J, Hetzer M. 2019. Selective clearance of the inner nuclear membrane protein emerin by vesicular transport during ER stress. eLife. 8, e49796.","chicago":"Buchwalter, Abigail, Roberta Schulte, Hsiao Tsai, Juliana Capitanio, and Martin Hetzer. “Selective Clearance of the Inner Nuclear Membrane Protein Emerin by Vesicular Transport during ER Stress.” ELife. eLife Sciences Publications, 2019. https://doi.org/10.7554/elife.49796.","apa":"Buchwalter, A., Schulte, R., Tsai, H., Capitanio, J., & Hetzer, M. (2019). Selective clearance of the inner nuclear membrane protein emerin by vesicular transport during ER stress. ELife. eLife Sciences Publications. https://doi.org/10.7554/elife.49796","ama":"Buchwalter A, Schulte R, Tsai H, Capitanio J, Hetzer M. Selective clearance of the inner nuclear membrane protein emerin by vesicular transport during ER stress. eLife. 2019;8. doi:10.7554/elife.49796","ieee":"A. Buchwalter, R. Schulte, H. Tsai, J. Capitanio, and M. Hetzer, “Selective clearance of the inner nuclear membrane protein emerin by vesicular transport during ER stress,” eLife, vol. 8. eLife Sciences Publications, 2019.","short":"A. Buchwalter, R. Schulte, H. Tsai, J. Capitanio, M. Hetzer, ELife 8 (2019).","mla":"Buchwalter, Abigail, et al. “Selective Clearance of the Inner Nuclear Membrane Protein Emerin by Vesicular Transport during ER Stress.” ELife, vol. 8, e49796, eLife Sciences Publications, 2019, doi:10.7554/elife.49796."},"user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","oa":1,"publisher":"eLife Sciences Publications","quality_controlled":"1","date_created":"2022-04-07T07:45:02Z","date_published":"2019-10-10T00:00:00Z","doi":"10.7554/elife.49796","year":"2019","has_accepted_license":"1","publication":"eLife","day":"10"},{"_id":"13079","tmp":{"image":"/images/cc_0.png","legal_code_url":"https://creativecommons.org/publicdomain/zero/1.0/legalcode","name":"Creative Commons Public Domain Dedication (CC0 1.0)","short":"CC0 (1.0)"},"type":"research_data_reference","status":"public","citation":{"ista":"Buchwalter A, Schulte R, Tsai H, Capitanio J, Hetzer M. 2019. Data from: Selective clearance of the inner nuclear membrane protein emerin by vesicular transport during ER stress, Dryad, 10.5061/DRYAD.N0R525H.","chicago":"Buchwalter, Abigail, Roberta Schulte, Hsiao Tsai, Juliana Capitanio, and Martin Hetzer. “Data from: Selective Clearance of the Inner Nuclear Membrane Protein Emerin by Vesicular Transport during ER Stress.” Dryad, 2019. https://doi.org/10.5061/DRYAD.N0R525H.","apa":"Buchwalter, A., Schulte, R., Tsai, H., Capitanio, J., & Hetzer, M. (2019). Data from: Selective clearance of the inner nuclear membrane protein emerin by vesicular transport during ER stress. Dryad. https://doi.org/10.5061/DRYAD.N0R525H","ama":"Buchwalter A, Schulte R, Tsai H, Capitanio J, Hetzer M. Data from: Selective clearance of the inner nuclear membrane protein emerin by vesicular transport during ER stress. 2019. doi:10.5061/DRYAD.N0R525H","ieee":"A. Buchwalter, R. Schulte, H. Tsai, J. Capitanio, and M. Hetzer, “Data from: Selective clearance of the inner nuclear membrane protein emerin by vesicular transport during ER stress.” Dryad, 2019.","short":"A. Buchwalter, R. Schulte, H. Tsai, J. Capitanio, M. Hetzer, (2019).","mla":"Buchwalter, Abigail, et al. Data from: Selective Clearance of the Inner Nuclear Membrane Protein Emerin by Vesicular Transport during ER Stress. Dryad, 2019, doi:10.5061/DRYAD.N0R525H."},"date_updated":"2023-05-31T06:36:23Z","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","ddc":["570"],"extern":"1","article_processing_charge":"No","author":[{"first_name":"Abigail","full_name":"Buchwalter, Abigail","last_name":"Buchwalter"},{"full_name":"Schulte, Roberta","last_name":"Schulte","first_name":"Roberta"},{"first_name":"Hsiao","last_name":"Tsai","full_name":"Tsai, Hsiao"},{"full_name":"Capitanio, Juliana","last_name":"Capitanio","first_name":"Juliana"},{"id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","first_name":"Martin W","last_name":"HETZER","orcid":"0000-0002-2111-992X","full_name":"HETZER, Martin W"}],"title":"Data from: Selective clearance of the inner nuclear membrane protein emerin by vesicular transport during ER stress","abstract":[{"lang":"eng","text":"The inner nuclear membrane (INM) is a subdomain of the endoplasmic reticulum (ER) that is gated by the nuclear pore complex. It is unknown whether proteins of the INM and ER are degraded through shared or distinct pathways in mammalian cells. We applied dynamic proteomics to profile protein half-lives and report that INM and ER residents turn over at similar rates, indicating that the INM’s unique topology is not a barrier to turnover. Using a microscopy approach, we observed that the proteasome can degrade INM proteins in situ. However, we also uncovered evidence for selective, vesicular transport-mediated turnover of a single INM protein, emerin, that is potentiated by ER stress. Emerin is rapidly cleared from the INM by a mechanism that requires emerin’s LEM domain to mediate vesicular trafficking to lysosomes. This work demonstrates that the INM can be dynamically remodeled in response to environmental inputs."}],"oa_version":"Published Version","oa":1,"main_file_link":[{"open_access":"1","url":"https://doi.org/10.5061/dryad.n0r525h"}],"publisher":"Dryad","month":"10","year":"2019","day":"28","date_created":"2023-05-23T17:09:30Z","license":"https://creativecommons.org/publicdomain/zero/1.0/","date_published":"2019-10-28T00:00:00Z","related_material":{"record":[{"relation":"used_in_publication","id":"11060","status":"public"}]},"doi":"10.5061/DRYAD.N0R525H"},{"language":[{"iso":"eng"}],"publication_status":"published","publication_identifier":{"issn":["0890-9369","1549-5477"]},"volume":32,"issue":"19-20","pmid":1,"oa_version":"Published Version","abstract":[{"lang":"eng","text":"The total number of nuclear pore complexes (NPCs) per nucleus varies greatly between different cell types and is known to change during cell differentiation and cell transformation. However, the underlying mechanisms that control how many nuclear transport channels are assembled into a given nuclear envelope remain unclear. Here, we report that depletion of the NPC basket protein Tpr, but not Nup153, dramatically increases the total NPC number in various cell types. This negative regulation of Tpr occurs via a phosphorylation cascade of extracellular signal-regulated kinase (ERK), the central kinase of the mitogen-activated protein kinase (MAPK) pathway. Tpr serves as a scaffold for ERK to phosphorylate the nucleoporin (Nup) Nup153, which is critical for early stages of NPC biogenesis. Our results reveal a critical role of the Nup Tpr in coordinating signal transduction pathways during cell proliferation and the dynamic organization of the nucleus."}],"intvolume":" 32","month":"09","main_file_link":[{"url":"https://doi.org/10.1101/gad.315523.118","open_access":"1"}],"scopus_import":"1","extern":"1","date_updated":"2022-07-18T08:32:32Z","_id":"11063","keyword":["Developmental Biology","Genetics"],"status":"public","type":"journal_article","article_type":"original","publication":"Genes & Development","day":"18","year":"2018","date_created":"2022-04-07T07:45:30Z","doi":"10.1101/gad.315523.118","date_published":"2018-09-18T00:00:00Z","page":"1321-1331","oa":1,"quality_controlled":"1","publisher":"Cold Spring Harbor Laboratory","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","citation":{"mla":"McCloskey, Asako, et al. “Tpr Regulates the Total Number of Nuclear Pore Complexes per Cell Nucleus.” Genes & Development, vol. 32, no. 19–20, Cold Spring Harbor Laboratory, 2018, pp. 1321–31, doi:10.1101/gad.315523.118.","short":"A. McCloskey, A. Ibarra, M. Hetzer, Genes & Development 32 (2018) 1321–1331.","ieee":"A. McCloskey, A. Ibarra, and M. Hetzer, “Tpr regulates the total number of nuclear pore complexes per cell nucleus,” Genes & Development, vol. 32, no. 19–20. Cold Spring Harbor Laboratory, pp. 1321–1331, 2018.","apa":"McCloskey, A., Ibarra, A., & Hetzer, M. (2018). Tpr regulates the total number of nuclear pore complexes per cell nucleus. Genes & Development. Cold Spring Harbor Laboratory. https://doi.org/10.1101/gad.315523.118","ama":"McCloskey A, Ibarra A, Hetzer M. Tpr regulates the total number of nuclear pore complexes per cell nucleus. Genes & Development. 2018;32(19-20):1321-1331. doi:10.1101/gad.315523.118","chicago":"McCloskey, Asako, Arkaitz Ibarra, and Martin Hetzer. “Tpr Regulates the Total Number of Nuclear Pore Complexes per Cell Nucleus.” Genes & Development. Cold Spring Harbor Laboratory, 2018. https://doi.org/10.1101/gad.315523.118.","ista":"McCloskey A, Ibarra A, Hetzer M. 2018. Tpr regulates the total number of nuclear pore complexes per cell nucleus. Genes & Development. 32(19–20), 1321–1331."},"title":"Tpr regulates the total number of nuclear pore complexes per cell nucleus","external_id":{"pmid":["30228202"]},"article_processing_charge":"No","author":[{"full_name":"McCloskey, Asako","last_name":"McCloskey","first_name":"Asako"},{"last_name":"Ibarra","full_name":"Ibarra, Arkaitz","first_name":"Arkaitz"},{"last_name":"HETZER","orcid":"0000-0002-2111-992X","full_name":"HETZER, Martin W","first_name":"Martin W","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed"}]},{"article_number":"221","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","citation":{"mla":"Fleischer, Jason G., et al. “Predicting Age from the Transcriptome of Human Dermal Fibroblasts.” Genome Biology, vol. 19, 221, BioMed Central, 2018, doi:10.1186/s13059-018-1599-6.","ama":"Fleischer JG, Schulte R, Tsai HH, et al. Predicting age from the transcriptome of human dermal fibroblasts. Genome Biology. 2018;19. doi:10.1186/s13059-018-1599-6","apa":"Fleischer, J. G., Schulte, R., Tsai, H. H., Tyagi, S., Ibarra, A., Shokhirev, M. N., … Navlakha, S. (2018). Predicting age from the transcriptome of human dermal fibroblasts. Genome Biology. BioMed Central. https://doi.org/10.1186/s13059-018-1599-6","ieee":"J. G. Fleischer et al., “Predicting age from the transcriptome of human dermal fibroblasts,” Genome Biology, vol. 19. BioMed Central, 2018.","short":"J.G. Fleischer, R. Schulte, H.H. Tsai, S. Tyagi, A. Ibarra, M.N. Shokhirev, L. Huang, M. Hetzer, S. Navlakha, Genome Biology 19 (2018).","chicago":"Fleischer, Jason G., Roberta Schulte, Hsiao H. Tsai, Swati Tyagi, Arkaitz Ibarra, Maxim N. Shokhirev, Ling Huang, Martin Hetzer, and Saket Navlakha. “Predicting Age from the Transcriptome of Human Dermal Fibroblasts.” Genome Biology. BioMed Central, 2018. https://doi.org/10.1186/s13059-018-1599-6.","ista":"Fleischer JG, Schulte R, Tsai HH, Tyagi S, Ibarra A, Shokhirev MN, Huang L, Hetzer M, Navlakha S. 2018. Predicting age from the transcriptome of human dermal fibroblasts. Genome Biology. 19, 221."},"title":"Predicting age from the transcriptome of human dermal fibroblasts","author":[{"first_name":"Jason G.","last_name":"Fleischer","full_name":"Fleischer, Jason G."},{"full_name":"Schulte, Roberta","last_name":"Schulte","first_name":"Roberta"},{"first_name":"Hsiao H.","last_name":"Tsai","full_name":"Tsai, Hsiao H."},{"first_name":"Swati","last_name":"Tyagi","full_name":"Tyagi, Swati"},{"last_name":"Ibarra","full_name":"Ibarra, Arkaitz","first_name":"Arkaitz"},{"last_name":"Shokhirev","full_name":"Shokhirev, Maxim N.","first_name":"Maxim N."},{"first_name":"Ling","last_name":"Huang","full_name":"Huang, Ling"},{"id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","first_name":"Martin W","orcid":"0000-0002-2111-992X","full_name":"HETZER, Martin W","last_name":"HETZER"},{"first_name":"Saket","last_name":"Navlakha","full_name":"Navlakha, Saket"}],"article_processing_charge":"No","external_id":{"pmid":["30567591"]},"quality_controlled":"1","publisher":"BioMed Central","oa":1,"day":"20","publication":"Genome Biology","year":"2018","doi":"10.1186/s13059-018-1599-6","date_published":"2018-12-20T00:00:00Z","date_created":"2022-04-07T07:45:40Z","_id":"11064","status":"public","type":"journal_article","article_type":"original","extern":"1","date_updated":"2022-07-18T08:32:34Z","pmid":1,"oa_version":"Published Version","abstract":[{"text":"Biomarkers of aging can be used to assess the health of individuals and to study aging and age-related diseases. We generate a large dataset of genome-wide RNA-seq profiles of human dermal fibroblasts from 133 people aged 1 to 94 years old to test whether signatures of aging are encoded within the transcriptome. We develop an ensemble machine learning method that predicts age to a median error of 4 years, outperforming previous methods used to predict age. The ensemble was further validated by testing it on ten progeria patients, and our method is the only one that predicts accelerated aging in these patients.","lang":"eng"}],"month":"12","intvolume":" 19","scopus_import":"1","main_file_link":[{"url":"https://doi.org/10.1186/s13059-018-1599-6","open_access":"1"}],"language":[{"iso":"eng"}],"publication_identifier":{"issn":["1474-760X"]},"publication_status":"published","volume":19},{"author":[{"first_name":"Tobias M.","last_name":"Franks","full_name":"Franks, Tobias M."},{"first_name":"Asako","last_name":"McCloskey","full_name":"McCloskey, Asako"},{"first_name":"Maxim Nikolaievich","last_name":"Shokhirev","full_name":"Shokhirev, Maxim Nikolaievich"},{"first_name":"Chris","last_name":"Benner","full_name":"Benner, Chris"},{"first_name":"Annie","last_name":"Rathore","full_name":"Rathore, Annie"},{"last_name":"HETZER","full_name":"HETZER, Martin W","orcid":"0000-0002-2111-992X","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","first_name":"Martin W"}],"external_id":{"pmid":["29269482"]},"article_processing_charge":"No","title":"Nup98 recruits the Wdr82–Set1A/COMPASS complex to promoters to regulate H3K4 trimethylation in hematopoietic progenitor cells","citation":{"chicago":"Franks, Tobias M., Asako McCloskey, Maxim Nikolaievich Shokhirev, Chris Benner, Annie Rathore, and Martin Hetzer. “Nup98 Recruits the Wdr82–Set1A/COMPASS Complex to Promoters to Regulate H3K4 Trimethylation in Hematopoietic Progenitor Cells.” Genes & Development. Cold Spring Harbor Laboratory, 2017. https://doi.org/10.1101/gad.306753.117.","ista":"Franks TM, McCloskey A, Shokhirev MN, Benner C, Rathore A, Hetzer M. 2017. Nup98 recruits the Wdr82–Set1A/COMPASS complex to promoters to regulate H3K4 trimethylation in hematopoietic progenitor cells. Genes & Development. 31(22), 2222–2234.","mla":"Franks, Tobias M., et al. “Nup98 Recruits the Wdr82–Set1A/COMPASS Complex to Promoters to Regulate H3K4 Trimethylation in Hematopoietic Progenitor Cells.” Genes & Development, vol. 31, no. 22, Cold Spring Harbor Laboratory, 2017, pp. 2222–34, doi:10.1101/gad.306753.117.","short":"T.M. Franks, A. McCloskey, M.N. Shokhirev, C. Benner, A. Rathore, M. Hetzer, Genes & Development 31 (2017) 2222–2234.","ieee":"T. M. Franks, A. McCloskey, M. N. Shokhirev, C. Benner, A. Rathore, and M. Hetzer, “Nup98 recruits the Wdr82–Set1A/COMPASS complex to promoters to regulate H3K4 trimethylation in hematopoietic progenitor cells,” Genes & Development, vol. 31, no. 22. Cold Spring Harbor Laboratory, pp. 2222–2234, 2017.","ama":"Franks TM, McCloskey A, Shokhirev MN, Benner C, Rathore A, Hetzer M. Nup98 recruits the Wdr82–Set1A/COMPASS complex to promoters to regulate H3K4 trimethylation in hematopoietic progenitor cells. Genes & Development. 2017;31(22):2222-2234. doi:10.1101/gad.306753.117","apa":"Franks, T. M., McCloskey, A., Shokhirev, M. N., Benner, C., Rathore, A., & Hetzer, M. (2017). Nup98 recruits the Wdr82–Set1A/COMPASS complex to promoters to regulate H3K4 trimethylation in hematopoietic progenitor cells. Genes & Development. Cold Spring Harbor Laboratory. https://doi.org/10.1101/gad.306753.117"},"user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","page":"2222-2234","date_published":"2017-12-21T00:00:00Z","doi":"10.1101/gad.306753.117","date_created":"2022-04-07T07:45:59Z","year":"2017","day":"21","publication":"Genes & Development","publisher":"Cold Spring Harbor Laboratory","quality_controlled":"1","oa":1,"date_updated":"2022-07-18T08:33:05Z","extern":"1","type":"journal_article","article_type":"original","status":"public","keyword":["Developmental Biology","Genetics"],"_id":"11066","volume":31,"issue":"22","publication_identifier":{"issn":["0890-9369","1549-5477"]},"publication_status":"published","language":[{"iso":"eng"}],"scopus_import":"1","main_file_link":[{"url":"https://doi.org/10.1101/gad.306753.117","open_access":"1"}],"month":"12","intvolume":" 31","abstract":[{"lang":"eng","text":"Recent studies have shown that a subset of nucleoporins (Nups) can detach from the nuclear pore complex and move into the nuclear interior to regulate transcription. One such dynamic Nup, called Nup98, has been implicated in gene activation in healthy cells and has been shown to drive leukemogenesis when mutated in patients with acute myeloid leukemia (AML). Here we show that in hematopoietic cells, Nup98 binds predominantly to transcription start sites to recruit the Wdr82–Set1A/COMPASS (complex of proteins associated with Set1) complex, which is required for deposition of the histone 3 Lys4 trimethyl (H3K4me3)-activating mark. Depletion of Nup98 or Wdr82 abolishes Set1A recruitment to chromatin and subsequently ablates H3K4me3 at adjacent promoters. Furthermore, expression of a Nup98 fusion protein implicated in aggressive AML causes mislocalization of H3K4me3 at abnormal regions and up-regulation of associated genes. Our findings establish a function of Nup98 in hematopoietic gene activation and provide mechanistic insight into which Nup98 leukemic fusion proteins promote AML."}],"pmid":1,"oa_version":"Published Version"},{"citation":{"ieee":"T. Toda et al., “Nup153 interacts with Sox2 to enable bimodal gene regulation and maintenance of neural progenitor cells,” Cell Stem Cell, vol. 21, no. 5. Elsevier, p. 618–634.e7, 2017.","short":"T. Toda, J.Y. Hsu, S.B. Linker, L. Hu, S.T. Schafer, J. Mertens, F.V. Jacinto, M. Hetzer, F.H. Gage, Cell Stem Cell 21 (2017) 618–634.e7.","apa":"Toda, T., Hsu, J. Y., Linker, S. B., Hu, L., Schafer, S. T., Mertens, J., … Gage, F. H. (2017). Nup153 interacts with Sox2 to enable bimodal gene regulation and maintenance of neural progenitor cells. Cell Stem Cell. Elsevier. https://doi.org/10.1016/j.stem.2017.08.012","ama":"Toda T, Hsu JY, Linker SB, et al. Nup153 interacts with Sox2 to enable bimodal gene regulation and maintenance of neural progenitor cells. Cell Stem Cell. 2017;21(5):618-634.e7. doi:10.1016/j.stem.2017.08.012","mla":"Toda, Tomohisa, et al. “Nup153 Interacts with Sox2 to Enable Bimodal Gene Regulation and Maintenance of Neural Progenitor Cells.” Cell Stem Cell, vol. 21, no. 5, Elsevier, 2017, p. 618–634.e7, doi:10.1016/j.stem.2017.08.012.","ista":"Toda T, Hsu JY, Linker SB, Hu L, Schafer ST, Mertens J, Jacinto FV, Hetzer M, Gage FH. 2017. Nup153 interacts with Sox2 to enable bimodal gene regulation and maintenance of neural progenitor cells. Cell Stem Cell. 21(5), 618–634.e7.","chicago":"Toda, Tomohisa, Jonathan Y. Hsu, Sara B. Linker, Lauren Hu, Simon T. Schafer, Jerome Mertens, Filipe V. Jacinto, Martin Hetzer, and Fred H. Gage. “Nup153 Interacts with Sox2 to Enable Bimodal Gene Regulation and Maintenance of Neural Progenitor Cells.” Cell Stem Cell. Elsevier, 2017. https://doi.org/10.1016/j.stem.2017.08.012."},"user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","author":[{"first_name":"Tomohisa","last_name":"Toda","full_name":"Toda, Tomohisa"},{"first_name":"Jonathan Y.","last_name":"Hsu","full_name":"Hsu, Jonathan Y."},{"first_name":"Sara B.","last_name":"Linker","full_name":"Linker, Sara B."},{"first_name":"Lauren","last_name":"Hu","full_name":"Hu, Lauren"},{"full_name":"Schafer, Simon T.","last_name":"Schafer","first_name":"Simon T."},{"last_name":"Mertens","full_name":"Mertens, Jerome","first_name":"Jerome"},{"first_name":"Filipe V.","last_name":"Jacinto","full_name":"Jacinto, Filipe V."},{"orcid":"0000-0002-2111-992X","full_name":"HETZER, Martin W","last_name":"HETZER","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","first_name":"Martin W"},{"full_name":"Gage, Fred H.","last_name":"Gage","first_name":"Fred H."}],"article_processing_charge":"No","external_id":{"pmid":["28919367"]},"title":"Nup153 interacts with Sox2 to enable bimodal gene regulation and maintenance of neural progenitor cells","year":"2017","day":"02","publication":"Cell Stem Cell","page":"618-634.e7","date_published":"2017-11-02T00:00:00Z","doi":"10.1016/j.stem.2017.08.012","date_created":"2022-04-07T07:46:12Z","publisher":"Elsevier","quality_controlled":"1","oa":1,"date_updated":"2022-07-18T08:33:07Z","extern":"1","_id":"11067","article_type":"original","type":"journal_article","status":"public","keyword":["Cell Biology","Genetics","Molecular Medicine"],"publication_identifier":{"issn":["1934-5909"]},"publication_status":"published","language":[{"iso":"eng"}],"volume":21,"issue":"5","abstract":[{"text":"Neural progenitor cells (NeuPCs) possess a unique nuclear architecture that changes during differentiation. Nucleoporins are linked with cell-type-specific gene regulation, coupling physical changes in nuclear structure to transcriptional output; but, whether and how they coordinate with key fate-determining transcription factors is unclear. Here we show that the nucleoporin Nup153 interacts with Sox2 in adult NeuPCs, where it is indispensable for their maintenance and controls neuronal differentiation. Genome-wide analyses show that Nup153 and Sox2 bind and co-regulate hundreds of genes. Binding of Nup153 to gene promoters or transcriptional end sites correlates with increased or decreased gene expression, respectively, and inhibiting Nup153 expression alters open chromatin configurations at its target genes, disrupts genomic localization of Sox2, and promotes differentiation in vitro and a gliogenic fate switch in vivo. Together, these findings reveal that nuclear structural proteins may exert bimodal transcriptional effects to control cell fate.","lang":"eng"}],"pmid":1,"oa_version":"Published Version","scopus_import":"1","main_file_link":[{"url":"https://doi.org/10.1016/j.stem.2017.08.012","open_access":"1"}],"month":"11","intvolume":" 21"},{"_id":"11065","article_type":"original","type":"journal_article","keyword":["General Physics and Astronomy","General Biochemistry","Genetics and Molecular Biology","General Chemistry"],"status":"public","date_updated":"2022-07-18T08:33:03Z","extern":"1","abstract":[{"text":"Premature aging disorders provide an opportunity to study the mechanisms that drive aging. In Hutchinson-Gilford progeria syndrome (HGPS), a mutant form of the nuclear scaffold protein lamin A distorts nuclei and sequesters nuclear proteins. We sought to investigate protein homeostasis in this disease. Here, we report a widespread increase in protein turnover in HGPS-derived cells compared to normal cells. We determine that global protein synthesis is elevated as a consequence of activated nucleoli and enhanced ribosome biogenesis in HGPS-derived fibroblasts. Depleting normal lamin A or inducing mutant lamin A expression are each sufficient to drive nucleolar expansion. We further show that nucleolar size correlates with donor age in primary fibroblasts derived from healthy individuals and that ribosomal RNA production increases with age, indicating that nucleolar size and activity can serve as aging biomarkers. While limiting ribosome biogenesis extends lifespan in several systems, we show that increased ribosome biogenesis and activity are a hallmark of premature aging.","lang":"eng"}],"oa_version":"Published Version","pmid":1,"main_file_link":[{"open_access":"1","url":"https://doi.org/10.1038/s41467-017-00322-z"}],"scopus_import":"1","intvolume":" 8","month":"08","publication_status":"published","publication_identifier":{"issn":["2041-1723"]},"language":[{"iso":"eng"}],"volume":8,"article_number":"328","citation":{"ista":"Buchwalter A, Hetzer M. 2017. Nucleolar expansion and elevated protein translation in premature aging. Nature Communications. 8, 328.","chicago":"Buchwalter, Abigail, and Martin Hetzer. “Nucleolar Expansion and Elevated Protein Translation in Premature Aging.” Nature Communications. Springer Nature, 2017. https://doi.org/10.1038/s41467-017-00322-z.","apa":"Buchwalter, A., & Hetzer, M. (2017). Nucleolar expansion and elevated protein translation in premature aging. Nature Communications. Springer Nature. https://doi.org/10.1038/s41467-017-00322-z","ama":"Buchwalter A, Hetzer M. Nucleolar expansion and elevated protein translation in premature aging. Nature Communications. 2017;8. doi:10.1038/s41467-017-00322-z","ieee":"A. Buchwalter and M. Hetzer, “Nucleolar expansion and elevated protein translation in premature aging,” Nature Communications, vol. 8. Springer Nature, 2017.","short":"A. Buchwalter, M. Hetzer, Nature Communications 8 (2017).","mla":"Buchwalter, Abigail, and Martin Hetzer. “Nucleolar Expansion and Elevated Protein Translation in Premature Aging.” Nature Communications, vol. 8, 328, Springer Nature, 2017, doi:10.1038/s41467-017-00322-z."},"user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","external_id":{"pmid":["28855503"]},"article_processing_charge":"No","author":[{"full_name":"Buchwalter, Abigail","last_name":"Buchwalter","first_name":"Abigail"},{"last_name":"HETZER","orcid":"0000-0002-2111-992X","full_name":"HETZER, Martin W","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","first_name":"Martin W"}],"title":"Nucleolar expansion and elevated protein translation in premature aging","oa":1,"publisher":"Springer Nature","quality_controlled":"1","year":"2017","publication":"Nature Communications","day":"30","date_created":"2022-04-07T07:45:50Z","doi":"10.1038/s41467-017-00322-z","date_published":"2017-08-30T00:00:00Z"},{"article_number":"13874","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","citation":{"chicago":"Ven, Robert A.H. van de, Jolien S. de Groot, Danielle Park, Robert van Domselaar, Danielle de Jong, Karoly Szuhai, Elsken van der Wall, et al. “P120-Catenin Prevents Multinucleation through Control of MKLP1-Dependent RhoA Activity during Cytokinesis.” Nature Communications. Springer Nature, 2016. https://doi.org/10.1038/ncomms13874.","ista":"van de Ven RAH, de Groot JS, Park D, van Domselaar R, de Jong D, Szuhai K, van der Wall E, Rueda OM, Ali HR, Caldas C, van Diest PJ, Hetzer M, Sahai E, Derksen PWB. 2016. p120-catenin prevents multinucleation through control of MKLP1-dependent RhoA activity during cytokinesis. Nature Communications. 7, 13874.","mla":"van de Ven, Robert A. H., et al. “P120-Catenin Prevents Multinucleation through Control of MKLP1-Dependent RhoA Activity during Cytokinesis.” Nature Communications, vol. 7, 13874, Springer Nature, 2016, doi:10.1038/ncomms13874.","ama":"van de Ven RAH, de Groot JS, Park D, et al. p120-catenin prevents multinucleation through control of MKLP1-dependent RhoA activity during cytokinesis. Nature Communications. 2016;7. doi:10.1038/ncomms13874","apa":"van de Ven, R. A. H., de Groot, J. S., Park, D., van Domselaar, R., de Jong, D., Szuhai, K., … Derksen, P. W. B. (2016). p120-catenin prevents multinucleation through control of MKLP1-dependent RhoA activity during cytokinesis. Nature Communications. Springer Nature. https://doi.org/10.1038/ncomms13874","short":"R.A.H. van de Ven, J.S. de Groot, D. Park, R. van Domselaar, D. de Jong, K. Szuhai, E. van der Wall, O.M. Rueda, H.R. Ali, C. Caldas, P.J. van Diest, M. Hetzer, E. Sahai, P.W.B. Derksen, Nature Communications 7 (2016).","ieee":"R. A. H. van de Ven et al., “p120-catenin prevents multinucleation through control of MKLP1-dependent RhoA activity during cytokinesis,” Nature Communications, vol. 7. Springer Nature, 2016."},"title":"p120-catenin prevents multinucleation through control of MKLP1-dependent RhoA activity during cytokinesis","author":[{"last_name":"van de Ven","full_name":"van de Ven, Robert A.H.","first_name":"Robert A.H."},{"full_name":"de Groot, Jolien S.","last_name":"de Groot","first_name":"Jolien S."},{"first_name":"Danielle","last_name":"Park","full_name":"Park, Danielle"},{"full_name":"van Domselaar, Robert","last_name":"van Domselaar","first_name":"Robert"},{"first_name":"Danielle","last_name":"de Jong","full_name":"de Jong, Danielle"},{"first_name":"Karoly","full_name":"Szuhai, Karoly","last_name":"Szuhai"},{"full_name":"van der Wall, Elsken","last_name":"van der Wall","first_name":"Elsken"},{"last_name":"Rueda","full_name":"Rueda, Oscar M.","first_name":"Oscar M."},{"full_name":"Ali, H. Raza","last_name":"Ali","first_name":"H. Raza"},{"last_name":"Caldas","full_name":"Caldas, Carlos","first_name":"Carlos"},{"full_name":"van Diest, Paul J.","last_name":"van Diest","first_name":"Paul J."},{"id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","first_name":"Martin W","full_name":"HETZER, Martin W","orcid":"0000-0002-2111-992X","last_name":"HETZER"},{"first_name":"Erik","last_name":"Sahai","full_name":"Sahai, Erik"},{"full_name":"Derksen, Patrick W.B.","last_name":"Derksen","first_name":"Patrick W.B."}],"article_processing_charge":"No","external_id":{"pmid":["28004812"]},"quality_controlled":"1","publisher":"Springer Nature","oa":1,"day":"22","publication":"Nature Communications","year":"2016","doi":"10.1038/ncomms13874","date_published":"2016-12-22T00:00:00Z","date_created":"2022-04-07T07:48:34Z","_id":"11072","status":"public","keyword":["General Physics and Astronomy","General Biochemistry","Genetics and Molecular Biology","General Chemistry"],"article_type":"original","type":"journal_article","extern":"1","date_updated":"2022-07-18T08:34:32Z","pmid":1,"oa_version":"Published Version","abstract":[{"lang":"eng","text":"Spatiotemporal activation of RhoA and actomyosin contraction underpins cellular adhesion and division. Loss of cell–cell adhesion and chromosomal instability are cardinal events that drive tumour progression. Here, we show that p120-catenin (p120) not only controls cell–cell adhesion, but also acts as a critical regulator of cytokinesis. We find that p120 regulates actomyosin contractility through concomitant binding to RhoA and the centralspindlin component MKLP1, independent of cadherin association. In anaphase, p120 is enriched at the cleavage furrow where it binds MKLP1 to spatially control RhoA GTPase cycling. Binding of p120 to MKLP1 during cytokinesis depends on the N-terminal coiled-coil domain of p120 isoform 1A. Importantly, clinical data show that loss of p120 expression is a common event in breast cancer that strongly correlates with multinucleation and adverse patient survival. In summary, our study identifies p120 loss as a driver event of chromosomal instability in cancer.\r\n"}],"month":"12","intvolume":" 7","scopus_import":"1","main_file_link":[{"open_access":"1","url":"https://doi.org/10.1038/ncomms13874"}],"language":[{"iso":"eng"}],"publication_identifier":{"issn":["2041-1723"]},"publication_status":"published","related_material":{"link":[{"relation":"erratum","url":"https://doi.org/10.1038/ncomms16030"}]},"volume":7},{"issue":"10","volume":30,"language":[{"iso":"eng"}],"publication_status":"published","publication_identifier":{"eissn":["1549-5477"],"issn":["0890-9369"]},"intvolume":" 30","month":"05","main_file_link":[{"url":"https://doi.org/10.1101/gad.280941.116","open_access":"1"}],"scopus_import":"1","oa_version":"Published Version","pmid":1,"abstract":[{"text":"Nuclear pore complexes (NPCs) emerged as nuclear transport channels in eukaryotic cells ∼1.5 billion years ago. While the primary role of NPCs is to regulate nucleo–cytoplasmic transport, recent research suggests that certain NPC proteins have additionally acquired the role of affecting gene expression at the nuclear periphery and in the nucleoplasm in metazoans. Here we identify a widely expressed variant of the transmembrane nucleoporin (Nup) Pom121 (named sPom121, for “soluble Pom121”) that arose by genomic rearrangement before the divergence of hominoids. sPom121 lacks the nuclear membrane-anchoring domain and thus does not localize to the NPC. Instead, sPom121 colocalizes and interacts with nucleoplasmic Nup98, a previously identified transcriptional regulator, at gene promoters to control transcription of its target genes in human cells. Interestingly, sPom121 transcripts appear independently in several mammalian species, suggesting convergent innovation of Nup-mediated transcription regulation during mammalian evolution. Our findings implicate alternate transcription initiation as a mechanism to increase the functional diversity of NPC components.","lang":"eng"}],"extern":"1","date_updated":"2022-07-18T08:33:50Z","keyword":["Developmental Biology","Genetics"],"status":"public","article_type":"original","type":"journal_article","_id":"11071","date_created":"2022-04-07T07:48:20Z","date_published":"2016-05-19T00:00:00Z","doi":"10.1101/gad.280941.116","page":"1155-1171","publication":"Genes & Development","day":"19","year":"2016","oa":1,"quality_controlled":"1","publisher":"Cold Spring Harbor Laboratory","title":"Evolution of a transcriptional regulator from a transmembrane nucleoporin","article_processing_charge":"No","external_id":{"pmid":["27198230"]},"author":[{"first_name":"Tobias M.","last_name":"Franks","full_name":"Franks, Tobias M."},{"first_name":"Chris","full_name":"Benner, Chris","last_name":"Benner"},{"last_name":"Narvaiza","full_name":"Narvaiza, Iñigo","first_name":"Iñigo"},{"full_name":"Marchetto, Maria C.N.","last_name":"Marchetto","first_name":"Maria C.N."},{"first_name":"Janet M.","full_name":"Young, Janet M.","last_name":"Young"},{"first_name":"Harmit S.","last_name":"Malik","full_name":"Malik, Harmit S."},{"full_name":"Gage, Fred H.","last_name":"Gage","first_name":"Fred H."},{"last_name":"HETZER","full_name":"HETZER, Martin W","orcid":"0000-0002-2111-992X","first_name":"Martin W","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed"}],"user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","citation":{"mla":"Franks, Tobias M., et al. “Evolution of a Transcriptional Regulator from a Transmembrane Nucleoporin.” Genes & Development, vol. 30, no. 10, Cold Spring Harbor Laboratory, 2016, pp. 1155–71, doi:10.1101/gad.280941.116.","ieee":"T. M. Franks et al., “Evolution of a transcriptional regulator from a transmembrane nucleoporin,” Genes & Development, vol. 30, no. 10. Cold Spring Harbor Laboratory, pp. 1155–1171, 2016.","short":"T.M. Franks, C. Benner, I. Narvaiza, M.C.N. Marchetto, J.M. Young, H.S. Malik, F.H. Gage, M. Hetzer, Genes & Development 30 (2016) 1155–1171.","apa":"Franks, T. M., Benner, C., Narvaiza, I., Marchetto, M. C. N., Young, J. M., Malik, H. S., … Hetzer, M. (2016). Evolution of a transcriptional regulator from a transmembrane nucleoporin. Genes & Development. Cold Spring Harbor Laboratory. https://doi.org/10.1101/gad.280941.116","ama":"Franks TM, Benner C, Narvaiza I, et al. Evolution of a transcriptional regulator from a transmembrane nucleoporin. Genes & Development. 2016;30(10):1155-1171. doi:10.1101/gad.280941.116","chicago":"Franks, Tobias M., Chris Benner, Iñigo Narvaiza, Maria C.N. Marchetto, Janet M. Young, Harmit S. Malik, Fred H. Gage, and Martin Hetzer. “Evolution of a Transcriptional Regulator from a Transmembrane Nucleoporin.” Genes & Development. Cold Spring Harbor Laboratory, 2016. https://doi.org/10.1101/gad.280941.116.","ista":"Franks TM, Benner C, Narvaiza I, Marchetto MCN, Young JM, Malik HS, Gage FH, Hetzer M. 2016. Evolution of a transcriptional regulator from a transmembrane nucleoporin. Genes & Development. 30(10), 1155–1171."}},{"extern":"1","date_updated":"2022-07-18T08:33:47Z","_id":"11069","keyword":["Cell Biology"],"status":"public","article_type":"original","type":"journal_article","language":[{"iso":"eng"}],"publication_status":"published","publication_identifier":{"issn":["0021-9525","1540-8140"]},"volume":215,"issue":"1","oa_version":"Published Version","pmid":1,"abstract":[{"text":"Repeated rounds of nuclear envelope (NE) rupture and repair have been observed in laminopathy and cancer cells and result in intermittent loss of nucleus compartmentalization. Currently, the causes of NE rupture are unclear. Here, we show that NE rupture in cancer cells relies on the assembly of contractile actin bundles that interact with the nucleus via the linker of nucleoskeleton and cytoskeleton (LINC) complex. We found that the loss of actin bundles or the LINC complex did not rescue nuclear lamina defects, a previously identified determinant of nuclear membrane stability, but did decrease the number and size of chromatin hernias. Finally, NE rupture inhibition could be rescued in cells treated with actin-depolymerizing drugs by mechanically constraining nucleus height. These data suggest a model of NE rupture where weak membrane areas, caused by defects in lamina organization, rupture because of an increase in intranuclear pressure from actin-based nucleus confinement.","lang":"eng"}],"intvolume":" 215","month":"10","main_file_link":[{"open_access":"1","url":"https://doi.org/10.1083/jcb.201603053"}],"scopus_import":"1","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","citation":{"chicago":"Hatch, Emily M., and Martin Hetzer. “Nuclear Envelope Rupture Is Induced by Actin-Based Nucleus Confinement.” Journal of Cell Biology. Rockefeller University Press, 2016. https://doi.org/10.1083/jcb.201603053.","ista":"Hatch EM, Hetzer M. 2016. Nuclear envelope rupture is induced by actin-based nucleus confinement. Journal of Cell Biology. 215(1), 27–36.","mla":"Hatch, Emily M., and Martin Hetzer. “Nuclear Envelope Rupture Is Induced by Actin-Based Nucleus Confinement.” Journal of Cell Biology, vol. 215, no. 1, Rockefeller University Press, 2016, pp. 27–36, doi:10.1083/jcb.201603053.","short":"E.M. Hatch, M. Hetzer, Journal of Cell Biology 215 (2016) 27–36.","ieee":"E. M. Hatch and M. Hetzer, “Nuclear envelope rupture is induced by actin-based nucleus confinement,” Journal of Cell Biology, vol. 215, no. 1. Rockefeller University Press, pp. 27–36, 2016.","apa":"Hatch, E. M., & Hetzer, M. (2016). Nuclear envelope rupture is induced by actin-based nucleus confinement. Journal of Cell Biology. Rockefeller University Press. https://doi.org/10.1083/jcb.201603053","ama":"Hatch EM, Hetzer M. Nuclear envelope rupture is induced by actin-based nucleus confinement. Journal of Cell Biology. 2016;215(1):27-36. doi:10.1083/jcb.201603053"},"title":"Nuclear envelope rupture is induced by actin-based nucleus confinement","external_id":{"pmid":["27697922"]},"article_processing_charge":"No","author":[{"first_name":"Emily M.","full_name":"Hatch, Emily M.","last_name":"Hatch"},{"orcid":"0000-0002-2111-992X","full_name":"HETZER, Martin W","last_name":"HETZER","first_name":"Martin W","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed"}],"publication":"Journal of Cell Biology","day":"03","year":"2016","date_created":"2022-04-07T07:47:42Z","date_published":"2016-10-03T00:00:00Z","doi":"10.1083/jcb.201603053","page":"27-36","oa":1,"quality_controlled":"1","publisher":"Rockefeller University Press"},{"_id":"11070","status":"public","keyword":["Developmental Biology","Genetics"],"type":"journal_article","article_type":"original","extern":"1","date_updated":"2022-07-18T08:33:49Z","oa_version":"Published Version","pmid":1,"abstract":[{"text":"The organization of the genome in the three-dimensional space of the nucleus is coupled with cell type-specific gene expression. However, how nuclear architecture influences transcription that governs cell identity remains unknown. Here, we show that nuclear pore complex (NPC) components Nup93 and Nup153 bind superenhancers (SE), regulatory structures that drive the expression of key genes that specify cell identity. We found that nucleoporin-associated SEs localize preferentially to the nuclear periphery, and absence of Nup153 and Nup93 results in dramatic transcriptional changes of SE-associated genes. Our results reveal a crucial role of NPC components in the regulation of cell type-specifying genes and highlight nuclear architecture as a regulatory layer of genome functions in cell fate.","lang":"eng"}],"month":"11","intvolume":" 30","scopus_import":"1","main_file_link":[{"url":"https://doi.org/10.1101/gad.287417.116","open_access":"1"}],"language":[{"iso":"eng"}],"publication_identifier":{"eissn":["1549-5477"],"issn":["0890-9369"]},"publication_status":"published","issue":"20","volume":30,"user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","citation":{"ista":"Ibarra A, Benner C, Tyagi S, Cool J, Hetzer M. 2016. Nucleoporin-mediated regulation of cell identity genes. Genes & Development. 30(20), 2253–2258.","chicago":"Ibarra, Arkaitz, Chris Benner, Swati Tyagi, Jonah Cool, and Martin Hetzer. “Nucleoporin-Mediated Regulation of Cell Identity Genes.” Genes & Development. Cold Spring Harbor Laboratory, 2016. https://doi.org/10.1101/gad.287417.116.","apa":"Ibarra, A., Benner, C., Tyagi, S., Cool, J., & Hetzer, M. (2016). Nucleoporin-mediated regulation of cell identity genes. Genes & Development. Cold Spring Harbor Laboratory. https://doi.org/10.1101/gad.287417.116","ama":"Ibarra A, Benner C, Tyagi S, Cool J, Hetzer M. Nucleoporin-mediated regulation of cell identity genes. Genes & Development. 2016;30(20):2253-2258. doi:10.1101/gad.287417.116","short":"A. Ibarra, C. Benner, S. Tyagi, J. Cool, M. Hetzer, Genes & Development 30 (2016) 2253–2258.","ieee":"A. Ibarra, C. Benner, S. Tyagi, J. Cool, and M. Hetzer, “Nucleoporin-mediated regulation of cell identity genes,” Genes & Development, vol. 30, no. 20. Cold Spring Harbor Laboratory, pp. 2253–2258, 2016.","mla":"Ibarra, Arkaitz, et al. “Nucleoporin-Mediated Regulation of Cell Identity Genes.” Genes & Development, vol. 30, no. 20, Cold Spring Harbor Laboratory, 2016, pp. 2253–58, doi:10.1101/gad.287417.116."},"title":"Nucleoporin-mediated regulation of cell identity genes","author":[{"first_name":"Arkaitz","full_name":"Ibarra, Arkaitz","last_name":"Ibarra"},{"first_name":"Chris","full_name":"Benner, Chris","last_name":"Benner"},{"full_name":"Tyagi, Swati","last_name":"Tyagi","first_name":"Swati"},{"first_name":"Jonah","last_name":"Cool","full_name":"Cool, Jonah"},{"id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","first_name":"Martin W","full_name":"HETZER, Martin W","orcid":"0000-0002-2111-992X","last_name":"HETZER"}],"external_id":{"pmid":["27807035"]},"article_processing_charge":"No","publisher":"Cold Spring Harbor Laboratory","quality_controlled":"1","oa":1,"day":"02","publication":"Genes & Development","year":"2016","date_published":"2016-11-02T00:00:00Z","doi":"10.1101/gad.287417.116","date_created":"2022-04-07T07:48:08Z","page":"2253-2258"},{"oa_version":"Published Version","pmid":1,"abstract":[{"text":"Aging is a major risk factor for many human diseases, and in vitro generation of human neurons is an attractive approach for modeling aging-related brain disorders. However, modeling aging in differentiated human neurons has proved challenging. We generated neurons from human donors across a broad range of ages, either by iPSC-based reprogramming and differentiation or by direct conversion into induced neurons (iNs). While iPSCs and derived neurons did not retain aging-associated gene signatures, iNs displayed age-specific transcriptional profiles and revealed age-associated decreases in the nuclear transport receptor RanBP17. We detected an age-dependent loss of nucleocytoplasmic compartmentalization (NCC) in donor fibroblasts and corresponding iNs and found that reduced RanBP17 impaired NCC in young cells, while iPSC rejuvenation restored NCC in aged cells. These results show that iNs retain important aging-related signatures, thus allowing modeling of the aging process in vitro, and they identify impaired NCC as an important factor in human aging.","lang":"eng"}],"month":"12","intvolume":" 17","scopus_import":"1","main_file_link":[{"open_access":"1","url":"https://doi.org/10.1016/j.stem.2015.09.001"}],"language":[{"iso":"eng"}],"publication_identifier":{"issn":["1934-5909"]},"publication_status":"published","issue":"6","volume":17,"_id":"11079","status":"public","keyword":["Cell Biology","Genetics","Molecular Medicine"],"type":"journal_article","article_type":"original","extern":"1","date_updated":"2022-07-18T08:44:21Z","quality_controlled":"1","publisher":"Elsevier","oa":1,"day":"03","publication":"Cell Stem Cell","year":"2015","doi":"10.1016/j.stem.2015.09.001","date_published":"2015-12-03T00:00:00Z","date_created":"2022-04-07T07:49:51Z","page":"705-718","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","citation":{"ista":"Mertens J, Paquola ACM, Ku M, Hatch E, Böhnke L, Ladjevardi S, McGrath S, Campbell B, Lee H, Herdy JR, Gonçalves JT, Toda T, Kim Y, Winkler J, Yao J, Hetzer M, Gage FH. 2015. Directly reprogrammed human neurons retain aging-associated transcriptomic signatures and reveal age-related nucleocytoplasmic defects. Cell Stem Cell. 17(6), 705–718.","chicago":"Mertens, Jerome, Apuã C.M. Paquola, Manching Ku, Emily Hatch, Lena Böhnke, Shauheen Ladjevardi, Sean McGrath, et al. “Directly Reprogrammed Human Neurons Retain Aging-Associated Transcriptomic Signatures and Reveal Age-Related Nucleocytoplasmic Defects.” Cell Stem Cell. Elsevier, 2015. https://doi.org/10.1016/j.stem.2015.09.001.","ieee":"J. Mertens et al., “Directly reprogrammed human neurons retain aging-associated transcriptomic signatures and reveal age-related nucleocytoplasmic defects,” Cell Stem Cell, vol. 17, no. 6. Elsevier, pp. 705–718, 2015.","short":"J. Mertens, A.C.M. Paquola, M. Ku, E. Hatch, L. Böhnke, S. Ladjevardi, S. McGrath, B. Campbell, H. Lee, J.R. Herdy, J.T. Gonçalves, T. Toda, Y. Kim, J. Winkler, J. Yao, M. Hetzer, F.H. Gage, Cell Stem Cell 17 (2015) 705–718.","ama":"Mertens J, Paquola ACM, Ku M, et al. Directly reprogrammed human neurons retain aging-associated transcriptomic signatures and reveal age-related nucleocytoplasmic defects. Cell Stem Cell. 2015;17(6):705-718. doi:10.1016/j.stem.2015.09.001","apa":"Mertens, J., Paquola, A. C. M., Ku, M., Hatch, E., Böhnke, L., Ladjevardi, S., … Gage, F. H. (2015). Directly reprogrammed human neurons retain aging-associated transcriptomic signatures and reveal age-related nucleocytoplasmic defects. Cell Stem Cell. Elsevier. https://doi.org/10.1016/j.stem.2015.09.001","mla":"Mertens, Jerome, et al. “Directly Reprogrammed Human Neurons Retain Aging-Associated Transcriptomic Signatures and Reveal Age-Related Nucleocytoplasmic Defects.” Cell Stem Cell, vol. 17, no. 6, Elsevier, 2015, pp. 705–18, doi:10.1016/j.stem.2015.09.001."},"title":"Directly reprogrammed human neurons retain aging-associated transcriptomic signatures and reveal age-related nucleocytoplasmic defects","author":[{"last_name":"Mertens","full_name":"Mertens, Jerome","first_name":"Jerome"},{"full_name":"Paquola, Apuã C.M.","last_name":"Paquola","first_name":"Apuã C.M."},{"last_name":"Ku","full_name":"Ku, Manching","first_name":"Manching"},{"full_name":"Hatch, Emily","last_name":"Hatch","first_name":"Emily"},{"first_name":"Lena","last_name":"Böhnke","full_name":"Böhnke, Lena"},{"last_name":"Ladjevardi","full_name":"Ladjevardi, Shauheen","first_name":"Shauheen"},{"last_name":"McGrath","full_name":"McGrath, Sean","first_name":"Sean"},{"first_name":"Benjamin","full_name":"Campbell, Benjamin","last_name":"Campbell"},{"last_name":"Lee","full_name":"Lee, Hyungjun","first_name":"Hyungjun"},{"last_name":"Herdy","full_name":"Herdy, Joseph R.","first_name":"Joseph R."},{"first_name":"J. Tiago","full_name":"Gonçalves, J. Tiago","last_name":"Gonçalves"},{"first_name":"Tomohisa","last_name":"Toda","full_name":"Toda, Tomohisa"},{"first_name":"Yongsung","full_name":"Kim, Yongsung","last_name":"Kim"},{"first_name":"Jürgen","full_name":"Winkler, Jürgen","last_name":"Winkler"},{"first_name":"Jun","full_name":"Yao, Jun","last_name":"Yao"},{"last_name":"HETZER","full_name":"HETZER, Martin W","orcid":"0000-0002-2111-992X","first_name":"Martin W","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed"},{"full_name":"Gage, Fred H.","last_name":"Gage","first_name":"Fred H."}],"external_id":{"pmid":["26456686"]},"article_processing_charge":"No"},{"citation":{"chicago":"Jacinto, Filipe V., Chris Benner, and Martin Hetzer. “The Nucleoporin Nup153 Regulates Embryonic Stem Cell Pluripotency through Gene Silencing.” Genes & Development. Cold Spring Harbor Laboratory, 2015. https://doi.org/10.1101/gad.260919.115.","ista":"Jacinto FV, Benner C, Hetzer M. 2015. The nucleoporin Nup153 regulates embryonic stem cell pluripotency through gene silencing. Genes & Development. 29(12), 1224–1238.","mla":"Jacinto, Filipe V., et al. “The Nucleoporin Nup153 Regulates Embryonic Stem Cell Pluripotency through Gene Silencing.” Genes & Development, vol. 29, no. 12, Cold Spring Harbor Laboratory, 2015, pp. 1224–38, doi:10.1101/gad.260919.115.","ieee":"F. V. Jacinto, C. Benner, and M. Hetzer, “The nucleoporin Nup153 regulates embryonic stem cell pluripotency through gene silencing,” Genes & Development, vol. 29, no. 12. Cold Spring Harbor Laboratory, pp. 1224–1238, 2015.","short":"F.V. Jacinto, C. Benner, M. Hetzer, Genes & Development 29 (2015) 1224–1238.","ama":"Jacinto FV, Benner C, Hetzer M. The nucleoporin Nup153 regulates embryonic stem cell pluripotency through gene silencing. Genes & Development. 2015;29(12):1224-1238. doi:10.1101/gad.260919.115","apa":"Jacinto, F. V., Benner, C., & Hetzer, M. (2015). The nucleoporin Nup153 regulates embryonic stem cell pluripotency through gene silencing. Genes & Development. Cold Spring Harbor Laboratory. https://doi.org/10.1101/gad.260919.115"},"user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","article_processing_charge":"No","external_id":{"pmid":["26080816"]},"author":[{"full_name":"Jacinto, Filipe V.","last_name":"Jacinto","first_name":"Filipe V."},{"first_name":"Chris","full_name":"Benner, Chris","last_name":"Benner"},{"first_name":"Martin W","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","last_name":"HETZER","full_name":"HETZER, Martin W","orcid":"0000-0002-2111-992X"}],"title":"The nucleoporin Nup153 regulates embryonic stem cell pluripotency through gene silencing","year":"2015","publication":"Genes & Development","day":"16","page":"1224-1238","date_created":"2022-04-07T07:49:31Z","doi":"10.1101/gad.260919.115","date_published":"2015-06-16T00:00:00Z","oa":1,"quality_controlled":"1","publisher":"Cold Spring Harbor Laboratory","date_updated":"2022-07-18T08:43:51Z","extern":"1","_id":"11077","article_type":"original","type":"journal_article","keyword":["Developmental Biology","Genetics"],"status":"public","publication_status":"published","publication_identifier":{"eissn":["1549-5477"],"issn":["0890-9369"]},"language":[{"iso":"eng"}],"issue":"12","volume":29,"abstract":[{"lang":"eng","text":"Nucleoporins (Nups) are a family of proteins best known as the constituent building blocks of nuclear pore complexes (NPCs), membrane-embedded channels that mediate nuclear transport across the nuclear envelope. Recent evidence suggests that several Nups have additional roles in controlling the activation and silencing of developmental genes; however, the mechanistic details of these functions remain poorly understood. Here, we show that depletion of Nup153 in mouse embryonic stem cells (mESCs) causes the derepression of developmental genes and induction of early differentiation. This loss of stem cell identity is not associated with defects in the nuclear import of key pluripotency factors. Rather, Nup153 binds around the transcriptional start site (TSS) of developmental genes and mediates the recruitment of the polycomb-repressive complex 1 (PRC1) to a subset of its target loci. Our results demonstrate a chromatin-associated role of Nup153 in maintaining stem cell pluripotency by functioning in mammalian epigenetic gene silencing."}],"pmid":1,"oa_version":"Published Version","main_file_link":[{"open_access":"1","url":"https://doi.org/10.1101/gad.260919.115"}],"scopus_import":"1","intvolume":" 29","month":"06"},{"oa":1,"quality_controlled":"1","publisher":"Elsevier","year":"2015","publication":"Cell Systems","day":"23","page":"P224-237","date_created":"2022-04-07T07:49:39Z","date_published":"2015-09-23T00:00:00Z","doi":"10.1016/j.cels.2015.08.012","citation":{"chicago":"Ori, Alessandro, Brandon H. Toyama, Michael S. Harris, Thomas Bock, Murat Iskar, Peer Bork, Nicholas T. Ingolia, Martin Hetzer, and Martin Beck. “Integrated Transcriptome and Proteome Analyses Reveal Organ-Specific Proteome Deterioration in Old Rats.” Cell Systems. Elsevier, 2015. https://doi.org/10.1016/j.cels.2015.08.012.","ista":"Ori A, Toyama BH, Harris MS, Bock T, Iskar M, Bork P, Ingolia NT, Hetzer M, Beck M. 2015. Integrated transcriptome and proteome analyses reveal organ-specific proteome deterioration in old rats. Cell Systems. 1(3), P224-237.","mla":"Ori, Alessandro, et al. “Integrated Transcriptome and Proteome Analyses Reveal Organ-Specific Proteome Deterioration in Old Rats.” Cell Systems, vol. 1, no. 3, Elsevier, 2015, pp. P224-237, doi:10.1016/j.cels.2015.08.012.","ama":"Ori A, Toyama BH, Harris MS, et al. Integrated transcriptome and proteome analyses reveal organ-specific proteome deterioration in old rats. Cell Systems. 2015;1(3):P224-237. doi:10.1016/j.cels.2015.08.012","apa":"Ori, A., Toyama, B. H., Harris, M. S., Bock, T., Iskar, M., Bork, P., … Beck, M. (2015). Integrated transcriptome and proteome analyses reveal organ-specific proteome deterioration in old rats. Cell Systems. Elsevier. https://doi.org/10.1016/j.cels.2015.08.012","short":"A. Ori, B.H. Toyama, M.S. Harris, T. Bock, M. Iskar, P. Bork, N.T. Ingolia, M. Hetzer, M. Beck, Cell Systems 1 (2015) P224-237.","ieee":"A. Ori et al., “Integrated transcriptome and proteome analyses reveal organ-specific proteome deterioration in old rats,” Cell Systems, vol. 1, no. 3. Elsevier, pp. P224-237, 2015."},"user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","article_processing_charge":"No","external_id":{"pmid":["27135913"]},"author":[{"first_name":"Alessandro","last_name":"Ori","full_name":"Ori, Alessandro"},{"full_name":"Toyama, Brandon H.","last_name":"Toyama","first_name":"Brandon H."},{"first_name":"Michael S.","last_name":"Harris","full_name":"Harris, Michael S."},{"full_name":"Bock, Thomas","last_name":"Bock","first_name":"Thomas"},{"first_name":"Murat","last_name":"Iskar","full_name":"Iskar, Murat"},{"last_name":"Bork","full_name":"Bork, Peer","first_name":"Peer"},{"full_name":"Ingolia, Nicholas T.","last_name":"Ingolia","first_name":"Nicholas T."},{"first_name":"Martin W","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","last_name":"HETZER","orcid":"0000-0002-2111-992X","full_name":"HETZER, Martin W"},{"first_name":"Martin","full_name":"Beck, Martin","last_name":"Beck"}],"title":"Integrated transcriptome and proteome analyses reveal organ-specific proteome deterioration in old rats","abstract":[{"text":"Aging is associated with the decline of protein, cell, and organ function. Here, we use an integrated approach to characterize gene expression, bulk translation, and cell biology in the brains and livers of young and old rats. We identify 468 differences in protein abundance between young and old animals. The majority are a consequence of altered translation output, that is, the combined effect of changes in transcript abundance and translation efficiency. In addition, we identify 130 proteins whose overall abundance remains unchanged but whose sub-cellular localization, phosphorylation state, or splice-form varies. While some protein-level differences appear to be a generic property of the rats’ chronological age, the majority are specific to one organ. These may be a consequence of the organ’s physiology or the chronological age of the cells within the tissue. Taken together, our study provides an initial view of the proteome at the molecular, sub-cellular, and organ level in young and old rats.","lang":"eng"}],"oa_version":"Published Version","pmid":1,"main_file_link":[{"url":"https://doi.org/10.1016/j.cels.2015.08.012","open_access":"1"}],"scopus_import":"1","intvolume":" 1","month":"09","publication_status":"published","publication_identifier":{"issn":["2405-4712"]},"language":[{"iso":"eng"}],"volume":1,"issue":"3","_id":"11078","type":"journal_article","article_type":"original","keyword":["Cell Biology","Histology","Pathology and Forensic Medicine"],"status":"public","date_updated":"2022-07-18T08:44:07Z","extern":"1"},{"author":[{"last_name":"Gomez-Cavazos","full_name":"Gomez-Cavazos, J. Sebastian","first_name":"J. Sebastian"},{"id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","first_name":"Martin W","orcid":"0000-0002-2111-992X","full_name":"HETZER, Martin W","last_name":"HETZER"}],"external_id":{"pmid":["25778917"]},"article_processing_charge":"No","title":"The nucleoporin gp210/Nup210 controls muscle differentiation by regulating nuclear envelope/ER homeostasis","citation":{"mla":"Gomez-Cavazos, J. Sebastian, and Martin Hetzer. “The Nucleoporin Gp210/Nup210 Controls Muscle Differentiation by Regulating Nuclear Envelope/ER Homeostasis.” Journal of Cell Biology, vol. 208, no. 6, Rockefeller University Press, 2015, pp. 671–81, doi:10.1083/jcb.201410047.","short":"J.S. Gomez-Cavazos, M. Hetzer, Journal of Cell Biology 208 (2015) 671–681.","ieee":"J. S. Gomez-Cavazos and M. Hetzer, “The nucleoporin gp210/Nup210 controls muscle differentiation by regulating nuclear envelope/ER homeostasis,” Journal of Cell Biology, vol. 208, no. 6. Rockefeller University Press, pp. 671–681, 2015.","ama":"Gomez-Cavazos JS, Hetzer M. The nucleoporin gp210/Nup210 controls muscle differentiation by regulating nuclear envelope/ER homeostasis. Journal of Cell Biology. 2015;208(6):671-681. doi:10.1083/jcb.201410047","apa":"Gomez-Cavazos, J. S., & Hetzer, M. (2015). The nucleoporin gp210/Nup210 controls muscle differentiation by regulating nuclear envelope/ER homeostasis. Journal of Cell Biology. Rockefeller University Press. https://doi.org/10.1083/jcb.201410047","chicago":"Gomez-Cavazos, J. Sebastian, and Martin Hetzer. “The Nucleoporin Gp210/Nup210 Controls Muscle Differentiation by Regulating Nuclear Envelope/ER Homeostasis.” Journal of Cell Biology. Rockefeller University Press, 2015. https://doi.org/10.1083/jcb.201410047.","ista":"Gomez-Cavazos JS, Hetzer M. 2015. The nucleoporin gp210/Nup210 controls muscle differentiation by regulating nuclear envelope/ER homeostasis. Journal of Cell Biology. 208(6), 671–681."},"user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","quality_controlled":"1","publisher":"Rockefeller University Press","page":"671-681","date_published":"2015-03-16T00:00:00Z","doi":"10.1083/jcb.201410047","date_created":"2022-04-07T07:49:10Z","year":"2015","day":"16","publication":"Journal of Cell Biology","type":"journal_article","article_type":"original","status":"public","keyword":["Cell Biology"],"_id":"11075","date_updated":"2022-07-18T08:43:00Z","extern":"1","scopus_import":"1","month":"03","intvolume":" 208","abstract":[{"text":"Previously, we identified the nucleoporin gp210/Nup210 as a critical regulator of muscle and neuronal differentiation, but how this nucleoporin exerts its function and whether it modulates nuclear pore complex (NPC) activity remain unknown. Here, we show that gp210/Nup210 mediates muscle cell differentiation in vitro via its conserved N-terminal domain that extends into the perinuclear space. Removal of the C-terminal domain, which partially mislocalizes gp210/Nup210 away from NPCs, efficiently rescues the differentiation defect caused by the knockdown of endogenous gp210/Nup210. Unexpectedly, a gp210/Nup210 mutant lacking the NPC-targeting transmembrane and C-terminal domains is sufficient for C2C12 myoblast differentiation. We demonstrate that the endoplasmic reticulum (ER) stress-specific caspase cascade is exacerbated during Nup210 depletion and that blocking ER stress-mediated apoptosis rescues differentiation of Nup210-deficient cells. Our results suggest that the role of gp210/Nup210 in cell differentiation is mediated by its large luminal domain, which can act independently of NPC association and appears to play a pivotal role in the maintenance of nuclear envelope/ER homeostasis.","lang":"eng"}],"pmid":1,"oa_version":"Published Version","volume":208,"issue":"6","publication_identifier":{"issn":["0021-9525"],"eissn":["1540-8140"]},"publication_status":"published","language":[{"iso":"eng"}]},{"month":"02","intvolume":" 29","scopus_import":"1","main_file_link":[{"url":"https://doi.org/10.1101/gad.256495.114","open_access":"1"}],"oa_version":"Published Version","pmid":1,"abstract":[{"lang":"eng","text":"Nuclear pore complexes (NPCs) are composed of several copies of ∼30 different proteins called nucleoporins (Nups). NPCs penetrate the nuclear envelope (NE) and regulate the nucleocytoplasmic trafficking of macromolecules. Beyond this vital role, NPC components influence genome functions in a transport-independent manner. Nups play an evolutionarily conserved role in gene expression regulation that, in metazoans, extends into the nuclear interior. Additionally, in proliferative cells, Nups play a crucial role in genome integrity maintenance and mitotic progression. Here we discuss genome-related functions of Nups and their impact on essential DNA metabolism processes such as transcription, chromosome duplication, and segregation."}],"issue":"4","volume":29,"language":[{"iso":"eng"}],"publication_identifier":{"eissn":["1549-5477"],"issn":["0890-9369"]},"publication_status":"published","status":"public","keyword":["Developmental Biology","Genetics"],"type":"journal_article","article_type":"original","_id":"11076","extern":"1","date_updated":"2022-07-18T08:43:20Z","publisher":"Cold Spring Harbor Laboratory","quality_controlled":"1","oa":1,"doi":"10.1101/gad.256495.114","date_published":"2015-02-01T00:00:00Z","date_created":"2022-04-07T07:49:21Z","page":"337-349","day":"01","publication":"Genes & Development","year":"2015","title":"Nuclear pore proteins and the control of genome functions","author":[{"first_name":"Arkaitz","full_name":"Ibarra, Arkaitz","last_name":"Ibarra"},{"last_name":"HETZER","orcid":"0000-0002-2111-992X","full_name":"HETZER, Martin W","first_name":"Martin W","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed"}],"article_processing_charge":"No","external_id":{"pmid":["25691464"]},"user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","citation":{"chicago":"Ibarra, Arkaitz, and Martin Hetzer. “Nuclear Pore Proteins and the Control of Genome Functions.” Genes & Development. Cold Spring Harbor Laboratory, 2015. https://doi.org/10.1101/gad.256495.114.","ista":"Ibarra A, Hetzer M. 2015. Nuclear pore proteins and the control of genome functions. Genes & Development. 29(4), 337–349.","mla":"Ibarra, Arkaitz, and Martin Hetzer. “Nuclear Pore Proteins and the Control of Genome Functions.” Genes & Development, vol. 29, no. 4, Cold Spring Harbor Laboratory, 2015, pp. 337–49, doi:10.1101/gad.256495.114.","ama":"Ibarra A, Hetzer M. Nuclear pore proteins and the control of genome functions. Genes & Development. 2015;29(4):337-349. doi:10.1101/gad.256495.114","apa":"Ibarra, A., & Hetzer, M. (2015). Nuclear pore proteins and the control of genome functions. Genes & Development. Cold Spring Harbor Laboratory. https://doi.org/10.1101/gad.256495.114","short":"A. Ibarra, M. Hetzer, Genes & Development 29 (2015) 337–349.","ieee":"A. Ibarra and M. Hetzer, “Nuclear pore proteins and the control of genome functions,” Genes & Development, vol. 29, no. 4. Cold Spring Harbor Laboratory, pp. 337–349, 2015."}},{"year":"2015","publication":"Cell","day":"18","page":"1502-1504","date_created":"2022-04-07T07:48:49Z","date_published":"2015-06-18T00:00:00Z","doi":"10.1016/j.cell.2015.06.005","oa":1,"publisher":"Elsevier","quality_controlled":"1","citation":{"chicago":"Hatch, Emily M., and Martin Hetzer. “Linking Micronuclei to Chromosome Fragmentation.” Cell. Elsevier, 2015. https://doi.org/10.1016/j.cell.2015.06.005.","ista":"Hatch EM, Hetzer M. 2015. Linking micronuclei to chromosome fragmentation. Cell. 161(7), 1502–1504.","mla":"Hatch, Emily M., and Martin Hetzer. “Linking Micronuclei to Chromosome Fragmentation.” Cell, vol. 161, no. 7, Elsevier, 2015, pp. 1502–04, doi:10.1016/j.cell.2015.06.005.","short":"E.M. Hatch, M. Hetzer, Cell 161 (2015) 1502–1504.","ieee":"E. M. Hatch and M. Hetzer, “Linking micronuclei to chromosome fragmentation,” Cell, vol. 161, no. 7. Elsevier, pp. 1502–1504, 2015.","ama":"Hatch EM, Hetzer M. Linking micronuclei to chromosome fragmentation. Cell. 2015;161(7):1502-1504. doi:10.1016/j.cell.2015.06.005","apa":"Hatch, E. M., & Hetzer, M. (2015). Linking micronuclei to chromosome fragmentation. Cell. Elsevier. https://doi.org/10.1016/j.cell.2015.06.005"},"user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","external_id":{"pmid":["26091034"]},"article_processing_charge":"No","author":[{"first_name":"Emily M.","full_name":"Hatch, Emily M.","last_name":"Hatch"},{"orcid":"0000-0002-2111-992X","full_name":"HETZER, Martin W","last_name":"HETZER","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","first_name":"Martin W"}],"title":"Linking micronuclei to chromosome fragmentation","publication_status":"published","publication_identifier":{"issn":["0092-8674"]},"language":[{"iso":"eng"}],"volume":161,"issue":"7","abstract":[{"lang":"eng","text":"Human cancer cells bear complex chromosome rearrangements that can be potential drivers of cancer development. However, the molecular mechanisms underlying these rearrangements have been unclear. Zhang et al. use a new technique combining live-cell imaging and single-cell sequencing to demonstrate that chromosomes mis-segregated to micronuclei frequently undergo chromothripsis-like rearrangements in the subsequent cell cycle."}],"pmid":1,"oa_version":"Published Version","main_file_link":[{"url":"https://doi.org/10.1016/j.cell.2015.06.005","open_access":"1"}],"scopus_import":"1","intvolume":" 161","month":"06","date_updated":"2022-07-18T08:34:33Z","extern":"1","_id":"11073","type":"journal_article","article_type":"original","keyword":["General Biochemistry","Genetics and Molecular Biology"],"status":"public"},{"_id":"11074","type":"journal_article","article_type":"original","keyword":["General Agricultural and Biological Sciences","General Biochemistry","Genetics and Molecular Biology"],"status":"public","date_updated":"2022-07-18T08:34:34Z","extern":"1","pmid":1,"oa_version":"Published Version","main_file_link":[{"url":"https://doi.org/10.1016/j.cub.2015.02.033","open_access":"1"}],"scopus_import":"1","intvolume":" 25","month":"05","publication_status":"published","publication_identifier":{"issn":["0960-9822"]},"language":[{"iso":"eng"}],"volume":25,"issue":"10","citation":{"apa":"Hatch, E. M., & Hetzer, M. (2015). Chromothripsis. Current Biology. Elsevier. https://doi.org/10.1016/j.cub.2015.02.033","ama":"Hatch EM, Hetzer M. Chromothripsis. Current Biology. 2015;25(10):PR397-R399. doi:10.1016/j.cub.2015.02.033","short":"E.M. Hatch, M. Hetzer, Current Biology 25 (2015) PR397-R399.","ieee":"E. M. Hatch and M. Hetzer, “Chromothripsis,” Current Biology, vol. 25, no. 10. Elsevier, pp. PR397-R399, 2015.","mla":"Hatch, Emily M., and Martin Hetzer. “Chromothripsis.” Current Biology, vol. 25, no. 10, Elsevier, 2015, pp. PR397-R399, doi:10.1016/j.cub.2015.02.033.","ista":"Hatch EM, Hetzer M. 2015. Chromothripsis. Current Biology. 25(10), PR397-R399.","chicago":"Hatch, Emily M., and Martin Hetzer. “Chromothripsis.” Current Biology. Elsevier, 2015. https://doi.org/10.1016/j.cub.2015.02.033."},"user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","external_id":{"pmid":["25989073"]},"article_processing_charge":"No","author":[{"first_name":"Emily M.","last_name":"Hatch","full_name":"Hatch, Emily M."},{"id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","first_name":"Martin W","full_name":"HETZER, Martin W","orcid":"0000-0002-2111-992X","last_name":"HETZER"}],"title":"Chromothripsis","oa":1,"publisher":"Elsevier","quality_controlled":"1","year":"2015","publication":"Current Biology","day":"18","page":"PR397-R399","date_created":"2022-04-07T07:49:00Z","date_published":"2015-05-18T00:00:00Z","doi":"10.1016/j.cub.2015.02.033"},{"extern":"1","date_updated":"2022-07-18T08:44:33Z","_id":"11080","status":"public","keyword":["General Biochemistry","Genetics and Molecular Biology"],"article_type":"original","type":"journal_article","language":[{"iso":"eng"}],"publication_identifier":{"issn":["0092-8674"]},"publication_status":"published","issue":"5","volume":156,"pmid":1,"oa_version":"Published Version","abstract":[{"text":"The spindle assembly checkpoint prevents separation of sister chromatids until each kinetochore is attached to the mitotic spindle. Rodriguez-Bravo et al. report that the nuclear pore complex scaffolds spindle assembly checkpoint signaling in interphase, providing a store of inhibitory signals that limits the speed of the subsequent mitosis.","lang":"eng"}],"month":"02","intvolume":" 156","scopus_import":"1","main_file_link":[{"url":"https://doi.org/10.1016/j.cell.2014.02.004","open_access":"1"}],"user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","citation":{"mla":"Buchwalter, Abigail, and Martin Hetzer. “Nuclear Pores Set the Speed Limit for Mitosis.” Cell, vol. 156, no. 5, Elsevier, 2014, pp. 868–69, doi:10.1016/j.cell.2014.02.004.","apa":"Buchwalter, A., & Hetzer, M. (2014). Nuclear pores set the speed limit for mitosis. Cell. Elsevier. https://doi.org/10.1016/j.cell.2014.02.004","ama":"Buchwalter A, Hetzer M. Nuclear pores set the speed limit for mitosis. Cell. 2014;156(5):868-869. doi:10.1016/j.cell.2014.02.004","ieee":"A. Buchwalter and M. Hetzer, “Nuclear pores set the speed limit for mitosis,” Cell, vol. 156, no. 5. Elsevier, pp. 868–869, 2014.","short":"A. Buchwalter, M. Hetzer, Cell 156 (2014) 868–869.","chicago":"Buchwalter, Abigail, and Martin Hetzer. “Nuclear Pores Set the Speed Limit for Mitosis.” Cell. Elsevier, 2014. https://doi.org/10.1016/j.cell.2014.02.004.","ista":"Buchwalter A, Hetzer M. 2014. Nuclear pores set the speed limit for mitosis. Cell. 156(5), 868–869."},"title":"Nuclear pores set the speed limit for mitosis","author":[{"first_name":"Abigail","last_name":"Buchwalter","full_name":"Buchwalter, Abigail"},{"orcid":"0000-0002-2111-992X","full_name":"HETZER, Martin W","last_name":"HETZER","first_name":"Martin W","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed"}],"external_id":{"pmid":["24581486"]},"article_processing_charge":"No","day":"27","publication":"Cell","year":"2014","doi":"10.1016/j.cell.2014.02.004","date_published":"2014-02-27T00:00:00Z","date_created":"2022-04-07T07:50:04Z","page":"868-869","publisher":"Elsevier","quality_controlled":"1","oa":1},{"volume":25,"issue":"16","publication_status":"published","publication_identifier":{"issn":["1059-1524","1939-4586"]},"language":[{"iso":"eng"}],"main_file_link":[{"url":"https://doi.org/10.1091/mbc.e14-04-0865","open_access":"1"}],"scopus_import":"1","intvolume":" 25","month":"08","abstract":[{"text":"The nuclear pore complex (NPC) plays a critical role in gene expression by mediating import of transcription regulators into the nucleus and export of RNA transcripts to the cytoplasm. Emerging evidence suggests that in addition to mediating transport, a subset of nucleoporins (Nups) engage in transcriptional activation and elongation at genomic loci that are not associated with NPCs. The underlying mechanism and regulation of Nup mobility on and off nuclear pores remain unclear. Here we show that Nup50 is a mobile Nup with a pronounced presence both at the NPC and in the nucleoplasm that can move between these different localizations. Strikingly, the dynamic behavior of Nup50 in both locations is dependent on active transcription by RNA polymerase II and requires the N-terminal half of the protein, which contains importin α– and Nup153-binding domains. However, Nup50 dynamics are independent of importin α, Nup153, and Nup98, even though the latter two proteins also exhibit transcription-dependent mobility. Of interest, depletion of Nup50 from C2C12 myoblasts does not affect cell proliferation but inhibits differentiation into myotubes. Taken together, our results suggest a transport-independent role for Nup50 in chromatin biology that occurs away from the NPC.","lang":"eng"}],"oa_version":"Published Version","date_updated":"2022-07-18T08:45:20Z","extern":"1","type":"journal_article","article_type":"original","keyword":["Cell Biology","Molecular Biology"],"status":"public","_id":"11082","page":"2472-2484","date_created":"2022-04-07T07:50:24Z","doi":"10.1091/mbc.e14-04-0865","date_published":"2014-08-15T00:00:00Z","year":"2014","publication":"Molecular Biology of the Cell","day":"15","oa":1,"quality_controlled":"1","publisher":"American Society for Cell Biology","article_processing_charge":"No","author":[{"first_name":"Abigail L.","full_name":"Buchwalter, Abigail L.","last_name":"Buchwalter"},{"full_name":"Liang, Yun","last_name":"Liang","first_name":"Yun"},{"last_name":"HETZER","orcid":"0000-0002-2111-992X","full_name":"HETZER, Martin W","first_name":"Martin W","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed"}],"title":"Nup50 is required for cell differentiation and exhibits transcription-dependent dynamics","citation":{"chicago":"Buchwalter, Abigail L., Yun Liang, and Martin Hetzer. “Nup50 Is Required for Cell Differentiation and Exhibits Transcription-Dependent Dynamics.” Molecular Biology of the Cell. American Society for Cell Biology, 2014. https://doi.org/10.1091/mbc.e14-04-0865.","ista":"Buchwalter AL, Liang Y, Hetzer M. 2014. Nup50 is required for cell differentiation and exhibits transcription-dependent dynamics. Molecular Biology of the Cell. 25(16), 2472–2484.","mla":"Buchwalter, Abigail L., et al. “Nup50 Is Required for Cell Differentiation and Exhibits Transcription-Dependent Dynamics.” Molecular Biology of the Cell, vol. 25, no. 16, American Society for Cell Biology, 2014, pp. 2472–84, doi:10.1091/mbc.e14-04-0865.","ama":"Buchwalter AL, Liang Y, Hetzer M. Nup50 is required for cell differentiation and exhibits transcription-dependent dynamics. Molecular Biology of the Cell. 2014;25(16):2472-2484. doi:10.1091/mbc.e14-04-0865","apa":"Buchwalter, A. L., Liang, Y., & Hetzer, M. (2014). Nup50 is required for cell differentiation and exhibits transcription-dependent dynamics. Molecular Biology of the Cell. American Society for Cell Biology. https://doi.org/10.1091/mbc.e14-04-0865","ieee":"A. L. Buchwalter, Y. Liang, and M. Hetzer, “Nup50 is required for cell differentiation and exhibits transcription-dependent dynamics,” Molecular Biology of the Cell, vol. 25, no. 16. American Society for Cell Biology, pp. 2472–2484, 2014.","short":"A.L. Buchwalter, Y. Liang, M. Hetzer, Molecular Biology of the Cell 25 (2014) 2472–2484."},"user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd"},{"year":"2014","publication":"Journal of Cell Biology","day":"21","page":"133-141","date_created":"2022-04-07T07:50:13Z","date_published":"2014-04-21T00:00:00Z","doi":"10.1083/jcb.201402003","oa":1,"publisher":"Rockefeller University Press","quality_controlled":"1","citation":{"apa":"Hatch, E., & Hetzer, M. (2014). Breaching the nuclear envelope in development and disease. Journal of Cell Biology. Rockefeller University Press. https://doi.org/10.1083/jcb.201402003","ama":"Hatch E, Hetzer M. Breaching the nuclear envelope in development and disease. Journal of Cell Biology. 2014;205(2):133-141. doi:10.1083/jcb.201402003","ieee":"E. Hatch and M. Hetzer, “Breaching the nuclear envelope in development and disease,” Journal of Cell Biology, vol. 205, no. 2. Rockefeller University Press, pp. 133–141, 2014.","short":"E. Hatch, M. Hetzer, Journal of Cell Biology 205 (2014) 133–141.","mla":"Hatch, Emily, and Martin Hetzer. “Breaching the Nuclear Envelope in Development and Disease.” Journal of Cell Biology, vol. 205, no. 2, Rockefeller University Press, 2014, pp. 133–41, doi:10.1083/jcb.201402003.","ista":"Hatch E, Hetzer M. 2014. Breaching the nuclear envelope in development and disease. Journal of Cell Biology. 205(2), 133–141.","chicago":"Hatch, Emily, and Martin Hetzer. “Breaching the Nuclear Envelope in Development and Disease.” Journal of Cell Biology. Rockefeller University Press, 2014. https://doi.org/10.1083/jcb.201402003."},"user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","external_id":{"pmid":["24751535"]},"article_processing_charge":"No","author":[{"full_name":"Hatch, Emily","last_name":"Hatch","first_name":"Emily"},{"orcid":"0000-0002-2111-992X","full_name":"HETZER, Martin W","last_name":"HETZER","first_name":"Martin W","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed"}],"title":"Breaching the nuclear envelope in development and disease","publication_status":"published","publication_identifier":{"issn":["1540-8140","0021-9525"]},"language":[{"iso":"eng"}],"volume":205,"issue":"2","abstract":[{"lang":"eng","text":"In eukaryotic cells the nuclear genome is enclosed by the nuclear envelope (NE). In metazoans, the NE breaks down in mitosis and it has been assumed that the physical barrier separating nucleoplasm and cytoplasm remains intact during the rest of the cell cycle and cell differentiation. However, recent studies suggest that nonmitotic NE remodeling plays a critical role in development, virus infection, laminopathies, and cancer. Although the mechanisms underlying these NE restructuring events are currently being defined, one common theme is activation of protein kinase C family members in the interphase nucleus to disrupt the nuclear lamina, demonstrating the importance of the lamina in maintaining nuclear integrity."}],"oa_version":"Published Version","pmid":1,"main_file_link":[{"open_access":"1","url":"https://doi.org/10.1083/jcb.201402003"}],"scopus_import":"1","intvolume":" 205","month":"04","date_updated":"2022-07-18T08:45:09Z","extern":"1","_id":"11081","type":"journal_article","article_type":"review","keyword":["Cell Biology"],"status":"public"},{"article_number":"e1003308","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","citation":{"ama":"Liang Y, Franks TM, Marchetto MC, Gage FH, Hetzer M. Dynamic association of NUP98 with the human genome. PLoS Genetics. 2013;9(2). doi:10.1371/journal.pgen.1003308","apa":"Liang, Y., Franks, T. M., Marchetto, M. C., Gage, F. H., & Hetzer, M. (2013). Dynamic association of NUP98 with the human genome. PLoS Genetics. Public Library of Science. https://doi.org/10.1371/journal.pgen.1003308","short":"Y. Liang, T.M. Franks, M.C. Marchetto, F.H. Gage, M. Hetzer, PLoS Genetics 9 (2013).","ieee":"Y. Liang, T. M. Franks, M. C. Marchetto, F. H. Gage, and M. Hetzer, “Dynamic association of NUP98 with the human genome,” PLoS Genetics, vol. 9, no. 2. Public Library of Science, 2013.","mla":"Liang, Yun, et al. “Dynamic Association of NUP98 with the Human Genome.” PLoS Genetics, vol. 9, no. 2, e1003308, Public Library of Science, 2013, doi:10.1371/journal.pgen.1003308.","ista":"Liang Y, Franks TM, Marchetto MC, Gage FH, Hetzer M. 2013. Dynamic association of NUP98 with the human genome. PLoS Genetics. 9(2), e1003308.","chicago":"Liang, Yun, Tobias M. Franks, Maria C. Marchetto, Fred H. Gage, and Martin Hetzer. “Dynamic Association of NUP98 with the Human Genome.” PLoS Genetics. Public Library of Science, 2013. https://doi.org/10.1371/journal.pgen.1003308."},"title":"Dynamic association of NUP98 with the human genome","article_processing_charge":"No","external_id":{"pmid":["23468646"]},"author":[{"full_name":"Liang, Yun","last_name":"Liang","first_name":"Yun"},{"first_name":"Tobias M.","full_name":"Franks, Tobias M.","last_name":"Franks"},{"last_name":"Marchetto","full_name":"Marchetto, Maria C.","first_name":"Maria C."},{"last_name":"Gage","full_name":"Gage, Fred H.","first_name":"Fred H."},{"first_name":"Martin W","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","last_name":"HETZER","orcid":"0000-0002-2111-992X","full_name":"HETZER, Martin W"}],"oa":1,"quality_controlled":"1","publisher":"Public Library of Science","publication":"PLoS Genetics","day":"28","year":"2013","date_created":"2022-04-07T07:50:59Z","doi":"10.1371/journal.pgen.1003308","date_published":"2013-02-28T00:00:00Z","_id":"11086","keyword":["Cancer Research","Genetics (clinical)","Genetics","Molecular Biology","Ecology","Evolution","Behavior and Systematics"],"status":"public","article_type":"original","type":"journal_article","extern":"1","date_updated":"2022-07-18T08:45:58Z","oa_version":"Published Version","pmid":1,"abstract":[{"lang":"eng","text":"Faithful execution of developmental gene expression programs occurs at multiple levels and involves many different components such as transcription factors, histone-modification enzymes, and mRNA processing proteins. Recent evidence suggests that nucleoporins, well known components that control nucleo-cytoplasmic trafficking, have wide-ranging functions in developmental gene regulation that potentially extend beyond their role in nuclear transport. Whether the unexpected role of nuclear pore proteins in transcription regulation, which initially has been described in fungi and flies, also applies to human cells is unknown. Here we show at a genome-wide level that the nuclear pore protein NUP98 associates with developmentally regulated genes active during human embryonic stem cell differentiation. Overexpression of a dominant negative fragment of NUP98 levels decreases expression levels of NUP98-bound genes. In addition, we identify two modes of developmental gene regulation by NUP98 that are differentiated by the spatial localization of NUP98 target genes. Genes in the initial stage of developmental induction can associate with NUP98 that is embedded in the nuclear pores at the nuclear periphery. Alternatively, genes that are highly induced can interact with NUP98 in the nuclear interior, away from the nuclear pores. This work demonstrates for the first time that NUP98 dynamically associates with the human genome during differentiation, revealing a role of a nuclear pore protein in regulating developmental gene expression programs."}],"intvolume":" 9","month":"02","main_file_link":[{"url":"https://doi.org/10.1371/journal.pgen.1003308","open_access":"1"}],"scopus_import":"1","language":[{"iso":"eng"}],"publication_status":"published","publication_identifier":{"issn":["1553-7404"]},"issue":"2","volume":9},{"date_created":"2022-04-07T07:51:08Z","doi":"10.1016/j.cell.2013.07.037","date_published":"2013-08-29T00:00:00Z","page":"971-982","publication":"Cell","day":"29","year":"2013","oa":1,"quality_controlled":"1","publisher":"Elsevier","title":"Identification of long-lived proteins reveals exceptional stability of essential cellular structures","article_processing_charge":"No","external_id":{"pmid":["23993091"]},"author":[{"last_name":"Toyama","full_name":"Toyama, Brandon H.","first_name":"Brandon H."},{"first_name":"Jeffrey N.","last_name":"Savas","full_name":"Savas, Jeffrey N."},{"last_name":"Park","full_name":"Park, Sung Kyu","first_name":"Sung Kyu"},{"first_name":"Michael S.","full_name":"Harris, Michael S.","last_name":"Harris"},{"last_name":"Ingolia","full_name":"Ingolia, Nicholas T.","first_name":"Nicholas T."},{"first_name":"John R.","full_name":"Yates, John R.","last_name":"Yates"},{"id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","first_name":"Martin W","last_name":"HETZER","orcid":"0000-0002-2111-992X","full_name":"HETZER, Martin W"}],"user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","citation":{"ista":"Toyama BH, Savas JN, Park SK, Harris MS, Ingolia NT, Yates JR, Hetzer M. 2013. Identification of long-lived proteins reveals exceptional stability of essential cellular structures. Cell. 154(5), 971–982.","chicago":"Toyama, Brandon H., Jeffrey N. Savas, Sung Kyu Park, Michael S. Harris, Nicholas T. Ingolia, John R. Yates, and Martin Hetzer. “Identification of Long-Lived Proteins Reveals Exceptional Stability of Essential Cellular Structures.” Cell. Elsevier, 2013. https://doi.org/10.1016/j.cell.2013.07.037.","short":"B.H. Toyama, J.N. Savas, S.K. Park, M.S. Harris, N.T. Ingolia, J.R. Yates, M. Hetzer, Cell 154 (2013) 971–982.","ieee":"B. H. Toyama et al., “Identification of long-lived proteins reveals exceptional stability of essential cellular structures,” Cell, vol. 154, no. 5. Elsevier, pp. 971–982, 2013.","apa":"Toyama, B. H., Savas, J. N., Park, S. K., Harris, M. S., Ingolia, N. T., Yates, J. R., & Hetzer, M. (2013). Identification of long-lived proteins reveals exceptional stability of essential cellular structures. Cell. Elsevier. https://doi.org/10.1016/j.cell.2013.07.037","ama":"Toyama BH, Savas JN, Park SK, et al. Identification of long-lived proteins reveals exceptional stability of essential cellular structures. Cell. 2013;154(5):971-982. doi:10.1016/j.cell.2013.07.037","mla":"Toyama, Brandon H., et al. “Identification of Long-Lived Proteins Reveals Exceptional Stability of Essential Cellular Structures.” Cell, vol. 154, no. 5, Elsevier, 2013, pp. 971–82, doi:10.1016/j.cell.2013.07.037."},"volume":154,"issue":"5","language":[{"iso":"eng"}],"publication_status":"published","publication_identifier":{"issn":["0092-8674"]},"intvolume":" 154","month":"08","main_file_link":[{"open_access":"1","url":"https://doi.org/10.1016/j.cell.2013.07.037"}],"scopus_import":"1","pmid":1,"oa_version":"Published Version","abstract":[{"text":"Intracellular proteins with long lifespans have recently been linked to age-dependent defects, ranging from decreased fertility to the functional decline of neurons. Why long-lived proteins exist in metabolically active cellular environments and how they are maintained over time remains poorly understood. Here, we provide a system-wide identification of proteins with exceptional lifespans in the rat brain. These proteins are inefficiently replenished despite being translated robustly throughout adulthood. Using nucleoporins as a paradigm for long-term protein persistence, we found that nuclear pore complexes (NPCs) are maintained over a cell’s life through slow but finite exchange of even its most stable subcomplexes. This maintenance is limited, however, as some nucleoporin levels decrease during aging, providing a rationale for the previously observed age-dependent deterioration of NPC function. Our identification of a long-lived proteome reveals cellular components that are at increased risk for damage accumulation, linking long-term protein persistence to the cellular aging process.","lang":"eng"}],"extern":"1","date_updated":"2022-07-18T08:50:47Z","keyword":["General Biochemistry","Genetics and Molecular Biology"],"status":"public","article_type":"original","type":"journal_article","_id":"11087"},{"user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","citation":{"ista":"Hatch EM, Fischer AH, Deerinck TJ, Hetzer M. 2013. Catastrophic nuclear envelope collapse in cancer cell micronuclei. Cell. 154(1), 47–60.","chicago":"Hatch, Emily M., Andrew H. Fischer, Thomas J. Deerinck, and Martin Hetzer. “Catastrophic Nuclear Envelope Collapse in Cancer Cell Micronuclei.” Cell. Elsevier, 2013. https://doi.org/10.1016/j.cell.2013.06.007.","ama":"Hatch EM, Fischer AH, Deerinck TJ, Hetzer M. Catastrophic nuclear envelope collapse in cancer cell micronuclei. Cell. 2013;154(1):47-60. doi:10.1016/j.cell.2013.06.007","apa":"Hatch, E. M., Fischer, A. H., Deerinck, T. J., & Hetzer, M. (2013). Catastrophic nuclear envelope collapse in cancer cell micronuclei. Cell. Elsevier. https://doi.org/10.1016/j.cell.2013.06.007","short":"E.M. Hatch, A.H. Fischer, T.J. Deerinck, M. Hetzer, Cell 154 (2013) 47–60.","ieee":"E. M. Hatch, A. H. Fischer, T. J. Deerinck, and M. Hetzer, “Catastrophic nuclear envelope collapse in cancer cell micronuclei,” Cell, vol. 154, no. 1. Elsevier, pp. 47–60, 2013.","mla":"Hatch, Emily M., et al. “Catastrophic Nuclear Envelope Collapse in Cancer Cell Micronuclei.” Cell, vol. 154, no. 1, Elsevier, 2013, pp. 47–60, doi:10.1016/j.cell.2013.06.007."},"title":"Catastrophic nuclear envelope collapse in cancer cell micronuclei","external_id":{"pmid":["23827674"]},"article_processing_charge":"No","author":[{"last_name":"Hatch","full_name":"Hatch, Emily M.","first_name":"Emily M."},{"full_name":"Fischer, Andrew H.","last_name":"Fischer","first_name":"Andrew H."},{"first_name":"Thomas J.","last_name":"Deerinck","full_name":"Deerinck, Thomas J."},{"last_name":"HETZER","orcid":"0000-0002-2111-992X","full_name":"HETZER, Martin W","first_name":"Martin W","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed"}],"oa":1,"publisher":"Elsevier","quality_controlled":"1","publication":"Cell","day":"03","year":"2013","date_created":"2022-04-07T07:50:51Z","date_published":"2013-07-03T00:00:00Z","doi":"10.1016/j.cell.2013.06.007","page":"47-60","_id":"11085","keyword":["General Biochemistry","Genetics and Molecular Biology"],"status":"public","article_type":"original","type":"journal_article","extern":"1","date_updated":"2022-07-18T08:45:47Z","pmid":1,"oa_version":"Published Version","abstract":[{"text":"During mitotic exit, missegregated chromosomes can recruit their own nuclear envelope (NE) to form micronuclei (MN). MN have reduced functioning compared to primary nuclei in the same cell, although the two compartments appear to be structurally comparable. Here we show that over 60% of MN undergo an irreversible loss of compartmentalization during interphase due to NE collapse. This disruption of the MN, which is induced by defects in nuclear lamina assembly, drastically reduces nuclear functions and can trigger massive DNA damage. MN disruption is associated with chromatin compaction and invasion of endoplasmic reticulum (ER) tubules into the chromatin. We identified disrupted MN in both major subtypes of human non-small-cell lung cancer, suggesting that disrupted MN could be a useful objective biomarker for genomic instability in solid tumors. Our study shows that NE collapse is a key event underlying MN dysfunction and establishes a link between aberrant NE organization and aneuploidy.","lang":"eng"}],"intvolume":" 154","month":"07","main_file_link":[{"url":"https://doi.org/10.1016/j.cell.2013.06.007","open_access":"1"}],"scopus_import":"1","language":[{"iso":"eng"}],"publication_status":"published","publication_identifier":{"issn":["0092-8674"]},"volume":154,"issue":"1"},{"author":[{"last_name":"Regner","full_name":"Regner, Benjamin M.","first_name":"Benjamin M."},{"first_name":"Dejan","last_name":"Vučinić","full_name":"Vučinić, Dejan"},{"full_name":"Domnisoru, Cristina","last_name":"Domnisoru","first_name":"Cristina"},{"first_name":"Thomas M.","full_name":"Bartol, Thomas M.","last_name":"Bartol"},{"id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","first_name":"Martin W","full_name":"HETZER, Martin W","orcid":"0000-0002-2111-992X","last_name":"HETZER"},{"full_name":"Tartakovsky, Daniel M.","last_name":"Tartakovsky","first_name":"Daniel M."},{"last_name":"Sejnowski","full_name":"Sejnowski, Terrence J.","first_name":"Terrence J."}],"external_id":{"pmid":["23601312"]},"article_processing_charge":"No","title":"Anomalous diffusion of single particles in cytoplasm","citation":{"mla":"Regner, Benjamin M., et al. “Anomalous Diffusion of Single Particles in Cytoplasm.” Biophysical Journal, vol. 104, no. 8, Elsevier, 2013, pp. 1652–60, doi:10.1016/j.bpj.2013.01.049.","ieee":"B. M. Regner et al., “Anomalous diffusion of single particles in cytoplasm,” Biophysical Journal, vol. 104, no. 8. Elsevier, pp. 1652–1660, 2013.","short":"B.M. Regner, D. Vučinić, C. Domnisoru, T.M. Bartol, M. Hetzer, D.M. Tartakovsky, T.J. Sejnowski, Biophysical Journal 104 (2013) 1652–1660.","ama":"Regner BM, Vučinić D, Domnisoru C, et al. Anomalous diffusion of single particles in cytoplasm. Biophysical Journal. 2013;104(8):1652-1660. doi:10.1016/j.bpj.2013.01.049","apa":"Regner, B. M., Vučinić, D., Domnisoru, C., Bartol, T. M., Hetzer, M., Tartakovsky, D. M., & Sejnowski, T. J. (2013). Anomalous diffusion of single particles in cytoplasm. Biophysical Journal. Elsevier. https://doi.org/10.1016/j.bpj.2013.01.049","chicago":"Regner, Benjamin M., Dejan Vučinić, Cristina Domnisoru, Thomas M. Bartol, Martin Hetzer, Daniel M. Tartakovsky, and Terrence J. Sejnowski. “Anomalous Diffusion of Single Particles in Cytoplasm.” Biophysical Journal. Elsevier, 2013. https://doi.org/10.1016/j.bpj.2013.01.049.","ista":"Regner BM, Vučinić D, Domnisoru C, Bartol TM, Hetzer M, Tartakovsky DM, Sejnowski TJ. 2013. Anomalous diffusion of single particles in cytoplasm. Biophysical Journal. 104(8), 1652–1660."},"user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","page":"1652-1660","doi":"10.1016/j.bpj.2013.01.049","date_published":"2013-04-16T00:00:00Z","date_created":"2022-04-07T07:51:26Z","year":"2013","day":"16","publication":"Biophysical Journal","quality_controlled":"1","publisher":"Elsevier","oa":1,"date_updated":"2022-07-18T08:51:01Z","extern":"1","type":"journal_article","article_type":"original","status":"public","keyword":["Biophysics"],"_id":"11088","issue":"8","volume":104,"publication_identifier":{"issn":["0006-3495"]},"publication_status":"published","language":[{"iso":"eng"}],"scopus_import":"1","main_file_link":[{"open_access":"1","url":"https://doi.org/10.1016/j.bpj.2013.01.049"}],"month":"04","intvolume":" 104","abstract":[{"text":"The crowded intracellular environment poses a formidable challenge to experimental and theoretical analyses of intracellular transport mechanisms. Our measurements of single-particle trajectories in cytoplasm and their random-walk interpretations elucidate two of these mechanisms: molecular diffusion in crowded environments and cytoskeletal transport along microtubules. We employed acousto-optic deflector microscopy to map out the three-dimensional trajectories of microspheres migrating in the cytosolic fraction of a cellular extract. Classical Brownian motion (BM), continuous time random walk, and fractional BM were alternatively used to represent these trajectories. The comparison of the experimental and numerical data demonstrates that cytoskeletal transport along microtubules and diffusion in the cytosolic fraction exhibit anomalous (nonFickian) behavior and posses statistically distinct signatures. Among the three random-walk models used, continuous time random walk provides the best representation of diffusion, whereas microtubular transport is accurately modeled with fractional BM.","lang":"eng"}],"oa_version":"Published Version","pmid":1},{"publication":"Trends in Cell Biology","day":"01","year":"2013","date_created":"2022-04-07T07:50:33Z","date_published":"2013-03-01T00:00:00Z","doi":"10.1016/j.tcb.2012.10.013","page":"112-117","quality_controlled":"1","publisher":"Elsevier","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","citation":{"ista":"Franks TM, Hetzer M. 2013. The role of Nup98 in transcription regulation in healthy and diseased cells. Trends in Cell Biology. 23(3), 112–117.","chicago":"Franks, Tobias M., and Martin Hetzer. “The Role of Nup98 in Transcription Regulation in Healthy and Diseased Cells.” Trends in Cell Biology. Elsevier, 2013. https://doi.org/10.1016/j.tcb.2012.10.013.","apa":"Franks, T. M., & Hetzer, M. (2013). The role of Nup98 in transcription regulation in healthy and diseased cells. Trends in Cell Biology. Elsevier. https://doi.org/10.1016/j.tcb.2012.10.013","ama":"Franks TM, Hetzer M. The role of Nup98 in transcription regulation in healthy and diseased cells. Trends in Cell Biology. 2013;23(3):112-117. doi:10.1016/j.tcb.2012.10.013","short":"T.M. Franks, M. Hetzer, Trends in Cell Biology 23 (2013) 112–117.","ieee":"T. M. Franks and M. Hetzer, “The role of Nup98 in transcription regulation in healthy and diseased cells,” Trends in Cell Biology, vol. 23, no. 3. Elsevier, pp. 112–117, 2013.","mla":"Franks, Tobias M., and Martin Hetzer. “The Role of Nup98 in Transcription Regulation in Healthy and Diseased Cells.” Trends in Cell Biology, vol. 23, no. 3, Elsevier, 2013, pp. 112–17, doi:10.1016/j.tcb.2012.10.013."},"title":"The role of Nup98 in transcription regulation in healthy and diseased cells","external_id":{"pmid":["23246429"]},"article_processing_charge":"No","author":[{"full_name":"Franks, Tobias M.","last_name":"Franks","first_name":"Tobias M."},{"full_name":"HETZER, Martin W","orcid":"0000-0002-2111-992X","last_name":"HETZER","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","first_name":"Martin W"}],"language":[{"iso":"eng"}],"publication_status":"published","publication_identifier":{"issn":["0962-8924"]},"issue":"3","volume":23,"oa_version":"None","pmid":1,"abstract":[{"lang":"eng","text":"Nuclear pore complex (NPC) proteins are known for their critical roles in regulating nucleocytoplasmic traffic of macromolecules across the nuclear envelope. However, recent findings suggest that some nucleoporins (Nups), including Nup98, have additional functions in developmental gene regulation. Nup98, which exhibits transcription-dependent mobility at the NPC but can also bind chromatin away from the nuclear envelope, is frequently involved in chromosomal translocations in a subset of patients suffering from acute myeloid leukemia (AML). A common paradigm suggests that Nup98 translocations cause aberrant transcription when they are recuited to aberrant genomic loci. Importantly, this model fails to account for the potential loss of wild type (WT) Nup98 function in the presence of Nup98 translocation mutants. Here we examine how the cell might regulate Nup98 nucleoplasmic protein levels to control transcription in healthy cells. In addition, we discuss the possibility that dominant negative Nup98 fusion proteins disrupt the transcriptional activity of WT Nup98 in the nucleoplasm to drive AML."}],"intvolume":" 23","month":"03","scopus_import":"1","extern":"1","date_updated":"2022-07-18T08:45:34Z","_id":"11083","keyword":["Cell Biology"],"status":"public","type":"journal_article","article_type":"letter_note"},{"author":[{"full_name":"Toyama, Brandon H.","last_name":"Toyama","first_name":"Brandon H."},{"last_name":"HETZER","full_name":"HETZER, Martin W","orcid":"0000-0002-2111-992X","first_name":"Martin W","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed"}],"article_processing_charge":"No","external_id":{"pmid":["23258296"]},"title":"Protein homeostasis: Live long, won't prosper","citation":{"chicago":"Toyama, Brandon H., and Martin Hetzer. “Protein Homeostasis: Live Long, Won’t Prosper.” Nature Reviews Molecular Cell Biology. Springer Nature, 2013. https://doi.org/10.1038/nrm3496.","ista":"Toyama BH, Hetzer M. 2013. Protein homeostasis: Live long, won’t prosper. Nature Reviews Molecular Cell Biology. 14, 55–61.","mla":"Toyama, Brandon H., and Martin Hetzer. “Protein Homeostasis: Live Long, Won’t Prosper.” Nature Reviews Molecular Cell Biology, vol. 14, Springer Nature, 2013, pp. 55–61, doi:10.1038/nrm3496.","ieee":"B. H. Toyama and M. Hetzer, “Protein homeostasis: Live long, won’t prosper,” Nature Reviews Molecular Cell Biology, vol. 14. Springer Nature, pp. 55–61, 2013.","short":"B.H. Toyama, M. Hetzer, Nature Reviews Molecular Cell Biology 14 (2013) 55–61.","apa":"Toyama, B. H., & Hetzer, M. (2013). Protein homeostasis: Live long, won’t prosper. Nature Reviews Molecular Cell Biology. Springer Nature. https://doi.org/10.1038/nrm3496","ama":"Toyama BH, Hetzer M. Protein homeostasis: Live long, won’t prosper. Nature Reviews Molecular Cell Biology. 2013;14:55-61. doi:10.1038/nrm3496"},"user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","page":"55-61","date_published":"2013-01-01T00:00:00Z","doi":"10.1038/nrm3496","date_created":"2022-04-07T07:50:43Z","year":"2013","day":"01","publication":"Nature Reviews Molecular Cell Biology","quality_controlled":"1","publisher":"Springer Nature","date_updated":"2022-07-18T08:37:53Z","extern":"1","article_type":"original","type":"journal_article","status":"public","keyword":["Cell Biology","Molecular Biology"],"_id":"11084","volume":14,"publication_identifier":{"issn":["1471-0072","1471-0080"]},"publication_status":"published","language":[{"iso":"eng"}],"scopus_import":"1","month":"01","intvolume":" 14","abstract":[{"text":"Protein turnover is an effective way of maintaining a functional proteome, as old and potentially damaged polypeptides are destroyed and replaced by newly synthesized copies. An increasing number of intracellular proteins, however, have been identified that evade this turnover process and instead are maintained over a cell's lifetime. This diverse group of long-lived proteins might be particularly prone to accumulation of damage and thus have a crucial role in the functional deterioration of key regulatory processes during ageing.","lang":"eng"}],"pmid":1,"oa_version":"None"},{"keyword":["Cell Biology"],"status":"public","type":"journal_article","article_type":"original","_id":"11089","extern":"1","date_updated":"2022-07-18T08:38:47Z","intvolume":" 24","month":"12","scopus_import":"1","oa_version":"None","pmid":1,"abstract":[{"lang":"eng","text":"The Nuclear Envelope (NE) contains over 100 different proteins that associate with nuclear components such as chromatin, the lamina and the transcription machinery. Mutations in genes encoding NE proteins have been shown to result in tissue-specific defects and disease, suggesting cell-type specific differences in NE composition and function. Consistent with these observations, recent studies have revealed unexpected functions for numerous NE associated proteins during cell differentiation and development. Here we review the latest insights into the roles played by the NE in cell differentiation, development, disease and aging, focusing primarily on inner nuclear membrane (INM) proteins and nuclear pore components."}],"volume":24,"issue":"6","language":[{"iso":"eng"}],"publication_status":"published","publication_identifier":{"issn":["0955-0674"]},"title":"Outfits for different occasions: tissue-specific roles of Nuclear Envelope proteins","external_id":{"pmid":["22995343"]},"article_processing_charge":"No","author":[{"full_name":"Gomez-Cavazos, J Sebastian","last_name":"Gomez-Cavazos","first_name":"J Sebastian"},{"last_name":"HETZER","orcid":"0000-0002-2111-992X","full_name":"HETZER, Martin W","first_name":"Martin W","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed"}],"user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","citation":{"ieee":"J. S. Gomez-Cavazos and M. Hetzer, “Outfits for different occasions: tissue-specific roles of Nuclear Envelope proteins,” Current Opinion in Cell Biology, vol. 24, no. 6. Elsevier, pp. 775–783, 2012.","short":"J.S. Gomez-Cavazos, M. Hetzer, Current Opinion in Cell Biology 24 (2012) 775–783.","ama":"Gomez-Cavazos JS, Hetzer M. Outfits for different occasions: tissue-specific roles of Nuclear Envelope proteins. Current Opinion in Cell Biology. 2012;24(6):775-783. doi:10.1016/j.ceb.2012.08.008","apa":"Gomez-Cavazos, J. S., & Hetzer, M. (2012). Outfits for different occasions: tissue-specific roles of Nuclear Envelope proteins. Current Opinion in Cell Biology. Elsevier. https://doi.org/10.1016/j.ceb.2012.08.008","mla":"Gomez-Cavazos, J. Sebastian, and Martin Hetzer. “Outfits for Different Occasions: Tissue-Specific Roles of Nuclear Envelope Proteins.” Current Opinion in Cell Biology, vol. 24, no. 6, Elsevier, 2012, pp. 775–83, doi:10.1016/j.ceb.2012.08.008.","ista":"Gomez-Cavazos JS, Hetzer M. 2012. Outfits for different occasions: tissue-specific roles of Nuclear Envelope proteins. Current Opinion in Cell Biology. 24(6), 775–783.","chicago":"Gomez-Cavazos, J Sebastian, and Martin Hetzer. “Outfits for Different Occasions: Tissue-Specific Roles of Nuclear Envelope Proteins.” Current Opinion in Cell Biology. Elsevier, 2012. https://doi.org/10.1016/j.ceb.2012.08.008."},"quality_controlled":"1","publisher":"Elsevier","date_created":"2022-04-07T07:51:37Z","date_published":"2012-12-01T00:00:00Z","doi":"10.1016/j.ceb.2012.08.008","page":"775-783","publication":"Current Opinion in Cell Biology","day":"01","year":"2012"},{"date_updated":"2022-07-18T08:52:53Z","extern":"1","type":"journal_article","article_type":"original","keyword":["Cell Biology"],"status":"public","_id":"11091","issue":"1","volume":3,"publication_status":"published","publication_identifier":{"eissn":["1949-1042"],"issn":["1949-1034"]},"language":[{"iso":"eng"}],"scopus_import":"1","intvolume":" 3","month":"01","abstract":[{"text":"Neoplastic cells are often characterized by specific morphological abnormalities of the nuclear envelope (NE), which have been used for cancer diagnosis for more than a century. The NE is a double phospholipid bilayer that encapsulates the nuclear genome, regulates all nuclear trafficking of RNAs and proteins and prevents the passive diffusion of macromolecules between the nucleoplasm and the cytoplasm. Whether there is a consequence to the proper functioning of the cell and loss of structural integrity of the nucleus remains unclear. Using live cell imaging, we characterize a phenomenon wherein nuclei of several proliferating human cancer cell lines become temporarily ruptured during interphase. Strikingly, NE rupturing was associated with the mislocalization of nucleoplasmic and cytoplasmic proteins and, in the most extreme cases, the entrapment of cytoplasmic organelles in the nuclear interior. In addition, we observed the formation of micronuclei-like structures during interphase and the movement of chromatin out of the nuclear space. The frequency of these NE rupturing events was higher in cells in which the nuclear lamina, a network of intermediate filaments providing mechanical support to the NE, was not properly formed. Our data uncover the existence of a NE instability that has the potential to change the genomic landscape of cancer cells.","lang":"eng"}],"pmid":1,"oa_version":"None","external_id":{"pmid":["22567193"]},"article_processing_charge":"No","author":[{"full_name":"Vargas, Jesse D.","last_name":"Vargas","first_name":"Jesse D."},{"first_name":"Emily M.","last_name":"Hatch","full_name":"Hatch, Emily M."},{"last_name":"Anderson","full_name":"Anderson, Daniel J.","first_name":"Daniel J."},{"id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","first_name":"Martin W","orcid":"0000-0002-2111-992X","full_name":"HETZER, Martin W","last_name":"HETZER"}],"title":"Transient nuclear envelope rupturing during interphase in human cancer cells","citation":{"short":"J.D. Vargas, E.M. Hatch, D.J. Anderson, M. Hetzer, Nucleus 3 (2012) 88–100.","ieee":"J. D. Vargas, E. M. Hatch, D. J. Anderson, and M. Hetzer, “Transient nuclear envelope rupturing during interphase in human cancer cells,” Nucleus, vol. 3, no. 1. Taylor & Francis, pp. 88–100, 2012.","apa":"Vargas, J. D., Hatch, E. M., Anderson, D. J., & Hetzer, M. (2012). Transient nuclear envelope rupturing during interphase in human cancer cells. Nucleus. Taylor & Francis. https://doi.org/10.4161/nucl.18954","ama":"Vargas JD, Hatch EM, Anderson DJ, Hetzer M. Transient nuclear envelope rupturing during interphase in human cancer cells. Nucleus. 2012;3(1):88-100. doi:10.4161/nucl.18954","mla":"Vargas, Jesse D., et al. “Transient Nuclear Envelope Rupturing during Interphase in Human Cancer Cells.” Nucleus, vol. 3, no. 1, Taylor & Francis, 2012, pp. 88–100, doi:10.4161/nucl.18954.","ista":"Vargas JD, Hatch EM, Anderson DJ, Hetzer M. 2012. Transient nuclear envelope rupturing during interphase in human cancer cells. Nucleus. 3(1), 88–100.","chicago":"Vargas, Jesse D., Emily M. Hatch, Daniel J. Anderson, and Martin Hetzer. “Transient Nuclear Envelope Rupturing during Interphase in Human Cancer Cells.” Nucleus. Taylor & Francis, 2012. https://doi.org/10.4161/nucl.18954."},"user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","page":"88-100","date_created":"2022-04-07T07:51:53Z","doi":"10.4161/nucl.18954","date_published":"2012-01-01T00:00:00Z","year":"2012","publication":"Nucleus","day":"01","quality_controlled":"1","publisher":"Taylor & Francis"},{"_id":"11093","article_type":"original","type":"journal_article","keyword":["Developmental Biology","Cell Biology","General Biochemistry","Genetics and Molecular Biology","Molecular Biology"],"status":"public","date_updated":"2022-07-18T08:53:16Z","extern":"1","abstract":[{"lang":"eng","text":"Nuclear pore complexes (NPCs) are built from ∼30 different proteins called nucleoporins or Nups. Previous studies have shown that several Nups exhibit cell-type-specific expression and that mutations in NPC components result in tissue-specific diseases. Here we show that a specific change in NPC composition is required for both myogenic and neuronal differentiation. The transmembrane nucleoporin Nup210 is absent in proliferating myoblasts and embryonic stem cells (ESCs) but becomes expressed and incorporated into NPCs during cell differentiation. Preventing Nup210 production by RNAi blocks myogenesis and the differentiation of ESCs into neuroprogenitors. We found that the addition of Nup210 to NPCs does not affect nuclear transport but is required for the induction of genes that are essential for cell differentiation. Our results identify a single change in NPC composition as an essential step in cell differentiation and establish a role for Nup210 in gene expression regulation and cell fate determination."}],"pmid":1,"oa_version":"Published Version","main_file_link":[{"url":"https://doi.org/10.1016/j.devcel.2011.11.021","open_access":"1"}],"scopus_import":"1","intvolume":" 22","month":"01","publication_status":"published","publication_identifier":{"issn":["1534-5807"]},"language":[{"iso":"eng"}],"issue":"2","volume":22,"citation":{"ama":"D’Angelo MA, Gomez-Cavazos JS, Mei A, Lackner DH, Hetzer M. A change in nuclear pore complex composition regulates cell differentiation. Developmental Cell. 2012;22(2):446-458. doi:10.1016/j.devcel.2011.11.021","apa":"D’Angelo, M. A., Gomez-Cavazos, J. S., Mei, A., Lackner, D. H., & Hetzer, M. (2012). A change in nuclear pore complex composition regulates cell differentiation. Developmental Cell. Elsevier. https://doi.org/10.1016/j.devcel.2011.11.021","short":"M.A. D’Angelo, J.S. Gomez-Cavazos, A. Mei, D.H. Lackner, M. Hetzer, Developmental Cell 22 (2012) 446–458.","ieee":"M. A. D’Angelo, J. S. Gomez-Cavazos, A. Mei, D. H. Lackner, and M. Hetzer, “A change in nuclear pore complex composition regulates cell differentiation,” Developmental Cell, vol. 22, no. 2. Elsevier, pp. 446–458, 2012.","mla":"D’Angelo, Maximiliano A., et al. “A Change in Nuclear Pore Complex Composition Regulates Cell Differentiation.” Developmental Cell, vol. 22, no. 2, Elsevier, 2012, pp. 446–58, doi:10.1016/j.devcel.2011.11.021.","ista":"D’Angelo MA, Gomez-Cavazos JS, Mei A, Lackner DH, Hetzer M. 2012. A change in nuclear pore complex composition regulates cell differentiation. Developmental Cell. 22(2), 446–458.","chicago":"D’Angelo, Maximiliano A., J. Sebastian Gomez-Cavazos, Arianna Mei, Daniel H. Lackner, and Martin Hetzer. “A Change in Nuclear Pore Complex Composition Regulates Cell Differentiation.” Developmental Cell. Elsevier, 2012. https://doi.org/10.1016/j.devcel.2011.11.021."},"user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","article_processing_charge":"No","external_id":{"pmid":["22264802"]},"author":[{"full_name":"D'Angelo, Maximiliano A.","last_name":"D'Angelo","first_name":"Maximiliano A."},{"first_name":"J. Sebastian","last_name":"Gomez-Cavazos","full_name":"Gomez-Cavazos, J. Sebastian"},{"first_name":"Arianna","full_name":"Mei, Arianna","last_name":"Mei"},{"first_name":"Daniel H.","last_name":"Lackner","full_name":"Lackner, Daniel H."},{"id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","first_name":"Martin W","full_name":"HETZER, Martin W","orcid":"0000-0002-2111-992X","last_name":"HETZER"}],"title":"A change in nuclear pore complex composition regulates cell differentiation","oa":1,"publisher":"Elsevier","quality_controlled":"1","year":"2012","publication":"Developmental Cell","day":"19","page":"446-458","date_created":"2022-04-07T07:52:10Z","date_published":"2012-01-19T00:00:00Z","doi":"10.1016/j.devcel.2011.11.021"},{"quality_controlled":"1","publisher":"American Association for the Advancement of Science","year":"2012","publication":"Science","day":"02","page":"942-942","date_created":"2022-04-07T07:52:01Z","doi":"10.1126/science.1217421","date_published":"2012-02-02T00:00:00Z","citation":{"mla":"Savas, Jeffrey N., et al. “Extremely Long-Lived Nuclear Pore Proteins in the Rat Brain.” Science, vol. 335, no. 6071, American Association for the Advancement of Science, 2012, pp. 942–942, doi:10.1126/science.1217421.","apa":"Savas, J. N., Toyama, B. H., Xu, T., Yates, J. R., & Hetzer, M. (2012). Extremely long-lived nuclear pore proteins in the rat brain. Science. American Association for the Advancement of Science. https://doi.org/10.1126/science.1217421","ama":"Savas JN, Toyama BH, Xu T, Yates JR, Hetzer M. Extremely long-lived nuclear pore proteins in the rat brain. Science. 2012;335(6071):942-942. doi:10.1126/science.1217421","short":"J.N. Savas, B.H. Toyama, T. Xu, J.R. Yates, M. Hetzer, Science 335 (2012) 942–942.","ieee":"J. N. Savas, B. H. Toyama, T. Xu, J. R. Yates, and M. Hetzer, “Extremely long-lived nuclear pore proteins in the rat brain,” Science, vol. 335, no. 6071. American Association for the Advancement of Science, pp. 942–942, 2012.","chicago":"Savas, Jeffrey N., Brandon H. Toyama, Tao Xu, John R. Yates, and Martin Hetzer. “Extremely Long-Lived Nuclear Pore Proteins in the Rat Brain.” Science. American Association for the Advancement of Science, 2012. https://doi.org/10.1126/science.1217421.","ista":"Savas JN, Toyama BH, Xu T, Yates JR, Hetzer M. 2012. Extremely long-lived nuclear pore proteins in the rat brain. Science. 335(6071), 942–942."},"user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","article_processing_charge":"No","external_id":{"pmid":["22300851"]},"author":[{"full_name":"Savas, Jeffrey N.","last_name":"Savas","first_name":"Jeffrey N."},{"first_name":"Brandon H.","last_name":"Toyama","full_name":"Toyama, Brandon H."},{"last_name":"Xu","full_name":"Xu, Tao","first_name":"Tao"},{"first_name":"John R.","full_name":"Yates, John R.","last_name":"Yates"},{"first_name":"Martin W","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","last_name":"HETZER","full_name":"HETZER, Martin W","orcid":"0000-0002-2111-992X"}],"title":"Extremely long-lived nuclear pore proteins in the rat brain","abstract":[{"text":"To combat the functional decline of the proteome, cells use the process of protein turnover to replace potentially impaired polypeptides with new functional copies. We found that extremely long-lived proteins (ELLPs) did not turn over in postmitotic cells of the rat central nervous system. These ELLPs were associated with chromatin and the nuclear pore complex, the central transport channels that mediate all molecular trafficking in and out of the nucleus. The longevity of these proteins would be expected to expose them to potentially harmful metabolites, putting them at risk of accumulating damage over extended periods of time. Thus, it is possible that failure to maintain proper levels and functional integrity of ELLPs in nonproliferative cells might contribute to age-related deterioration in cell and tissue function.","lang":"eng"}],"oa_version":"None","pmid":1,"scopus_import":"1","intvolume":" 335","month":"02","publication_status":"published","publication_identifier":{"issn":["0036-8075"],"eissn":["1095-9203"]},"language":[{"iso":"eng"}],"issue":"6071","volume":335,"_id":"11092","type":"journal_article","article_type":"letter_note","keyword":["Multidisciplinary"],"status":"public","date_updated":"2022-07-18T08:53:06Z","extern":"1"},{"abstract":[{"lang":"eng","text":"Nuclear export of mRNAs is thought to occur exclusively through nuclear pore complexes. In this issue of Cell, Speese et al. identify an alternate pathway for mRNA export in muscle cells where ribonucleoprotein complexes involved in forming neuromuscular junctions transit the nuclear envelope by fusing with and budding through the nuclear membrane."}],"oa_version":"Published Version","pmid":1,"main_file_link":[{"open_access":"1","url":"https://doi.org/10.1016/j.cell.2012.04.018"}],"scopus_import":"1","intvolume":" 149","month":"05","publication_status":"published","publication_identifier":{"issn":["0092-8674"]},"language":[{"iso":"eng"}],"issue":"4","volume":149,"_id":"11090","article_type":"letter_note","type":"journal_article","keyword":["General Biochemistry","Genetics and Molecular Biology"],"status":"public","date_updated":"2022-07-18T08:58:48Z","extern":"1","oa":1,"publisher":"Elsevier","quality_controlled":"1","year":"2012","publication":"Cell","day":"11","page":"733-735","date_created":"2022-04-07T07:51:45Z","doi":"10.1016/j.cell.2012.04.018","date_published":"2012-05-11T00:00:00Z","citation":{"apa":"Hatch, E. M., & Hetzer, M. (2012). RNP export by nuclear envelope budding. Cell. Elsevier. https://doi.org/10.1016/j.cell.2012.04.018","ama":"Hatch EM, Hetzer M. RNP export by nuclear envelope budding. Cell. 2012;149(4):733-735. doi:10.1016/j.cell.2012.04.018","short":"E.M. Hatch, M. Hetzer, Cell 149 (2012) 733–735.","ieee":"E. M. Hatch and M. Hetzer, “RNP export by nuclear envelope budding,” Cell, vol. 149, no. 4. Elsevier, pp. 733–735, 2012.","mla":"Hatch, Emily M., and Martin Hetzer. “RNP Export by Nuclear Envelope Budding.” Cell, vol. 149, no. 4, Elsevier, 2012, pp. 733–35, doi:10.1016/j.cell.2012.04.018.","ista":"Hatch EM, Hetzer M. 2012. RNP export by nuclear envelope budding. Cell. 149(4), 733–735.","chicago":"Hatch, Emily M., and Martin Hetzer. “RNP Export by Nuclear Envelope Budding.” Cell. Elsevier, 2012. https://doi.org/10.1016/j.cell.2012.04.018."},"user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","external_id":{"pmid":["22579277"]},"article_processing_charge":"No","author":[{"full_name":"Hatch, Emily M.","last_name":"Hatch","first_name":"Emily M."},{"last_name":"HETZER","full_name":"HETZER, Martin W","orcid":"0000-0002-2111-992X","first_name":"Martin W","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed"}],"title":"RNP export by nuclear envelope budding"},{"publication":"Journal of Cell Biology","day":"04","year":"2011","date_created":"2022-04-07T07:52:18Z","doi":"10.1083/jcb.201012154","date_published":"2011-07-04T00:00:00Z","page":"27-37","oa":1,"quality_controlled":"1","publisher":"Rockefeller University Press","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","citation":{"ieee":"J. A. Talamas and M. Hetzer, “POM121 and Sun1 play a role in early steps of interphase NPC assembly,” Journal of Cell Biology, vol. 194, no. 1. Rockefeller University Press, pp. 27–37, 2011.","short":"J.A. Talamas, M. Hetzer, Journal of Cell Biology 194 (2011) 27–37.","apa":"Talamas, J. A., & Hetzer, M. (2011). POM121 and Sun1 play a role in early steps of interphase NPC assembly. Journal of Cell Biology. Rockefeller University Press. https://doi.org/10.1083/jcb.201012154","ama":"Talamas JA, Hetzer M. POM121 and Sun1 play a role in early steps of interphase NPC assembly. Journal of Cell Biology. 2011;194(1):27-37. doi:10.1083/jcb.201012154","mla":"Talamas, Jessica A., and Martin Hetzer. “POM121 and Sun1 Play a Role in Early Steps of Interphase NPC Assembly.” Journal of Cell Biology, vol. 194, no. 1, Rockefeller University Press, 2011, pp. 27–37, doi:10.1083/jcb.201012154.","ista":"Talamas JA, Hetzer M. 2011. POM121 and Sun1 play a role in early steps of interphase NPC assembly. Journal of Cell Biology. 194(1), 27–37.","chicago":"Talamas, Jessica A., and Martin Hetzer. “POM121 and Sun1 Play a Role in Early Steps of Interphase NPC Assembly.” Journal of Cell Biology. Rockefeller University Press, 2011. https://doi.org/10.1083/jcb.201012154."},"title":"POM121 and Sun1 play a role in early steps of interphase NPC assembly","article_processing_charge":"No","external_id":{"pmid":["21727197"]},"author":[{"last_name":"Talamas","full_name":"Talamas, Jessica A.","first_name":"Jessica A."},{"id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","first_name":"Martin W","last_name":"HETZER","full_name":"HETZER, Martin W","orcid":"0000-0002-2111-992X"}],"language":[{"iso":"eng"}],"publication_status":"published","publication_identifier":{"issn":["0021-9525"],"eissn":["1540-8140"]},"volume":194,"issue":"1","oa_version":"Published Version","pmid":1,"abstract":[{"lang":"eng","text":"Nuclear pore complexes (NPCs) assemble at the end of mitosis during nuclear envelope (NE) reformation and into an intact NE as cells progress through interphase. Although recent studies have shown that NPC formation occurs by two different molecular mechanisms at two distinct cell cycle stages, little is known about the molecular players that mediate the fusion of the outer and inner nuclear membranes to form pores. In this paper, we provide evidence that the transmembrane nucleoporin (Nup), POM121, but not the Nup107–160 complex, is present at new pore assembly sites at a time that coincides with inner nuclear membrane (INM) and outer nuclear membrane (ONM) fusion. Overexpression of POM121 resulted in juxtaposition of the INM and ONM. Additionally, Sun1, an INM protein that is known to interact with the cytoskeleton, was specifically required for interphase assembly and localized with POM121 at forming pores. We propose a model in which POM121 and Sun1 interact transiently to promote early steps of interphase NPC assembly."}],"intvolume":" 194","month":"07","main_file_link":[{"open_access":"1","url":"https://doi.org/10.1083/jcb.201012154"}],"scopus_import":"1","extern":"1","date_updated":"2022-07-18T08:53:46Z","_id":"11094","keyword":["Cell Biology"],"status":"public","type":"journal_article","article_type":"original"},{"publisher":"Elsevier","quality_controlled":"1","year":"2011","publication":"Current Opinion in Cell Biology","day":"01","page":"65-70","date_created":"2022-04-07T07:52:37Z","date_published":"2011-02-01T00:00:00Z","doi":"10.1016/j.ceb.2010.09.008","citation":{"short":"Y. Liang, M. Hetzer, Current Opinion in Cell Biology 23 (2011) 65–70.","ieee":"Y. Liang and M. Hetzer, “Functional interactions between nucleoporins and chromatin,” Current Opinion in Cell Biology, vol. 23, no. 1. Elsevier, pp. 65–70, 2011.","ama":"Liang Y, Hetzer M. Functional interactions between nucleoporins and chromatin. Current Opinion in Cell Biology. 2011;23(1):65-70. doi:10.1016/j.ceb.2010.09.008","apa":"Liang, Y., & Hetzer, M. (2011). Functional interactions between nucleoporins and chromatin. Current Opinion in Cell Biology. Elsevier. https://doi.org/10.1016/j.ceb.2010.09.008","mla":"Liang, Yun, and Martin Hetzer. “Functional Interactions between Nucleoporins and Chromatin.” Current Opinion in Cell Biology, vol. 23, no. 1, Elsevier, 2011, pp. 65–70, doi:10.1016/j.ceb.2010.09.008.","ista":"Liang Y, Hetzer M. 2011. Functional interactions between nucleoporins and chromatin. Current Opinion in Cell Biology. 23(1), 65–70.","chicago":"Liang, Yun, and Martin Hetzer. “Functional Interactions between Nucleoporins and Chromatin.” Current Opinion in Cell Biology. Elsevier, 2011. https://doi.org/10.1016/j.ceb.2010.09.008."},"user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","article_processing_charge":"No","external_id":{"pmid":["21030234"]},"author":[{"first_name":"Yun","full_name":"Liang, Yun","last_name":"Liang"},{"first_name":"Martin W","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","full_name":"HETZER, Martin W","orcid":"0000-0002-2111-992X","last_name":"HETZER"}],"title":"Functional interactions between nucleoporins and chromatin","abstract":[{"lang":"eng","text":"As the gatekeepers of the eukaryotic cell nucleus, nuclear pore complexes (NPCs) mediate all molecular trafficking between the nucleoplasm and the cytoplasm. In recent years, transport-independent functions of NPC components, nucleoporins, have been identified including roles in chromatin organization and gene regulation. Here, we summarize our current view of the NPC as a dynamic hub for the integration of chromatin regulation and nuclear trafficking and discuss the functional interplay between nucleoporins and the nuclear genome."}],"pmid":1,"oa_version":"None","scopus_import":"1","intvolume":" 23","month":"02","publication_status":"published","publication_identifier":{"issn":["0955-0674"]},"language":[{"iso":"eng"}],"volume":23,"issue":"1","_id":"11096","article_type":"original","type":"journal_article","keyword":["Cell Biology"],"status":"public","date_updated":"2022-07-18T08:53:48Z","extern":"1"},{"article_type":"letter_note","type":"journal_article","status":"public","keyword":["Cell Biology"],"_id":"11095","date_updated":"2022-07-18T08:39:40Z","extern":"1","scopus_import":"1","month":"06","intvolume":" 23","oa_version":"None","pmid":1,"issue":"3","volume":23,"publication_identifier":{"issn":["0955-0674"]},"publication_status":"published","language":[{"iso":"eng"}],"author":[{"orcid":"0000-0002-2111-992X","full_name":"HETZER, Martin W","last_name":"HETZER","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","first_name":"Martin W"},{"first_name":"Giacomo","last_name":"Cavalli","full_name":"Cavalli, Giacomo"}],"external_id":{"pmid":["21592757"]},"article_processing_charge":"No","title":"Editorial overview","citation":{"chicago":"Hetzer, Martin, and Giacomo Cavalli. “Editorial Overview.” Current Opinion in Cell Biology. Elsevier, 2011. https://doi.org/10.1016/j.ceb.2011.04.013.","ista":"Hetzer M, Cavalli G. 2011. Editorial overview. Current Opinion in Cell Biology. 23(3), 255–257.","mla":"Hetzer, Martin, and Giacomo Cavalli. “Editorial Overview.” Current Opinion in Cell Biology, vol. 23, no. 3, Elsevier, 2011, pp. 255–57, doi:10.1016/j.ceb.2011.04.013.","ieee":"M. Hetzer and G. Cavalli, “Editorial overview,” Current Opinion in Cell Biology, vol. 23, no. 3. Elsevier, pp. 255–257, 2011.","short":"M. Hetzer, G. Cavalli, Current Opinion in Cell Biology 23 (2011) 255–257.","apa":"Hetzer, M., & Cavalli, G. (2011). Editorial overview. Current Opinion in Cell Biology. Elsevier. https://doi.org/10.1016/j.ceb.2011.04.013","ama":"Hetzer M, Cavalli G. Editorial overview. Current Opinion in Cell Biology. 2011;23(3):255-257. doi:10.1016/j.ceb.2011.04.013"},"user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","publisher":"Elsevier","quality_controlled":"1","page":"255-257","date_published":"2011-06-01T00:00:00Z","doi":"10.1016/j.ceb.2011.04.013","date_created":"2022-04-07T07:52:27Z","year":"2011","day":"01","publication":"Current Opinion in Cell Biology"},{"extern":"1","date_updated":"2022-07-18T08:54:23Z","keyword":["Genetics","Molecular Biology","Biochemistry"],"status":"public","type":"journal_article","article_type":"original","_id":"11100","volume":75,"language":[{"iso":"eng"}],"publication_status":"published","publication_identifier":{"issn":["0091-7451","1943-4456"],"isbn":["9781936113071"]},"intvolume":" 75","month":"04","scopus_import":"1","oa_version":"None","pmid":1,"abstract":[{"text":"Eukaryotic cell function depends on the physical separation of nucleoplasmic and cytoplasmic components by the nuclear envelope (NE). Molecular communication between the two compartments involves active, signal-mediated trafficking, a function that is exclusively performed by nuclear pore complexes (NPCs). The individual NPC components and the mechanisms that are involved in nuclear trafficking are well documented and have become textbook knowledge. However, in addition to their roles as nuclear gatekeepers, NPC components-nucleoporins-have been shown to have critical roles in chromatin organization and gene regulation. These findings have sparked new enthusiasm to study the roles of this multiprotein complex in nuclear organization and explore novel functions that in some cases appear to go beyond a role in transport. Here, we discuss our present view of NPC biogenesis, which is tightly linked to proper cell cycle progression and cell differentiation. In addition, we summarize new data suggesting that NPCs represent dynamic hubs for the integration of gene regulation and nuclear transport processes.","lang":"eng"}],"title":"Nuclear pore complexes: Guardians of the nuclear genome","article_processing_charge":"No","external_id":{"pmid":["21502404"]},"author":[{"full_name":"Capelson, M.","last_name":"Capelson","first_name":"M."},{"full_name":"Doucet, C.","last_name":"Doucet","first_name":"C."},{"last_name":"HETZER","full_name":"HETZER, Martin W","orcid":"0000-0002-2111-992X","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","first_name":"Martin W"}],"user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","citation":{"chicago":"Capelson, M., C. Doucet, and Martin Hetzer. “Nuclear Pore Complexes: Guardians of the Nuclear Genome.” Cold Spring Harbor Symposia on Quantitative Biology. Cold Spring Harbor Laboratory Press, 2011. https://doi.org/10.1101/sqb.2010.75.059.","ista":"Capelson M, Doucet C, Hetzer M. 2011. Nuclear pore complexes: Guardians of the nuclear genome. Cold Spring Harbor Symposia on Quantitative Biology. 75, 585–597.","mla":"Capelson, M., et al. “Nuclear Pore Complexes: Guardians of the Nuclear Genome.” Cold Spring Harbor Symposia on Quantitative Biology, vol. 75, Cold Spring Harbor Laboratory Press, 2011, pp. 585–97, doi:10.1101/sqb.2010.75.059.","short":"M. Capelson, C. Doucet, M. Hetzer, Cold Spring Harbor Symposia on Quantitative Biology 75 (2011) 585–597.","ieee":"M. Capelson, C. Doucet, and M. Hetzer, “Nuclear pore complexes: Guardians of the nuclear genome,” Cold Spring Harbor Symposia on Quantitative Biology, vol. 75. Cold Spring Harbor Laboratory Press, pp. 585–597, 2011.","apa":"Capelson, M., Doucet, C., & Hetzer, M. (2011). Nuclear pore complexes: Guardians of the nuclear genome. Cold Spring Harbor Symposia on Quantitative Biology. Cold Spring Harbor Laboratory Press. https://doi.org/10.1101/sqb.2010.75.059","ama":"Capelson M, Doucet C, Hetzer M. Nuclear pore complexes: Guardians of the nuclear genome. Cold Spring Harbor Symposia on Quantitative Biology. 2011;75:585-597. doi:10.1101/sqb.2010.75.059"},"date_created":"2022-04-07T07:53:18Z","date_published":"2011-04-18T00:00:00Z","doi":"10.1101/sqb.2010.75.059","page":"585-597","publication":"Cold Spring Harbor Symposia on Quantitative Biology","day":"18","year":"2011","publisher":"Cold Spring Harbor Laboratory Press","quality_controlled":"1"},{"external_id":{"pmid":["20300205"]},"article_processing_charge":"No","author":[{"last_name":"HETZER","orcid":"0000-0002-2111-992X","full_name":"HETZER, Martin W","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","first_name":"Martin W"}],"title":"The nuclear envelope","citation":{"ista":"Hetzer M. 2010. The nuclear envelope. Cold Spring Harbor Perspectives in Biology. 2(3), a000539–a000539.","chicago":"Hetzer, Martin. “The Nuclear Envelope.” Cold Spring Harbor Perspectives in Biology. Cold Spring Harbor Laboratory, 2010. https://doi.org/10.1101/cshperspect.a000539.","short":"M. Hetzer, Cold Spring Harbor Perspectives in Biology 2 (2010) a000539–a000539.","ieee":"M. Hetzer, “The nuclear envelope,” Cold Spring Harbor Perspectives in Biology, vol. 2, no. 3. Cold Spring Harbor Laboratory, pp. a000539–a000539, 2010.","apa":"Hetzer, M. (2010). The nuclear envelope. Cold Spring Harbor Perspectives in Biology. Cold Spring Harbor Laboratory. https://doi.org/10.1101/cshperspect.a000539","ama":"Hetzer M. The nuclear envelope. Cold Spring Harbor Perspectives in Biology. 2010;2(3):a000539-a000539. doi:10.1101/cshperspect.a000539","mla":"Hetzer, Martin. “The Nuclear Envelope.” Cold Spring Harbor Perspectives in Biology, vol. 2, no. 3, Cold Spring Harbor Laboratory, 2010, pp. a000539–a000539, doi:10.1101/cshperspect.a000539."},"user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","page":"a000539-a000539","date_created":"2022-04-07T07:52:49Z","date_published":"2010-02-03T00:00:00Z","doi":"10.1101/cshperspect.a000539","year":"2010","publication":"Cold Spring Harbor Perspectives in Biology","day":"03","quality_controlled":"1","publisher":"Cold Spring Harbor Laboratory","date_updated":"2022-07-18T08:53:50Z","extern":"1","type":"journal_article","article_type":"original","keyword":["General Biochemistry","Genetics and Molecular Biology"],"status":"public","_id":"11097","volume":2,"issue":"3","publication_status":"published","publication_identifier":{"issn":["1943-0264"]},"language":[{"iso":"eng"}],"scopus_import":"1","intvolume":" 2","month":"02","abstract":[{"lang":"eng","text":"The nuclear envelope (NE) is a highly regulated membrane barrier that separates the nucleus from the cytoplasm in eukaryotic cells. It contains a large number of different proteins that have been implicated in chromatin organization and gene regulation. Although the nuclear membrane enables complex levels of gene expression, it also poses a challenge when it comes to cell division. To allow access of the mitotic spindle to chromatin, the nucleus of metazoans must completely disassemble during mitosis, generating the need to re-establish the nuclear compartment at the end of each cell division. Here, I summarize our current understanding of the dynamic remodeling of the NE during the cell cycle."}],"oa_version":"None","pmid":1},{"date_published":"2010-10-01T00:00:00Z","doi":"10.1007/s00412-010-0289-2","date_created":"2022-04-07T07:53:12Z","page":"469-477","day":"01","publication":"Chromosoma","year":"2010","publisher":"Springer Nature","quality_controlled":"1","title":"Nuclear pore biogenesis into an intact nuclear envelope","author":[{"full_name":"Doucet, Christine M.","last_name":"Doucet","first_name":"Christine M."},{"id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","first_name":"Martin W","full_name":"HETZER, Martin W","orcid":"0000-0002-2111-992X","last_name":"HETZER"}],"external_id":{"pmid":["20721671"]},"article_processing_charge":"No","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","citation":{"apa":"Doucet, C. M., & Hetzer, M. (2010). Nuclear pore biogenesis into an intact nuclear envelope. Chromosoma. Springer Nature. https://doi.org/10.1007/s00412-010-0289-2","ama":"Doucet CM, Hetzer M. Nuclear pore biogenesis into an intact nuclear envelope. Chromosoma. 2010;119:469-477. doi:10.1007/s00412-010-0289-2","short":"C.M. Doucet, M. Hetzer, Chromosoma 119 (2010) 469–477.","ieee":"C. M. Doucet and M. Hetzer, “Nuclear pore biogenesis into an intact nuclear envelope,” Chromosoma, vol. 119. Springer Nature, pp. 469–477, 2010.","mla":"Doucet, Christine M., and Martin Hetzer. “Nuclear Pore Biogenesis into an Intact Nuclear Envelope.” Chromosoma, vol. 119, Springer Nature, 2010, pp. 469–77, doi:10.1007/s00412-010-0289-2.","ista":"Doucet CM, Hetzer M. 2010. Nuclear pore biogenesis into an intact nuclear envelope. Chromosoma. 119, 469–477.","chicago":"Doucet, Christine M., and Martin Hetzer. “Nuclear Pore Biogenesis into an Intact Nuclear Envelope.” Chromosoma. Springer Nature, 2010. https://doi.org/10.1007/s00412-010-0289-2."},"volume":119,"language":[{"iso":"eng"}],"publication_identifier":{"issn":["0009-5915"],"eissn":["1432-0886"]},"publication_status":"published","month":"10","intvolume":" 119","scopus_import":"1","pmid":1,"oa_version":"None","abstract":[{"lang":"eng","text":"Nuclear pore complexes (NPCs) serve as transport channels across the nuclear membrane, a double lipid bilayer that physically separates the nucleoplasm and cytoplasm of eukaryotic cells. New evidence suggests that the multiprotein nuclear pores also play a role in chromatin organization and gene expression. Given the importance of NPC function, it is not surprising that a growing list of human diseases and developmental defects have been linked to its malfunction. In order to fully understand the functional repertoire of NPCs and their essential role for nuclear organization, it is critical to determine the sequence of events that lead to the formation of nuclear pores. This is particularly relevant since NPC number, and possibly composition, are tightly linked to metabolic activity. Most of our knowledge is derived from NPC formation that occurs in dividing cells at the end of mitosis when the nuclear envelope (NE) and NPCs reform from disassembled precursors. However, NPC assembly also takes place during interphase into an intact NE. Importantly, this process is not restricted to dividing cells but also occurs during cell differentiation. Here, we will review aspects unique to this process, namely the regulation of nuclear expansion and the mechanisms of fusion between the outer and inner nuclear membranes. We will then discuss conserved and diverging mechanisms between post-mitotic and interphase assembly of the proteinaceous structure in light of recently published data."}],"extern":"1","date_updated":"2022-07-18T08:54:20Z","status":"public","keyword":["Genetics (clinical)","Genetics"],"article_type":"review","type":"journal_article","_id":"11099"},{"type":"journal_article","article_type":"original","status":"public","keyword":["General Biochemistry","Genetics and Molecular Biology"],"_id":"11102","date_updated":"2022-07-18T08:55:03Z","extern":"1","scopus_import":"1","main_file_link":[{"url":"https://doi.org/10.1016/j.cell.2009.12.054","open_access":"1"}],"month":"02","intvolume":" 140","abstract":[{"lang":"eng","text":"Nuclear pore complexes have recently been shown to play roles in gene activation; however their potential involvement in metazoan transcription remains unclear. Here we show that the nucleoporins Sec13, Nup98, and Nup88, as well as a group of FG-repeat nucleoporins, bind to the Drosophila genome at functionally distinct loci that often do not represent nuclear envelope contact sites. Whereas Nup88 localizes to silent loci, Sec13, Nup98, and a subset of FG-repeat nucleoporins bind to developmentally regulated genes undergoing transcription induction. Strikingly, RNAi-mediated knockdown of intranuclear Sec13 and Nup98 specifically inhibits transcription of their target genes and prevents efficient reactivation of transcription after heat shock, suggesting an essential role of NPC components in regulating complex gene expression programs of multicellular organisms."}],"pmid":1,"oa_version":"Published Version","volume":140,"issue":"3","publication_identifier":{"issn":["0092-8674"]},"publication_status":"published","language":[{"iso":"eng"}],"author":[{"first_name":"Maya","full_name":"Capelson, Maya","last_name":"Capelson"},{"first_name":"Yun","last_name":"Liang","full_name":"Liang, Yun"},{"last_name":"Schulte","full_name":"Schulte, Roberta","first_name":"Roberta"},{"first_name":"William","last_name":"Mair","full_name":"Mair, William"},{"full_name":"Wagner, Ulrich","last_name":"Wagner","first_name":"Ulrich"},{"first_name":"Martin W","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","last_name":"HETZER","orcid":"0000-0002-2111-992X","full_name":"HETZER, Martin W"}],"external_id":{"pmid":["20144761"]},"article_processing_charge":"No","title":"Chromatin-bound nuclear pore components regulate gene expression in higher eukaryotes","citation":{"chicago":"Capelson, Maya, Yun Liang, Roberta Schulte, William Mair, Ulrich Wagner, and Martin Hetzer. “Chromatin-Bound Nuclear Pore Components Regulate Gene Expression in Higher Eukaryotes.” Cell. Elsevier, 2010. https://doi.org/10.1016/j.cell.2009.12.054.","ista":"Capelson M, Liang Y, Schulte R, Mair W, Wagner U, Hetzer M. 2010. Chromatin-bound nuclear pore components regulate gene expression in higher eukaryotes. Cell. 140(3), 372–383.","mla":"Capelson, Maya, et al. “Chromatin-Bound Nuclear Pore Components Regulate Gene Expression in Higher Eukaryotes.” Cell, vol. 140, no. 3, Elsevier, 2010, pp. 372–83, doi:10.1016/j.cell.2009.12.054.","short":"M. Capelson, Y. Liang, R. Schulte, W. Mair, U. Wagner, M. Hetzer, Cell 140 (2010) 372–383.","ieee":"M. Capelson, Y. Liang, R. Schulte, W. Mair, U. Wagner, and M. Hetzer, “Chromatin-bound nuclear pore components regulate gene expression in higher eukaryotes,” Cell, vol. 140, no. 3. Elsevier, pp. 372–383, 2010.","ama":"Capelson M, Liang Y, Schulte R, Mair W, Wagner U, Hetzer M. Chromatin-bound nuclear pore components regulate gene expression in higher eukaryotes. Cell. 2010;140(3):372-383. doi:10.1016/j.cell.2009.12.054","apa":"Capelson, M., Liang, Y., Schulte, R., Mair, W., Wagner, U., & Hetzer, M. (2010). Chromatin-bound nuclear pore components regulate gene expression in higher eukaryotes. Cell. Elsevier. https://doi.org/10.1016/j.cell.2009.12.054"},"user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","quality_controlled":"1","publisher":"Elsevier","oa":1,"page":"372-383","doi":"10.1016/j.cell.2009.12.054","date_published":"2010-02-05T00:00:00Z","date_created":"2022-04-07T07:53:36Z","year":"2010","day":"05","publication":"Cell"},{"abstract":[{"text":"In metazoa, nuclear pore complexes (NPCs) assemble from disassembled precursors into a reforming nuclear envelope (NE) at the end of mitosis and into growing intact NEs during interphase. Here, we show via RNAi-mediated knockdown that ELYS, a nucleoporin critical for the recruitment of the essential Nup107/160 complex to chromatin, is required for NPC assembly at the end of mitosis but not during interphase. Conversely, the transmembrane nucleoporin POM121 is critical for the incorporation of the Nup107/160 complex into new assembly sites specifically during interphase. Strikingly, recruitment of the Nup107/160 complex to an intact NE involves a membrane curvature-sensing domain of its constituent Nup133, which is not required for postmitotic NPC formation. Our results suggest that in organisms with open mitosis, NPCs assemble via two distinct mechanisms to accommodate cell cycle-dependent differences in NE topology.","lang":"eng"}],"pmid":1,"oa_version":"Published Version","main_file_link":[{"open_access":"1","url":"https://doi.org/10.1016/j.cell.2010.04.036"}],"scopus_import":"1","intvolume":" 141","month":"06","publication_status":"published","publication_identifier":{"issn":["0092-8674"]},"language":[{"iso":"eng"}],"volume":141,"issue":"6","_id":"11101","article_type":"original","type":"journal_article","keyword":["General Biochemistry","Genetics and Molecular Biology"],"status":"public","date_updated":"2022-07-18T08:54:52Z","extern":"1","oa":1,"quality_controlled":"1","publisher":"Elsevier","year":"2010","publication":"Cell","day":"11","page":"1030-1041","date_created":"2022-04-07T07:53:29Z","doi":"10.1016/j.cell.2010.04.036","date_published":"2010-06-11T00:00:00Z","citation":{"ista":"Doucet CM, Talamas JA, Hetzer M. 2010. Cell cycle-dependent differences in nuclear pore complex assembly in metazoa. Cell. 141(6), 1030–1041.","chicago":"Doucet, Christine M., Jessica A. Talamas, and Martin Hetzer. “Cell Cycle-Dependent Differences in Nuclear Pore Complex Assembly in Metazoa.” Cell. Elsevier, 2010. https://doi.org/10.1016/j.cell.2010.04.036.","ieee":"C. M. Doucet, J. A. Talamas, and M. Hetzer, “Cell cycle-dependent differences in nuclear pore complex assembly in metazoa,” Cell, vol. 141, no. 6. Elsevier, pp. 1030–1041, 2010.","short":"C.M. Doucet, J.A. Talamas, M. Hetzer, Cell 141 (2010) 1030–1041.","apa":"Doucet, C. M., Talamas, J. A., & Hetzer, M. (2010). Cell cycle-dependent differences in nuclear pore complex assembly in metazoa. Cell. Elsevier. https://doi.org/10.1016/j.cell.2010.04.036","ama":"Doucet CM, Talamas JA, Hetzer M. Cell cycle-dependent differences in nuclear pore complex assembly in metazoa. Cell. 2010;141(6):1030-1041. doi:10.1016/j.cell.2010.04.036","mla":"Doucet, Christine M., et al. “Cell Cycle-Dependent Differences in Nuclear Pore Complex Assembly in Metazoa.” Cell, vol. 141, no. 6, Elsevier, 2010, pp. 1030–41, doi:10.1016/j.cell.2010.04.036."},"user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","article_processing_charge":"No","external_id":{"pmid":["20550937"]},"author":[{"first_name":"Christine M.","last_name":"Doucet","full_name":"Doucet, Christine M."},{"first_name":"Jessica A.","full_name":"Talamas, Jessica A.","last_name":"Talamas"},{"id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","first_name":"Martin W","orcid":"0000-0002-2111-992X","full_name":"HETZER, Martin W","last_name":"HETZER"}],"title":"Cell cycle-dependent differences in nuclear pore complex assembly in metazoa"},{"user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","citation":{"mla":"Hetzer, Martin. “The Role of the Nuclear Pore Complex in Aging of Post-Mitotic Cells.” Aging, vol. 2, no. 2, Impact Journals, 2010, pp. 74–75, doi:10.18632/aging.100125.","short":"M. Hetzer, Aging 2 (2010) 74–75.","ieee":"M. Hetzer, “The role of the nuclear pore complex in aging of post-mitotic cells,” Aging, vol. 2, no. 2. Impact Journals, pp. 74–75, 2010.","ama":"Hetzer M. The role of the nuclear pore complex in aging of post-mitotic cells. Aging. 2010;2(2):74-75. doi:10.18632/aging.100125","apa":"Hetzer, M. (2010). The role of the nuclear pore complex in aging of post-mitotic cells. Aging. Impact Journals. https://doi.org/10.18632/aging.100125","chicago":"Hetzer, Martin. “The Role of the Nuclear Pore Complex in Aging of Post-Mitotic Cells.” Aging. Impact Journals, 2010. https://doi.org/10.18632/aging.100125.","ista":"Hetzer M. 2010. The role of the nuclear pore complex in aging of post-mitotic cells. Aging. 2(2), 74–75."},"title":"The role of the nuclear pore complex in aging of post-mitotic cells","article_processing_charge":"No","external_id":{"pmid":["20354266"]},"author":[{"id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","first_name":"Martin W","orcid":"0000-0002-2111-992X","full_name":"HETZER, Martin W","last_name":"HETZER"}],"publication":"Aging","day":"01","year":"2010","date_created":"2022-04-07T07:52:58Z","date_published":"2010-02-01T00:00:00Z","doi":"10.18632/aging.100125","page":"74-75","oa":1,"publisher":"Impact Journals","quality_controlled":"1","extern":"1","date_updated":"2022-07-18T08:54:15Z","_id":"11098","keyword":["Cell Biology","Aging"],"status":"public","type":"journal_article","article_type":"original","language":[{"iso":"eng"}],"publication_status":"published","publication_identifier":{"issn":["1945-4589"]},"issue":"2","volume":2,"pmid":1,"oa_version":"Published Version","intvolume":" 2","month":"02","main_file_link":[{"url":"https://doi.org/10.18632/aging.100125","open_access":"1"}],"scopus_import":"1"},{"title":"Border control at the nucleus: Biogenesis and organization of the nuclear membrane and pore complexes","author":[{"last_name":"HETZER","full_name":"HETZER, Martin W","orcid":"0000-0002-2111-992X","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","first_name":"Martin W"},{"first_name":"Susan R.","last_name":"Wente","full_name":"Wente, Susan R."}],"external_id":{"pmid":["19922866"]},"article_processing_charge":"No","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","citation":{"chicago":"Hetzer, Martin, and Susan R. Wente. “Border Control at the Nucleus: Biogenesis and Organization of the Nuclear Membrane and Pore Complexes.” Developmental Cell. Elsevier, 2009. https://doi.org/10.1016/j.devcel.2009.10.007.","ista":"Hetzer M, Wente SR. 2009. Border control at the nucleus: Biogenesis and organization of the nuclear membrane and pore complexes. Developmental Cell. 17(5), 606–616.","mla":"Hetzer, Martin, and Susan R. Wente. “Border Control at the Nucleus: Biogenesis and Organization of the Nuclear Membrane and Pore Complexes.” Developmental Cell, vol. 17, no. 5, Elsevier, 2009, pp. 606–16, doi:10.1016/j.devcel.2009.10.007.","short":"M. Hetzer, S.R. Wente, Developmental Cell 17 (2009) 606–616.","ieee":"M. Hetzer and S. R. Wente, “Border control at the nucleus: Biogenesis and organization of the nuclear membrane and pore complexes,” Developmental Cell, vol. 17, no. 5. Elsevier, pp. 606–616, 2009.","apa":"Hetzer, M., & Wente, S. R. (2009). Border control at the nucleus: Biogenesis and organization of the nuclear membrane and pore complexes. Developmental Cell. Elsevier. https://doi.org/10.1016/j.devcel.2009.10.007","ama":"Hetzer M, Wente SR. Border control at the nucleus: Biogenesis and organization of the nuclear membrane and pore complexes. Developmental Cell. 2009;17(5):606-616. doi:10.1016/j.devcel.2009.10.007"},"date_published":"2009-11-17T00:00:00Z","doi":"10.1016/j.devcel.2009.10.007","date_created":"2022-04-07T07:53:45Z","page":"606-616","day":"17","publication":"Developmental Cell","year":"2009","publisher":"Elsevier","quality_controlled":"1","oa":1,"extern":"1","date_updated":"2022-07-18T08:55:01Z","status":"public","keyword":["Developmental Biology","Cell Biology","General Biochemistry","Genetics and Molecular Biology","Molecular Biology"],"article_type":"review","type":"journal_article","_id":"11103","volume":17,"issue":"5","language":[{"iso":"eng"}],"publication_identifier":{"issn":["1534-5807"]},"publication_status":"published","month":"11","intvolume":" 17","scopus_import":"1","main_file_link":[{"open_access":"1","url":"https://doi.org/10.1016/j.devcel.2009.10.007"}],"oa_version":"Published Version","pmid":1,"abstract":[{"text":"Over the last decade, the nuclear envelope (NE) has emerged as a key component in the organization and function of the nuclear genome. As many as 100 different proteins are thought to specifically localize to this double membrane that separates the cytoplasm and the nucleoplasm of eukaryotic cells. Selective portals through the NE are formed at sites where the inner and outer nuclear membranes are fused, and the coincident assembly of ∼30 proteins into nuclear pore complexes occurs. These nuclear pore complexes are essential for the control of nucleocytoplasmic exchange. Many of the NE and nuclear pore proteins are thought to play crucial roles in gene regulation and thus are increasingly linked to human diseases.","lang":"eng"}]},{"extern":"1","date_updated":"2022-07-18T08:58:35Z","status":"public","keyword":["Cell Biology"],"article_type":"original","type":"journal_article","_id":"11106","volume":186,"issue":"2","related_material":{"link":[{"relation":"erratum","url":"https://doi.org/10.1083/jcb.20090110620090903c"}]},"language":[{"iso":"eng"}],"publication_identifier":{"eissn":["1540-8140"],"issn":["0021-9525"]},"publication_status":"published","month":"07","intvolume":" 186","scopus_import":"1","main_file_link":[{"url":"https://doi.org/10.1083/jcb.200901106","open_access":"1"}],"pmid":1,"oa_version":"Published Version","abstract":[{"lang":"eng","text":"Formation of the nuclear envelope (NE) around segregated chromosomes occurs by the reshaping of the endoplasmic reticulum (ER), a reservoir for disassembled nuclear membrane components during mitosis. In this study, we show that inner nuclear membrane proteins such as lamin B receptor (LBR), MAN1, Lap2β, and the trans-membrane nucleoporins Ndc1 and POM121 drive the spreading of ER membranes into the emerging NE via their capacity to bind chromatin in a collaborative manner. Despite their redundant functions, decreasing the levels of any of these trans-membrane proteins by RNAi-mediated knockdown delayed NE formation, whereas increasing the levels of any of them had the opposite effect. Furthermore, acceleration of NE formation interferes with chromosome separation during mitosis, indicating that the time frame over which chromatin becomes membrane enclosed is physiologically relevant and regulated. These data suggest that functionally distinct classes of chromatin-interacting membrane proteins, which are present at nonsaturating levels, collaborate to rapidly reestablish the nuclear compartment at the end of mitosis."}],"title":"Recruitment of functionally distinct membrane proteins to chromatin mediates nuclear envelope formation in vivo","author":[{"first_name":"Daniel J.","last_name":"Anderson","full_name":"Anderson, Daniel J."},{"first_name":"Jesse D.","full_name":"Vargas, Jesse D.","last_name":"Vargas"},{"last_name":"Hsiao","full_name":"Hsiao, Joshua P.","first_name":"Joshua P."},{"id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","first_name":"Martin W","last_name":"HETZER","full_name":"HETZER, Martin W","orcid":"0000-0002-2111-992X"}],"external_id":{"pmid":["19620630"]},"article_processing_charge":"No","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","citation":{"short":"D.J. Anderson, J.D. Vargas, J.P. Hsiao, M. Hetzer, Journal of Cell Biology 186 (2009) 183–191.","ieee":"D. J. Anderson, J. D. Vargas, J. P. Hsiao, and M. Hetzer, “Recruitment of functionally distinct membrane proteins to chromatin mediates nuclear envelope formation in vivo,” Journal of Cell Biology, vol. 186, no. 2. Rockefeller University Press, pp. 183–191, 2009.","ama":"Anderson DJ, Vargas JD, Hsiao JP, Hetzer M. Recruitment of functionally distinct membrane proteins to chromatin mediates nuclear envelope formation in vivo. Journal of Cell Biology. 2009;186(2):183-191. doi:10.1083/jcb.200901106","apa":"Anderson, D. J., Vargas, J. D., Hsiao, J. P., & Hetzer, M. (2009). Recruitment of functionally distinct membrane proteins to chromatin mediates nuclear envelope formation in vivo. Journal of Cell Biology. Rockefeller University Press. https://doi.org/10.1083/jcb.200901106","mla":"Anderson, Daniel J., et al. “Recruitment of Functionally Distinct Membrane Proteins to Chromatin Mediates Nuclear Envelope Formation in Vivo.” Journal of Cell Biology, vol. 186, no. 2, Rockefeller University Press, 2009, pp. 183–91, doi:10.1083/jcb.200901106.","ista":"Anderson DJ, Vargas JD, Hsiao JP, Hetzer M. 2009. Recruitment of functionally distinct membrane proteins to chromatin mediates nuclear envelope formation in vivo. Journal of Cell Biology. 186(2), 183–191.","chicago":"Anderson, Daniel J., Jesse D. Vargas, Joshua P. Hsiao, and Martin Hetzer. “Recruitment of Functionally Distinct Membrane Proteins to Chromatin Mediates Nuclear Envelope Formation in Vivo.” Journal of Cell Biology. Rockefeller University Press, 2009. https://doi.org/10.1083/jcb.200901106."},"date_published":"2009-07-20T00:00:00Z","doi":"10.1083/jcb.200901106","date_created":"2022-04-07T07:54:18Z","page":"183-191","day":"20","publication":"Journal of Cell Biology","year":"2009","publisher":"Rockefeller University Press","quality_controlled":"1","oa":1},{"title":"ER membrane–bending proteins are necessary for de novo nuclear pore formation","author":[{"first_name":"T. Renee","full_name":"Dawson, T. Renee","last_name":"Dawson"},{"full_name":"Lazarus, Michelle D.","last_name":"Lazarus","first_name":"Michelle D."},{"last_name":"HETZER","orcid":"0000-0002-2111-992X","full_name":"HETZER, Martin W","first_name":"Martin W","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed"},{"full_name":"Wente, Susan R.","last_name":"Wente","first_name":"Susan R."}],"article_processing_charge":"No","external_id":{"pmid":["19273614"]},"user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","citation":{"apa":"Dawson, T. R., Lazarus, M. D., Hetzer, M., & Wente, S. R. (2009). ER membrane–bending proteins are necessary for de novo nuclear pore formation. Journal of Cell Biology. Rockefeller University Press. https://doi.org/10.1083/jcb.200806174","ama":"Dawson TR, Lazarus MD, Hetzer M, Wente SR. ER membrane–bending proteins are necessary for de novo nuclear pore formation. Journal of Cell Biology. 2009;184(5):659-675. doi:10.1083/jcb.200806174","ieee":"T. R. Dawson, M. D. Lazarus, M. Hetzer, and S. R. Wente, “ER membrane–bending proteins are necessary for de novo nuclear pore formation,” Journal of Cell Biology, vol. 184, no. 5. Rockefeller University Press, pp. 659–675, 2009.","short":"T.R. Dawson, M.D. Lazarus, M. Hetzer, S.R. Wente, Journal of Cell Biology 184 (2009) 659–675.","mla":"Dawson, T. Renee, et al. “ER Membrane–Bending Proteins Are Necessary for de Novo Nuclear Pore Formation.” Journal of Cell Biology, vol. 184, no. 5, Rockefeller University Press, 2009, pp. 659–75, doi:10.1083/jcb.200806174.","ista":"Dawson TR, Lazarus MD, Hetzer M, Wente SR. 2009. ER membrane–bending proteins are necessary for de novo nuclear pore formation. Journal of Cell Biology. 184(5), 659–675.","chicago":"Dawson, T. Renee, Michelle D. Lazarus, Martin Hetzer, and Susan R. Wente. “ER Membrane–Bending Proteins Are Necessary for de Novo Nuclear Pore Formation.” Journal of Cell Biology. Rockefeller University Press, 2009. https://doi.org/10.1083/jcb.200806174."},"quality_controlled":"1","publisher":"Rockefeller University Press","oa":1,"date_published":"2009-03-09T00:00:00Z","doi":"10.1083/jcb.200806174","date_created":"2022-04-07T07:54:44Z","page":"659-675","day":"09","publication":"Journal of Cell Biology","year":"2009","status":"public","keyword":["Cell Biology"],"article_type":"original","type":"journal_article","_id":"11107","extern":"1","date_updated":"2022-07-18T08:55:05Z","month":"03","intvolume":" 184","scopus_import":"1","main_file_link":[{"open_access":"1","url":"https://doi.org/10.1083/jcb.200806174"}],"pmid":1,"oa_version":"Published Version","abstract":[{"lang":"eng","text":"Nucleocytoplasmic transport occurs exclusively through nuclear pore complexes (NPCs) embedded in pores formed by inner and outer nuclear membrane fusion. The mechanism for de novo pore and NPC biogenesis remains unclear. Reticulons (RTNs) and Yop1/DP1 are conserved membrane protein families required to form and maintain the tubular endoplasmic reticulum (ER) and the postmitotic nuclear envelope. In this study, we report that members of the RTN and Yop1/DP1 families are required for nuclear pore formation. Analysis of Saccharomyces cerevisiae prp20-G282S and nup133Δ NPC assembly mutants revealed perturbations in Rtn1–green fluorescent protein (GFP) and Yop1-GFP ER distribution and colocalization to NPC clusters. Combined deletion of RTN1 and YOP1 resulted in NPC clustering, nuclear import defects, and synthetic lethality with the additional absence of Pom34, Pom152, and Nup84 subcomplex members. We tested for a direct role in NPC biogenesis using Xenopus laevis in vitro assays and found that anti-Rtn4a antibodies specifically inhibited de novo nuclear pore formation. We hypothesize that these ER membrane–bending proteins mediate early NPC assembly steps."}],"volume":184,"issue":"5","language":[{"iso":"eng"}],"publication_identifier":{"eissn":["1540-8140"],"issn":["0021-9525"]},"publication_status":"published"},{"status":"public","keyword":["General Biochemistry","Genetics and Molecular Biology"],"article_type":"original","type":"journal_article","_id":"11108","extern":"1","date_updated":"2022-07-18T08:55:29Z","month":"01","intvolume":" 136","scopus_import":"1","main_file_link":[{"url":"https://doi.org/10.1016/j.cell.2008.11.037","open_access":"1"}],"oa_version":"Published Version","pmid":1,"abstract":[{"lang":"eng","text":"In dividing cells, nuclear pore complexes (NPCs) disassemble during mitosis and reassemble into the newly forming nuclei. However, the fate of nuclear pores in postmitotic cells is unknown. Here, we show that NPCs, unlike other nuclear structures, do not turn over in differentiated cells. While a subset of NPC components, like Nup153 and Nup50, are continuously exchanged, scaffold nucleoporins, like the Nup107/160 complex, are extremely long-lived and remain incorporated in the nuclear membrane during the entire cellular life span. Besides the lack of nucleoporin expression and NPC turnover, we discovered an age-related deterioration of NPCs, leading to an increase in nuclear permeability and the leaking of cytoplasmic proteins into the nucleus. Our finding that nuclear “leakiness” is dramatically accelerated during aging and that a subset of nucleoporins is oxidatively damaged in old cells suggests that the accumulation of damage at the NPC might be a crucial aging event."}],"issue":"2","volume":136,"language":[{"iso":"eng"}],"publication_identifier":{"issn":["0092-8674"]},"publication_status":"published","title":"Age-dependent deterioration of nuclear pore complexes causes a loss of nuclear integrity in postmitotic cells","author":[{"last_name":"D'Angelo","full_name":"D'Angelo, Maximiliano A.","first_name":"Maximiliano A."},{"first_name":"Marcela","full_name":"Raices, Marcela","last_name":"Raices"},{"last_name":"Panowski","full_name":"Panowski, Siler H.","first_name":"Siler H."},{"full_name":"HETZER, Martin W","orcid":"0000-0002-2111-992X","last_name":"HETZER","first_name":"Martin W","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed"}],"article_processing_charge":"No","external_id":{"pmid":["19167330"]},"user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","citation":{"mla":"D’Angelo, Maximiliano A., et al. “Age-Dependent Deterioration of Nuclear Pore Complexes Causes a Loss of Nuclear Integrity in Postmitotic Cells.” Cell, vol. 136, no. 2, Elsevier, 2009, pp. 284–95, doi:10.1016/j.cell.2008.11.037.","apa":"D’Angelo, M. A., Raices, M., Panowski, S. H., & Hetzer, M. (2009). Age-dependent deterioration of nuclear pore complexes causes a loss of nuclear integrity in postmitotic cells. Cell. Elsevier. https://doi.org/10.1016/j.cell.2008.11.037","ama":"D’Angelo MA, Raices M, Panowski SH, Hetzer M. Age-dependent deterioration of nuclear pore complexes causes a loss of nuclear integrity in postmitotic cells. Cell. 2009;136(2):284-295. doi:10.1016/j.cell.2008.11.037","ieee":"M. A. D’Angelo, M. Raices, S. H. Panowski, and M. Hetzer, “Age-dependent deterioration of nuclear pore complexes causes a loss of nuclear integrity in postmitotic cells,” Cell, vol. 136, no. 2. Elsevier, pp. 284–295, 2009.","short":"M.A. D’Angelo, M. Raices, S.H. Panowski, M. Hetzer, Cell 136 (2009) 284–295.","chicago":"D’Angelo, Maximiliano A., Marcela Raices, Siler H. Panowski, and Martin Hetzer. “Age-Dependent Deterioration of Nuclear Pore Complexes Causes a Loss of Nuclear Integrity in Postmitotic Cells.” Cell. Elsevier, 2009. https://doi.org/10.1016/j.cell.2008.11.037.","ista":"D’Angelo MA, Raices M, Panowski SH, Hetzer M. 2009. Age-dependent deterioration of nuclear pore complexes causes a loss of nuclear integrity in postmitotic cells. Cell. 136(2), 284–295."},"publisher":"Elsevier","quality_controlled":"1","oa":1,"doi":"10.1016/j.cell.2008.11.037","date_published":"2009-01-23T00:00:00Z","date_created":"2022-04-07T07:54:52Z","page":"284-295","day":"23","publication":"Cell","year":"2009"},{"page":"697-705","doi":"10.1038/embor.2009.147","date_published":"2009-07-01T00:00:00Z","date_created":"2022-04-07T07:54:06Z","year":"2009","day":"01","publication":"EMBO reports","publisher":"EMBO","quality_controlled":"1","oa":1,"author":[{"first_name":"Maya","last_name":"Capelson","full_name":"Capelson, Maya"},{"last_name":"HETZER","orcid":"0000-0002-2111-992X","full_name":"HETZER, Martin W","first_name":"Martin W","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed"}],"external_id":{"pmid":["19543230"]},"article_processing_charge":"No","title":"The role of nuclear pores in gene regulation, development and disease","citation":{"short":"M. Capelson, M. Hetzer, EMBO Reports 10 (2009) 697–705.","ieee":"M. Capelson and M. Hetzer, “The role of nuclear pores in gene regulation, development and disease,” EMBO reports, vol. 10, no. 7. EMBO, pp. 697–705, 2009.","apa":"Capelson, M., & Hetzer, M. (2009). The role of nuclear pores in gene regulation, development and disease. EMBO Reports. EMBO. https://doi.org/10.1038/embor.2009.147","ama":"Capelson M, Hetzer M. The role of nuclear pores in gene regulation, development and disease. EMBO reports. 2009;10(7):697-705. doi:10.1038/embor.2009.147","mla":"Capelson, Maya, and Martin Hetzer. “The Role of Nuclear Pores in Gene Regulation, Development and Disease.” EMBO Reports, vol. 10, no. 7, EMBO, 2009, pp. 697–705, doi:10.1038/embor.2009.147.","ista":"Capelson M, Hetzer M. 2009. The role of nuclear pores in gene regulation, development and disease. EMBO reports. 10(7), 697–705.","chicago":"Capelson, Maya, and Martin Hetzer. “The Role of Nuclear Pores in Gene Regulation, Development and Disease.” EMBO Reports. EMBO, 2009. https://doi.org/10.1038/embor.2009.147."},"user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","related_material":{"link":[{"relation":"erratum","url":"https://doi.org/10.1038/embor.2009.176"}]},"volume":10,"issue":"7","publication_identifier":{"issn":["1469-221X"],"eissn":["1469-3178"]},"publication_status":"published","language":[{"iso":"eng"}],"scopus_import":"1","main_file_link":[{"open_access":"1","url":"https://doi.org/10.1038/embor.2009.147"}],"month":"07","intvolume":" 10","abstract":[{"lang":"eng","text":"Nuclear-pore complexes (NPCs) are large protein channels that span the nuclear envelope (NE), which is a double membrane that encloses the nuclear genome of eukaryotes. Each of the typically 2,000–4,000 pores in the NE of vertebrate cells is composed of multiple copies of 30 different proteins known as nucleoporins. The evolutionarily conserved NPC proteins have the well-characterized function of mediating the transport of molecules between the nucleoplasm and the cytoplasm. Mutations in nucleoporins are often linked to specific developmental defects and disease, and the resulting phenotypes are usually interpreted as the consequences of perturbed nuclear transport activity. However, recent evidence suggests that NPCs have additional functions in chromatin organization and gene regulation, some of which might be independent of nuclear transport. Here, we review the transport-dependent and transport-independent roles of NPCs in the regulation of nuclear function and gene expression."}],"pmid":1,"oa_version":"Published Version","date_updated":"2022-07-18T08:42:44Z","extern":"1","article_type":"original","type":"journal_article","status":"public","keyword":["Genetics","Molecular Biology","Biochemistry"],"_id":"11105"},{"article_processing_charge":"No","external_id":{"pmid":["18779370"]},"author":[{"full_name":"Anderson, Daniel J.","last_name":"Anderson","first_name":"Daniel J."},{"id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","first_name":"Martin W","last_name":"HETZER","full_name":"HETZER, Martin W","orcid":"0000-0002-2111-992X"}],"title":"Reshaping of the endoplasmic reticulum limits the rate for nuclear envelope formation","citation":{"chicago":"Anderson, Daniel J., and Martin Hetzer. “Reshaping of the Endoplasmic Reticulum Limits the Rate for Nuclear Envelope Formation.” Journal of Cell Biology. Rockefeller University Press, 2008. https://doi.org/10.1083/jcb.200805140.","ista":"Anderson DJ, Hetzer M. 2008. Reshaping of the endoplasmic reticulum limits the rate for nuclear envelope formation. Journal of Cell Biology. 182(5), 911–924.","mla":"Anderson, Daniel J., and Martin Hetzer. “Reshaping of the Endoplasmic Reticulum Limits the Rate for Nuclear Envelope Formation.” Journal of Cell Biology, vol. 182, no. 5, Rockefeller University Press, 2008, pp. 911–24, doi:10.1083/jcb.200805140.","ama":"Anderson DJ, Hetzer M. Reshaping of the endoplasmic reticulum limits the rate for nuclear envelope formation. Journal of Cell Biology. 2008;182(5):911-924. doi:10.1083/jcb.200805140","apa":"Anderson, D. J., & Hetzer, M. (2008). Reshaping of the endoplasmic reticulum limits the rate for nuclear envelope formation. Journal of Cell Biology. Rockefeller University Press. https://doi.org/10.1083/jcb.200805140","ieee":"D. J. Anderson and M. Hetzer, “Reshaping of the endoplasmic reticulum limits the rate for nuclear envelope formation,” Journal of Cell Biology, vol. 182, no. 5. Rockefeller University Press, pp. 911–924, 2008.","short":"D.J. Anderson, M. Hetzer, Journal of Cell Biology 182 (2008) 911–924."},"user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","publisher":"Rockefeller University Press","quality_controlled":"1","page":"911-924","date_created":"2022-04-07T07:55:23Z","doi":"10.1083/jcb.200805140","date_published":"2008-09-08T00:00:00Z","year":"2008","publication":"Journal of Cell Biology","day":"08","article_type":"original","type":"journal_article","keyword":["Cell Biology"],"status":"public","_id":"11111","date_updated":"2022-07-18T08:56:02Z","extern":"1","scopus_import":"1","intvolume":" 182","month":"09","abstract":[{"text":"During mitosis in metazoans, segregated chromosomes become enclosed by the nuclear envelope (NE), a double membrane that is continuous with the endoplasmic reticulum (ER). Recent in vitro data suggest that NE formation occurs by chromatin-mediated reorganization of the tubular ER; however, the basic principles of such a membrane-reshaping process remain uncharacterized. Here, we present a quantitative analysis of nuclear membrane assembly in mammalian cells using time-lapse microscopy. From the initial recruitment of ER tubules to chromatin, the formation of a membrane-enclosed, transport-competent nucleus occurs within ∼12 min. Overexpression of the ER tubule-forming proteins reticulon 3, reticulon 4, and DP1 inhibits NE formation and nuclear expansion, whereas their knockdown accelerates nuclear assembly. This suggests that the transition from membrane tubules to sheets is rate-limiting for nuclear assembly. Our results provide evidence that ER-shaping proteins are directly involved in the reconstruction of the nuclear compartment and that morphological restructuring of the ER is the principal mechanism of NE formation in vivo.","lang":"eng"}],"oa_version":"None","pmid":1,"volume":182,"issue":"5","publication_status":"published","publication_identifier":{"issn":["0021-9525"],"eissn":["1540-8140"]},"language":[{"iso":"eng"}]},{"publisher":"Elsevier","quality_controlled":"1","year":"2008","day":"01","publication":"Trends in Cell Biology","page":"456-466","doi":"10.1016/j.tcb.2008.07.009","date_published":"2008-10-01T00:00:00Z","date_created":"2022-04-07T07:55:10Z","citation":{"ista":"D’Angelo MA, Hetzer M. 2008. Structure, dynamics and function of nuclear pore complexes. Trends in Cell Biology. 18(10), 456–466.","chicago":"D’Angelo, Maximiliano A., and Martin Hetzer. “Structure, Dynamics and Function of Nuclear Pore Complexes.” Trends in Cell Biology. Elsevier, 2008. https://doi.org/10.1016/j.tcb.2008.07.009.","ama":"D’Angelo MA, Hetzer M. Structure, dynamics and function of nuclear pore complexes. Trends in Cell Biology. 2008;18(10):456-466. doi:10.1016/j.tcb.2008.07.009","apa":"D’Angelo, M. A., & Hetzer, M. (2008). Structure, dynamics and function of nuclear pore complexes. Trends in Cell Biology. Elsevier. https://doi.org/10.1016/j.tcb.2008.07.009","ieee":"M. A. D’Angelo and M. Hetzer, “Structure, dynamics and function of nuclear pore complexes,” Trends in Cell Biology, vol. 18, no. 10. Elsevier, pp. 456–466, 2008.","short":"M.A. D’Angelo, M. Hetzer, Trends in Cell Biology 18 (2008) 456–466.","mla":"D’Angelo, Maximiliano A., and Martin Hetzer. “Structure, Dynamics and Function of Nuclear Pore Complexes.” Trends in Cell Biology, vol. 18, no. 10, Elsevier, 2008, pp. 456–66, doi:10.1016/j.tcb.2008.07.009."},"user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","author":[{"last_name":"D’Angelo","full_name":"D’Angelo, Maximiliano A.","first_name":"Maximiliano A."},{"first_name":"Martin W","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","last_name":"HETZER","orcid":"0000-0002-2111-992X","full_name":"HETZER, Martin W"}],"external_id":{"pmid":["18786826"]},"article_processing_charge":"No","title":"Structure, dynamics and function of nuclear pore complexes","abstract":[{"text":"Nuclear pore complexes are large aqueous channels that penetrate the nuclear envelope, thereby connecting the nuclear interior with the cytoplasm. Until recently, these macromolecular complexes were viewed as static structures, the only function of which was to control the molecular trafficking between the two compartments. It has now become evident that this simplistic scenario is inaccurate and that nuclear pore complexes are highly dynamic multiprotein assemblies involved in diverse cellular processes ranging from the organization of the cytoskeleton to gene expression. In this review, we discuss the most recent developments in the nuclear-pore-complex field, focusing on the assembly, disassembly, maintenance and function of this macromolecular structure.","lang":"eng"}],"oa_version":"None","pmid":1,"scopus_import":"1","month":"10","intvolume":" 18","publication_identifier":{"issn":["0962-8924"]},"publication_status":"published","language":[{"iso":"eng"}],"volume":18,"issue":"10","_id":"11110","type":"journal_article","article_type":"review","status":"public","keyword":["Cell Biology"],"date_updated":"2022-07-18T08:55:33Z","extern":"1"},{"quality_controlled":"1","publisher":"Elsevier","page":"669-677","date_published":"2008-12-01T00:00:00Z","doi":"10.1016/j.ceb.2008.09.010","date_created":"2022-04-07T07:55:00Z","year":"2008","day":"01","publication":"Current Opinion in Cell Biology","author":[{"full_name":"Kutay, Ulrike","last_name":"Kutay","first_name":"Ulrike"},{"first_name":"Martin W","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","last_name":"HETZER","full_name":"HETZER, Martin W","orcid":"0000-0002-2111-992X"}],"external_id":{"pmid":["18938243"]},"article_processing_charge":"No","title":"Reorganization of the nuclear envelope during open mitosis","citation":{"chicago":"Kutay, Ulrike, and Martin Hetzer. “Reorganization of the Nuclear Envelope during Open Mitosis.” Current Opinion in Cell Biology. Elsevier, 2008. https://doi.org/10.1016/j.ceb.2008.09.010.","ista":"Kutay U, Hetzer M. 2008. Reorganization of the nuclear envelope during open mitosis. Current Opinion in Cell Biology. 20(6), 669–677.","mla":"Kutay, Ulrike, and Martin Hetzer. “Reorganization of the Nuclear Envelope during Open Mitosis.” Current Opinion in Cell Biology, vol. 20, no. 6, Elsevier, 2008, pp. 669–77, doi:10.1016/j.ceb.2008.09.010.","short":"U. Kutay, M. Hetzer, Current Opinion in Cell Biology 20 (2008) 669–677.","ieee":"U. Kutay and M. Hetzer, “Reorganization of the nuclear envelope during open mitosis,” Current Opinion in Cell Biology, vol. 20, no. 6. Elsevier, pp. 669–677, 2008.","apa":"Kutay, U., & Hetzer, M. (2008). Reorganization of the nuclear envelope during open mitosis. Current Opinion in Cell Biology. Elsevier. https://doi.org/10.1016/j.ceb.2008.09.010","ama":"Kutay U, Hetzer M. Reorganization of the nuclear envelope during open mitosis. Current Opinion in Cell Biology. 2008;20(6):669-677. doi:10.1016/j.ceb.2008.09.010"},"user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","scopus_import":"1","month":"12","intvolume":" 20","abstract":[{"lang":"eng","text":"The nuclear envelope (NE) provides a selective barrier between the nuclear interior and the cytoplasm and constitutes a central component of intracellular architecture. During mitosis in metazoa, the NE breaks down leading to the complete mixing of the nuclear content with the cytosol. Interestingly, many NE components actively participate in mitotic progression. After chromosome segregation, the NE is reassembled around decondensing chromatin and the nuclear compartment is reestablished in the daughter cells. Here, we summarize recent progress in deciphering the molecular mechanisms underlying NE dynamics during cell division."}],"oa_version":"None","pmid":1,"volume":20,"issue":"6","publication_identifier":{"issn":["0955-0674"]},"publication_status":"published","language":[{"iso":"eng"}],"article_type":"original","type":"journal_article","status":"public","keyword":["Cell Biology"],"_id":"11109","date_updated":"2022-07-18T08:55:32Z","extern":"1"},{"author":[{"last_name":"Anderson","full_name":"Anderson, Daniel J","first_name":"Daniel J"},{"last_name":"HETZER","full_name":"HETZER, Martin W","orcid":"0000-0002-2111-992X","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","first_name":"Martin W"}],"external_id":{"pmid":["18495454"]},"article_processing_charge":"No","title":"The life cycle of the metazoan nuclear envelope","citation":{"mla":"Anderson, Daniel J., and Martin Hetzer. “The Life Cycle of the Metazoan Nuclear Envelope.” Current Opinion in Cell Biology, vol. 20, no. 4, Elsevier, 2008, pp. 386–92, doi:10.1016/j.ceb.2008.03.016.","short":"D.J. Anderson, M. Hetzer, Current Opinion in Cell Biology 20 (2008) 386–392.","ieee":"D. J. Anderson and M. Hetzer, “The life cycle of the metazoan nuclear envelope,” Current Opinion in Cell Biology, vol. 20, no. 4. Elsevier, pp. 386–392, 2008.","ama":"Anderson DJ, Hetzer M. The life cycle of the metazoan nuclear envelope. Current Opinion in Cell Biology. 2008;20(4):386-392. doi:10.1016/j.ceb.2008.03.016","apa":"Anderson, D. J., & Hetzer, M. (2008). The life cycle of the metazoan nuclear envelope. Current Opinion in Cell Biology. Elsevier. https://doi.org/10.1016/j.ceb.2008.03.016","chicago":"Anderson, Daniel J, and Martin Hetzer. “The Life Cycle of the Metazoan Nuclear Envelope.” Current Opinion in Cell Biology. Elsevier, 2008. https://doi.org/10.1016/j.ceb.2008.03.016.","ista":"Anderson DJ, Hetzer M. 2008. The life cycle of the metazoan nuclear envelope. Current Opinion in Cell Biology. 20(4), 386–392."},"user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","page":"386-392","date_published":"2008-08-01T00:00:00Z","doi":"10.1016/j.ceb.2008.03.016","date_created":"2022-04-07T07:55:34Z","year":"2008","day":"01","publication":"Current Opinion in Cell Biology","quality_controlled":"1","publisher":"Elsevier","date_updated":"2022-07-18T08:56:07Z","extern":"1","article_type":"original","type":"journal_article","status":"public","keyword":["Cell Biology"],"_id":"11112","issue":"4","volume":20,"publication_identifier":{"issn":["0955-0674"]},"publication_status":"published","language":[{"iso":"eng"}],"scopus_import":"1","month":"08","intvolume":" 20","abstract":[{"text":"The nuclear envelope is a double-layered membrane that encloses the nuclear genome and transcriptional machinery. In dividing cells of metazoa, the nucleus completely disassembles during mitosis, creating the need to re-establish the nuclear compartment at the end of each cell division. Given the crucial role of the nuclear envelope in gene regulation and cellular organization, it is not surprising that its biogenesis and organization have become active research areas. We will review recent insights into nuclear membrane dynamics during the cell cycle.","lang":"eng"}],"oa_version":"None","pmid":1},{"_id":"11113","status":"public","keyword":["Cell Biology"],"type":"journal_article","article_type":"letter_note","extern":"1","date_updated":"2022-07-18T08:56:10Z","pmid":1,"oa_version":"Published Version","abstract":[{"lang":"eng","text":"The nuclear envelope (NE), a double membrane enclosing the nucleus of eukaryotic cells, controls the flow of information between the nucleoplasm and the cytoplasm and provides a scaffold for the organization of chromatin and the cytoskeleton. In dividing metazoan cells, the NE breaks down at the onset of mitosis and then reforms around segregated chromosomes to generate the daughter nuclei. Recent data from intact cells and cell-free nuclear assembly systems suggest that the endoplasmic reticulum (ER) is the source of membrane for NE assembly. At the end of mitosis, ER membrane tubules are targeted to chromatin via tubule ends and reorganized into flat nuclear membrane sheets by specific DNA-binding membrane proteins. In contrast to previous models, which proposed vesicle fusion to be the principal mechanism of NE formation, these new studies suggest that the nuclear membrane forms by the chromatin-mediated reshaping of the ER."}],"month":"01","intvolume":" 121","scopus_import":"1","main_file_link":[{"open_access":"1","url":"https://doi.org/10.1242/jcs.005777"}],"language":[{"iso":"eng"}],"publication_identifier":{"eissn":["1477-9137"],"issn":["0021-9533"]},"publication_status":"published","issue":"2","volume":121,"user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","citation":{"chicago":"Anderson, Daniel J., and Martin Hetzer. “Shaping the Endoplasmic Reticulum into the Nuclear Envelope.” Journal of Cell Science. The Company of Biologists, 2008. https://doi.org/10.1242/jcs.005777.","ista":"Anderson DJ, Hetzer M. 2008. Shaping the endoplasmic reticulum into the nuclear envelope. Journal of Cell Science. 121(2), 137–142.","mla":"Anderson, Daniel J., and Martin Hetzer. “Shaping the Endoplasmic Reticulum into the Nuclear Envelope.” Journal of Cell Science, vol. 121, no. 2, The Company of Biologists, 2008, pp. 137–42, doi:10.1242/jcs.005777.","ama":"Anderson DJ, Hetzer M. Shaping the endoplasmic reticulum into the nuclear envelope. Journal of Cell Science. 2008;121(2):137-142. doi:10.1242/jcs.005777","apa":"Anderson, D. J., & Hetzer, M. (2008). Shaping the endoplasmic reticulum into the nuclear envelope. Journal of Cell Science. The Company of Biologists. https://doi.org/10.1242/jcs.005777","short":"D.J. Anderson, M. Hetzer, Journal of Cell Science 121 (2008) 137–142.","ieee":"D. J. Anderson and M. Hetzer, “Shaping the endoplasmic reticulum into the nuclear envelope,” Journal of Cell Science, vol. 121, no. 2. The Company of Biologists, pp. 137–142, 2008."},"title":"Shaping the endoplasmic reticulum into the nuclear envelope","author":[{"first_name":"Daniel J.","last_name":"Anderson","full_name":"Anderson, Daniel J."},{"first_name":"Martin W","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","last_name":"HETZER","orcid":"0000-0002-2111-992X","full_name":"HETZER, Martin W"}],"article_processing_charge":"No","external_id":{"pmid":["18187447"]},"quality_controlled":"1","publisher":"The Company of Biologists","oa":1,"day":"15","publication":"Journal of Cell Science","year":"2008","date_published":"2008-01-15T00:00:00Z","doi":"10.1242/jcs.005777","date_created":"2022-04-07T07:55:46Z","page":"137-142"},{"status":"public","keyword":["Multidisciplinary"],"type":"journal_article","article_type":"original","_id":"11114","extern":"1","date_updated":"2022-07-18T08:56:36Z","month":"04","intvolume":" 3","scopus_import":"1","main_file_link":[{"url":" https://doi.org/10.1371/journal.pone.0002061","open_access":"1"}],"oa_version":"Published Version","pmid":1,"abstract":[{"text":"We present a miniaturized pull-down method for the detection of protein-protein interactions using standard affinity chromatography reagents. Binding events between different proteins, which are color-coded with quantum dots (QDs), are visualized on single affinity chromatography beads by fluorescence microscopy. The use of QDs for single molecule detection allows the simultaneous analysis of multiple protein-protein binding events and reduces the amount of time and material needed to perform a pull-down experiment.","lang":"eng"}],"volume":3,"issue":"4","language":[{"iso":"eng"}],"publication_identifier":{"issn":["1932-6203"]},"publication_status":"published","article_number":"e2061","title":"Single bead affinity detection (SINBAD) for the analysis of protein-protein interactions","author":[{"full_name":"Schulte, Roberta","last_name":"Schulte","first_name":"Roberta"},{"full_name":"Talamas, Jessica","last_name":"Talamas","first_name":"Jessica"},{"first_name":"Christine","full_name":"Doucet, Christine","last_name":"Doucet"},{"last_name":"HETZER","full_name":"HETZER, Martin W","orcid":"0000-0002-2111-992X","first_name":"Martin W","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed"}],"external_id":{"pmid":["18446240"]},"article_processing_charge":"No","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","citation":{"chicago":"Schulte, Roberta, Jessica Talamas, Christine Doucet, and Martin Hetzer. “Single Bead Affinity Detection (SINBAD) for the Analysis of Protein-Protein Interactions.” PLoS ONE. Public Library of Science, 2008. https://doi.org/10.1371/journal.pone.0002061.","ista":"Schulte R, Talamas J, Doucet C, Hetzer M. 2008. Single bead affinity detection (SINBAD) for the analysis of protein-protein interactions. PLoS ONE. 3(4), e2061.","mla":"Schulte, Roberta, et al. “Single Bead Affinity Detection (SINBAD) for the Analysis of Protein-Protein Interactions.” PLoS ONE, vol. 3, no. 4, e2061, Public Library of Science, 2008, doi:10.1371/journal.pone.0002061.","ama":"Schulte R, Talamas J, Doucet C, Hetzer M. Single bead affinity detection (SINBAD) for the analysis of protein-protein interactions. PLoS ONE. 2008;3(4). doi:10.1371/journal.pone.0002061","apa":"Schulte, R., Talamas, J., Doucet, C., & Hetzer, M. (2008). Single bead affinity detection (SINBAD) for the analysis of protein-protein interactions. PLoS ONE. Public Library of Science. https://doi.org/10.1371/journal.pone.0002061","ieee":"R. Schulte, J. Talamas, C. Doucet, and M. Hetzer, “Single bead affinity detection (SINBAD) for the analysis of protein-protein interactions,” PLoS ONE, vol. 3, no. 4. Public Library of Science, 2008.","short":"R. Schulte, J. Talamas, C. Doucet, M. Hetzer, PLoS ONE 3 (2008)."},"publisher":"Public Library of Science","quality_controlled":"1","oa":1,"doi":"10.1371/journal.pone.0002061","date_published":"2008-04-30T00:00:00Z","date_created":"2022-04-07T07:55:57Z","day":"30","publication":"PLoS ONE","year":"2008"},{"user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","citation":{"chicago":"Franz, Cerstin, Rudolf Walczak, Sevil Yavuz, Rachel Santarella, Marc Gentzel, Peter Askjaer, Vincent Galy, Martin Hetzer, Iain W Mattaj, and Wolfram Antonin. “MEL‐28/ELYS Is Required for the Recruitment of Nucleoporins to Chromatin and Postmitotic Nuclear Pore Complex Assembly.” EMBO Reports. EMBO, 2007. https://doi.org/10.1038/sj.embor.7400889.","ista":"Franz C, Walczak R, Yavuz S, Santarella R, Gentzel M, Askjaer P, Galy V, Hetzer M, Mattaj IW, Antonin W. 2007. MEL‐28/ELYS is required for the recruitment of nucleoporins to chromatin and postmitotic nuclear pore complex assembly. EMBO reports. 8(2), 165–172.","mla":"Franz, Cerstin, et al. “MEL‐28/ELYS Is Required for the Recruitment of Nucleoporins to Chromatin and Postmitotic Nuclear Pore Complex Assembly.” EMBO Reports, vol. 8, no. 2, EMBO, 2007, pp. 165–72, doi:10.1038/sj.embor.7400889.","ieee":"C. Franz et al., “MEL‐28/ELYS is required for the recruitment of nucleoporins to chromatin and postmitotic nuclear pore complex assembly,” EMBO reports, vol. 8, no. 2. EMBO, pp. 165–172, 2007.","short":"C. Franz, R. Walczak, S. Yavuz, R. Santarella, M. Gentzel, P. Askjaer, V. Galy, M. Hetzer, I.W. Mattaj, W. Antonin, EMBO Reports 8 (2007) 165–172.","apa":"Franz, C., Walczak, R., Yavuz, S., Santarella, R., Gentzel, M., Askjaer, P., … Antonin, W. (2007). MEL‐28/ELYS is required for the recruitment of nucleoporins to chromatin and postmitotic nuclear pore complex assembly. EMBO Reports. EMBO. https://doi.org/10.1038/sj.embor.7400889","ama":"Franz C, Walczak R, Yavuz S, et al. MEL‐28/ELYS is required for the recruitment of nucleoporins to chromatin and postmitotic nuclear pore complex assembly. EMBO reports. 2007;8(2):165-172. doi:10.1038/sj.embor.7400889"},"title":"MEL‐28/ELYS is required for the recruitment of nucleoporins to chromatin and postmitotic nuclear pore complex assembly","author":[{"first_name":"Cerstin","last_name":"Franz","full_name":"Franz, Cerstin"},{"last_name":"Walczak","full_name":"Walczak, Rudolf","first_name":"Rudolf"},{"full_name":"Yavuz, Sevil","last_name":"Yavuz","first_name":"Sevil"},{"first_name":"Rachel","last_name":"Santarella","full_name":"Santarella, Rachel"},{"first_name":"Marc","last_name":"Gentzel","full_name":"Gentzel, Marc"},{"first_name":"Peter","full_name":"Askjaer, Peter","last_name":"Askjaer"},{"full_name":"Galy, Vincent","last_name":"Galy","first_name":"Vincent"},{"full_name":"HETZER, Martin W","orcid":"0000-0002-2111-992X","last_name":"HETZER","first_name":"Martin W","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed"},{"first_name":"Iain W","last_name":"Mattaj","full_name":"Mattaj, Iain W"},{"first_name":"Wolfram","last_name":"Antonin","full_name":"Antonin, Wolfram"}],"external_id":{"pmid":["17235358"]},"article_processing_charge":"No","day":"19","publication":"EMBO reports","year":"2007","date_published":"2007-01-19T00:00:00Z","doi":"10.1038/sj.embor.7400889","date_created":"2022-04-07T07:56:13Z","page":"165-172","quality_controlled":"1","publisher":"EMBO","oa":1,"extern":"1","date_updated":"2022-07-18T08:56:40Z","_id":"11116","status":"public","keyword":["Genetics","Molecular Biology","Biochemistry"],"article_type":"original","type":"journal_article","language":[{"iso":"eng"}],"publication_identifier":{"issn":["1469-221X"],"eissn":["1469-3178"]},"publication_status":"published","volume":8,"issue":"2","pmid":1,"oa_version":"Published Version","abstract":[{"lang":"eng","text":"The metazoan nuclear envelope (NE) breaks down and re-forms during each cell cycle. Nuclear pore complexes (NPCs), which allow nucleocytoplasmic transport during interphase, assemble into the re-forming NE at the end of mitosis. Using in vitro NE assembly, we show that the vertebrate homologue of MEL-28 (maternal effect lethal), a recently discovered NE component in Caenorhabditis elegans, functions in postmitotic NPC assembly. MEL-28 interacts with the Nup107–160 complex (Nup for nucleoporin), an important building block of the NPC, and is essential for the recruitment of the Nup107–160 complex to chromatin. We suggest that MEL-28 acts as a seeding point for NPC assembly."}],"month":"01","intvolume":" 8","scopus_import":"1","main_file_link":[{"open_access":"1","url":"https://doi.org/10.1038/sj.embor.7400889"}]},{"scopus_import":"1","month":"09","intvolume":" 9","abstract":[{"text":"The formation of the nuclear envelope (NE) around chromatin is a major membrane-remodelling event that occurs during cell division of metazoa. It is unclear whether the nuclear membrane reforms by the fusion of NE fragments or if it re-emerges from an intact tubular network of the endoplasmic reticulum (ER). Here, we show that NE formation and expansion requires a tubular ER network and occurs efficiently in the presence of the membrane fusion inhibitor GTPγS. Chromatin recruitment of membranes, which is initiated by tubule-end binding, followed by the formation, expansion and sealing of flat membrane sheets, is mediated by DNA-binding proteins residing in the ER. Thus, chromatin plays an active role in reshaping of the ER during NE formation.","lang":"eng"}],"pmid":1,"oa_version":"None","volume":9,"issue":"10","publication_identifier":{"eissn":["1476-4679"],"issn":["1465-7392"]},"publication_status":"published","language":[{"iso":"eng"}],"type":"journal_article","article_type":"original","status":"public","keyword":["Cell Biology"],"_id":"11115","date_updated":"2022-07-18T08:56:38Z","extern":"1","publisher":"Springer Nature","quality_controlled":"1","page":"1160-1166","doi":"10.1038/ncb1636","date_published":"2007-09-09T00:00:00Z","date_created":"2022-04-07T07:56:04Z","year":"2007","day":"09","publication":"Nature Cell Biology","author":[{"first_name":"Daniel J.","full_name":"Anderson, Daniel J.","last_name":"Anderson"},{"id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","first_name":"Martin W","last_name":"HETZER","orcid":"0000-0002-2111-992X","full_name":"HETZER, Martin W"}],"article_processing_charge":"No","external_id":{"pmid":["17828249"]},"title":"Nuclear envelope formation by chromatin-mediated reorganization of the endoplasmic reticulum","citation":{"ieee":"D. J. Anderson and M. Hetzer, “Nuclear envelope formation by chromatin-mediated reorganization of the endoplasmic reticulum,” Nature Cell Biology, vol. 9, no. 10. Springer Nature, pp. 1160–1166, 2007.","short":"D.J. Anderson, M. Hetzer, Nature Cell Biology 9 (2007) 1160–1166.","apa":"Anderson, D. J., & Hetzer, M. (2007). Nuclear envelope formation by chromatin-mediated reorganization of the endoplasmic reticulum. Nature Cell Biology. Springer Nature. https://doi.org/10.1038/ncb1636","ama":"Anderson DJ, Hetzer M. Nuclear envelope formation by chromatin-mediated reorganization of the endoplasmic reticulum. Nature Cell Biology. 2007;9(10):1160-1166. doi:10.1038/ncb1636","mla":"Anderson, Daniel J., and Martin Hetzer. “Nuclear Envelope Formation by Chromatin-Mediated Reorganization of the Endoplasmic Reticulum.” Nature Cell Biology, vol. 9, no. 10, Springer Nature, 2007, pp. 1160–66, doi:10.1038/ncb1636.","ista":"Anderson DJ, Hetzer M. 2007. Nuclear envelope formation by chromatin-mediated reorganization of the endoplasmic reticulum. Nature Cell Biology. 9(10), 1160–1166.","chicago":"Anderson, Daniel J., and Martin Hetzer. “Nuclear Envelope Formation by Chromatin-Mediated Reorganization of the Endoplasmic Reticulum.” Nature Cell Biology. Springer Nature, 2007. https://doi.org/10.1038/ncb1636."},"user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd"},{"oa_version":"None","quality_controlled":"1","publisher":"Wiley","scopus_import":"1","month":"01","place":"Chichester, UK","publication_identifier":{"eisbn":["9780470033487 "],"isbn":["9780470847589 "]},"year":"2006","publication_status":"published","day":"27","language":[{"iso":"eng"}],"publication":"Cell Biology Protocols","page":"201-378","date_published":"2006-01-27T00:00:00Z","doi":"10.1002/0470033487.ch6","date_created":"2022-04-07T07:56:42Z","_id":"11119","type":"book_chapter","status":"public","date_updated":"2022-07-18T08:57:08Z","citation":{"ista":"Harris JR, Almouzni G, Kirschner D, Dimitrova D, Nickerson JA, Underwood J, Wagner S, Korbei B, Foisner R, Walther TC, Hetzer M, Peters R, Walev I, de Kroon AIPM, Staffhorst RWHM, de Kruijff B, Burger KNJ, Netto LES, Bertrand E, Alimonti JB, Greenberg AH, Xiao J, Pradhan A, Liu Y, Paiement J, Young R, Goñi FM, Villar A-V, Contreras F-X, Alonso A, Peter BJ, Mills IG, Higgins MK, Brown WJ, Chambers K, Doody A, Cheng CY, Mruk DD, Yang C, Kirchhoff H, Haase W, Boggasch S, Paulsen H, Benesova J, Liffers S-T, Rögner M, Gao Y, Sztul E, Thiemann M, Fahimi HD, Gniadecki R, Gajkowska B, Bane SL, Hess JF, Voss JC, Fitzgerald PG, Hisanaga S, Sasaki T, Uéda K, Town T, Tan J, Milton NGN, Chi R, Keller TCS, Kriajevska M, Bronstein I, Lukanidin E, Holmes DF, Kadler KE. 2006.In Vitro Techniques. In: Cell Biology Protocols. , 201–378.","chicago":"Harris, J. Robin, Geneviève Almouzni, Doris Kirschner, Daniela Dimitrova, Jeffrey A. Nickerson, Jean Underwood, Stefan Wagner, et al. “In Vitro Techniques.” In Cell Biology Protocols, edited by Robin Harris, John Graham, and David Rickwood, 201–378. Chichester, UK: Wiley, 2006. https://doi.org/10.1002/0470033487.ch6.","ama":"Harris JR, Almouzni G, Kirschner D, et al. In Vitro Techniques. In: Harris R, Graham J, Rickwood D, eds. Cell Biology Protocols. Chichester, UK: Wiley; 2006:201-378. doi:10.1002/0470033487.ch6","apa":"Harris, J. R., Almouzni, G., Kirschner, D., Dimitrova, D., Nickerson, J. A., Underwood, J., … Kadler, K. E. (2006). In Vitro Techniques. In R. Harris, J. Graham, & D. Rickwood (Eds.), Cell Biology Protocols (pp. 201–378). Chichester, UK: Wiley. https://doi.org/10.1002/0470033487.ch6","ieee":"J. R. Harris et al., “In Vitro Techniques,” in Cell Biology Protocols, R. Harris, J. Graham, and D. Rickwood, Eds. Chichester, UK: Wiley, 2006, pp. 201–378.","short":"J.R. Harris, G. Almouzni, D. Kirschner, D. Dimitrova, J.A. Nickerson, J. Underwood, S. Wagner, B. Korbei, R. Foisner, T.C. Walther, M. Hetzer, R. Peters, I. Walev, A.I.P.M. de Kroon, R.W.H.M. Staffhorst, B. de Kruijff, K.N.J. Burger, L.E.S. Netto, E. Bertrand, J.B. Alimonti, A.H. Greenberg, J. Xiao, A. Pradhan, Y. Liu, J. Paiement, R. Young, F.M. Goñi, A.-V. Villar, F.-X. Contreras, A. Alonso, B.J. Peter, I.G. Mills, M.K. Higgins, W.J. Brown, K. Chambers, A. Doody, C.Y. Cheng, D.D. Mruk, C. Yang, H. Kirchhoff, W. Haase, S. Boggasch, H. Paulsen, J. Benesova, S.-T. Liffers, M. Rögner, Y. Gao, E. Sztul, M. Thiemann, H.D. Fahimi, R. Gniadecki, B. Gajkowska, S.L. Bane, J.F. Hess, J.C. Voss, P.G. Fitzgerald, S. Hisanaga, T. Sasaki, K. Uéda, T. Town, J. Tan, N.G.N. Milton, R. Chi, T.C.S. Keller, M. Kriajevska, I. Bronstein, E. Lukanidin, D.F. Holmes, K.E. Kadler, in:, R. Harris, J. Graham, D. Rickwood (Eds.), Cell Biology Protocols, Wiley, Chichester, UK, 2006, pp. 201–378.","mla":"Harris, J. Robin, et al. “In Vitro Techniques.” Cell Biology Protocols, edited by Robin Harris et al., Wiley, 2006, pp. 201–378, doi:10.1002/0470033487.ch6."},"extern":"1","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","author":[{"last_name":"Harris","full_name":"Harris, J. Robin","first_name":"J. Robin"},{"full_name":"Almouzni, Geneviève","last_name":"Almouzni","first_name":"Geneviève"},{"full_name":"Kirschner, Doris","last_name":"Kirschner","first_name":"Doris"},{"full_name":"Dimitrova, Daniela","last_name":"Dimitrova","first_name":"Daniela"},{"first_name":"Jeffrey A.","last_name":"Nickerson","full_name":"Nickerson, Jeffrey A."},{"full_name":"Underwood, Jean","last_name":"Underwood","first_name":"Jean"},{"last_name":"Wagner","full_name":"Wagner, Stefan","first_name":"Stefan"},{"full_name":"Korbei, Barbara","last_name":"Korbei","first_name":"Barbara"},{"last_name":"Foisner","full_name":"Foisner, Roland","first_name":"Roland"},{"last_name":"Walther","full_name":"Walther, Tobias C.","first_name":"Tobias C."},{"first_name":"Martin W","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","full_name":"HETZER, Martin W","orcid":"0000-0002-2111-992X","last_name":"HETZER"},{"first_name":"Reiner","full_name":"Peters, Reiner","last_name":"Peters"},{"first_name":"Ivan","last_name":"Walev","full_name":"Walev, Ivan"},{"first_name":"Anton I. P. M.","full_name":"de Kroon, Anton I. P. M.","last_name":"de Kroon"},{"last_name":"Staffhorst","full_name":"Staffhorst, Rutger W. H. M.","first_name":"Rutger W. H. M."},{"first_name":"Ben","full_name":"de Kruijff, Ben","last_name":"de Kruijff"},{"full_name":"Burger, Koert N. J.","last_name":"Burger","first_name":"Koert N. J."},{"last_name":"Netto","full_name":"Netto, Luis Eduardo Soares","first_name":"Luis Eduardo Soares"},{"first_name":"Eric","last_name":"Bertrand","full_name":"Bertrand, Eric"},{"full_name":"Alimonti, Judie B.","last_name":"Alimonti","first_name":"Judie B."},{"full_name":"Greenberg, Arnold H.","last_name":"Greenberg","first_name":"Arnold H."},{"first_name":"Jinnan","last_name":"Xiao","full_name":"Xiao, Jinnan"},{"last_name":"Pradhan","full_name":"Pradhan, Anuradha","first_name":"Anuradha"},{"first_name":"Yuechueng","last_name":"Liu","full_name":"Liu, Yuechueng"},{"full_name":"Paiement, Jacques","last_name":"Paiement","first_name":"Jacques"},{"full_name":"Young, Robin","last_name":"Young","first_name":"Robin"},{"first_name":"Félix M.","last_name":"Goñi","full_name":"Goñi, Félix M."},{"full_name":"Villar, Ana-Victoria","last_name":"Villar","first_name":"Ana-Victoria"},{"first_name":"F.-Xabier","last_name":"Contreras","full_name":"Contreras, F.-Xabier"},{"last_name":"Alonso","full_name":"Alonso, Alicia","first_name":"Alicia"},{"first_name":"Brian J.","last_name":"Peter","full_name":"Peter, Brian J."},{"first_name":"Ian G.","last_name":"Mills","full_name":"Mills, Ian G."},{"first_name":"Matthew K.","last_name":"Higgins","full_name":"Higgins, Matthew K."},{"last_name":"Brown","full_name":"Brown, William J.","first_name":"William J."},{"last_name":"Chambers","full_name":"Chambers, K.","first_name":"K."},{"full_name":"Doody, A.","last_name":"Doody","first_name":"A."},{"first_name":"C. Yan","full_name":"Cheng, C. Yan","last_name":"Cheng"},{"full_name":"Mruk, Dolores D.","last_name":"Mruk","first_name":"Dolores D."},{"last_name":"Yang","full_name":"Yang, Chunhong","first_name":"Chunhong"},{"first_name":"Helmut","full_name":"Kirchhoff, Helmut","last_name":"Kirchhoff"},{"first_name":"Winfried","last_name":"Haase","full_name":"Haase, Winfried"},{"first_name":"Stephanie","last_name":"Boggasch","full_name":"Boggasch, Stephanie"},{"first_name":"Harald","last_name":"Paulsen","full_name":"Paulsen, Harald"},{"first_name":"Julie","full_name":"Benesova, Julie","last_name":"Benesova"},{"last_name":"Liffers","full_name":"Liffers, Sven-T.","first_name":"Sven-T."},{"full_name":"Rögner, Matthias","last_name":"Rögner","first_name":"Matthias"},{"first_name":"Ya-sheng","full_name":"Gao, Ya-sheng","last_name":"Gao"},{"first_name":"Elizabeth","last_name":"Sztul","full_name":"Sztul, Elizabeth"},{"first_name":"Meinolf","full_name":"Thiemann, Meinolf","last_name":"Thiemann"},{"last_name":"Fahimi","full_name":"Fahimi, H. Dariush","first_name":"H. Dariush"},{"first_name":"Robert","full_name":"Gniadecki, Robert","last_name":"Gniadecki"},{"first_name":"Barbara","full_name":"Gajkowska, Barbara","last_name":"Gajkowska"},{"last_name":"Bane","full_name":"Bane, Susan L.","first_name":"Susan L."},{"first_name":"John F.","full_name":"Hess, John F.","last_name":"Hess"},{"full_name":"Voss, John C.","last_name":"Voss","first_name":"John C."},{"first_name":"Paul G.","full_name":"Fitzgerald, Paul G.","last_name":"Fitzgerald"},{"first_name":"Shin-ichi","last_name":"Hisanaga","full_name":"Hisanaga, Shin-ichi"},{"first_name":"Takahiro","full_name":"Sasaki, Takahiro","last_name":"Sasaki"},{"first_name":"Kenji","last_name":"Uéda","full_name":"Uéda, Kenji"},{"full_name":"Town, Terrence","last_name":"Town","first_name":"Terrence"},{"first_name":"Jun","full_name":"Tan, Jun","last_name":"Tan"},{"last_name":"Milton","full_name":"Milton, Nathaniel G. N.","first_name":"Nathaniel G. N."},{"full_name":"Chi, Richard","last_name":"Chi","first_name":"Richard"},{"last_name":"Keller","full_name":"Keller, Thomas C. S.","first_name":"Thomas C. S."},{"first_name":"Marina","last_name":"Kriajevska","full_name":"Kriajevska, Marina"},{"full_name":"Bronstein, Igor","last_name":"Bronstein","first_name":"Igor"},{"first_name":"Eugene","full_name":"Lukanidin, Eugene","last_name":"Lukanidin"},{"full_name":"Holmes, David F.","last_name":"Holmes","first_name":"David F."},{"last_name":"Kadler","full_name":"Kadler, Karl E.","first_name":"Karl E."}],"article_processing_charge":"No","editor":[{"last_name":"Harris","full_name":"Harris, Robin","first_name":"Robin"},{"first_name":"John","full_name":"Graham, John","last_name":"Graham"},{"full_name":"Rickwood, David","last_name":"Rickwood","first_name":"David"}],"title":"In Vitro Techniques"},{"volume":63,"issue":"3","publication_status":"published","publication_identifier":{"issn":["1420-682X"],"eissn":["1420-9071"]},"language":[{"iso":"eng"}],"scopus_import":"1","intvolume":" 63","month":"01","abstract":[{"text":"Over the last years it has become evident that the nuclear envelope (NE) is more than a passive membrane barrier that separates the nucleus from the cytoplasm. The NE not only controls the trafficking of macromolecules between the nucleoplasm and the cytosol, but also provides anchoring sites for chromosomes and cytoskeleton to the nuclear periphery. Targeting of chromatin to the NE might actually be part of gene expression regulation in eukaryotes. Mutations in certain NE proteins are associated with a diversity of human diseases, including muscular dystrophy, neuropathy, lipodistrophy, torsion dystonia and the premature aging condition progeria. Despite the importance of the NE for cell division and differentiation, relatively little is known about its biogenesis and its role in human diseases. It is our goal to provide a comprehensive view of the NE and to discuss possible implications of NE-associated changes for gene expression, chromatin organization and signal transduction.","lang":"eng"}],"oa_version":"None","pmid":1,"date_updated":"2022-07-18T08:56:58Z","extern":"1","type":"journal_article","article_type":"review","keyword":["Cell Biology","Cellular and Molecular Neuroscience","Pharmacology","Molecular Biology","Molecular Medicine"],"status":"public","_id":"11117","page":"316-332","date_created":"2022-04-07T07:56:22Z","date_published":"2006-01-02T00:00:00Z","doi":"10.1007/s00018-005-5361-3","year":"2006","publication":"Cellular and Molecular Life Sciences","day":"02","quality_controlled":"1","publisher":"Springer Nature","external_id":{"pmid":["16389459"]},"article_processing_charge":"No","author":[{"first_name":"M. A.","full_name":"D’Angelo, M. A.","last_name":"D’Angelo"},{"id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","first_name":"Martin W","full_name":"HETZER, Martin W","orcid":"0000-0002-2111-992X","last_name":"HETZER"}],"title":"The role of the nuclear envelope in cellular organization","citation":{"ama":"D’Angelo MA, Hetzer M. The role of the nuclear envelope in cellular organization. Cellular and Molecular Life Sciences. 2006;63(3):316-332. doi:10.1007/s00018-005-5361-3","apa":"D’Angelo, M. A., & Hetzer, M. (2006). The role of the nuclear envelope in cellular organization. Cellular and Molecular Life Sciences. Springer Nature. https://doi.org/10.1007/s00018-005-5361-3","ieee":"M. A. D’Angelo and M. Hetzer, “The role of the nuclear envelope in cellular organization,” Cellular and Molecular Life Sciences, vol. 63, no. 3. Springer Nature, pp. 316–332, 2006.","short":"M.A. D’Angelo, M. Hetzer, Cellular and Molecular Life Sciences 63 (2006) 316–332.","mla":"D’Angelo, M. A., and Martin Hetzer. “The Role of the Nuclear Envelope in Cellular Organization.” Cellular and Molecular Life Sciences, vol. 63, no. 3, Springer Nature, 2006, pp. 316–32, doi:10.1007/s00018-005-5361-3.","ista":"D’Angelo MA, Hetzer M. 2006. The role of the nuclear envelope in cellular organization. Cellular and Molecular Life Sciences. 63(3), 316–332.","chicago":"D’Angelo, M. A., and Martin Hetzer. “The Role of the Nuclear Envelope in Cellular Organization.” Cellular and Molecular Life Sciences. Springer Nature, 2006. https://doi.org/10.1007/s00018-005-5361-3."},"user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd"},{"publication_identifier":{"issn":["0036-8075","1095-9203"]},"publication_status":"published","language":[{"iso":"eng"}],"volume":312,"issue":"5772","abstract":[{"text":"Nuclear pore complexes are multiprotein channels that span the double lipid bilayer of the nuclear envelope. How new pores are inserted into the intact nuclear envelope of proliferating and differentiating eukaryotic cells is unknown. We found that the Nup107-160 complex was incorporated into assembly sites in the nuclear envelope from both the nucleoplasmic and the cytoplasmic sides. Nuclear pore insertion required the generation of Ran guanosine triphosphate in the nuclear and cytoplasmic compartments. Newly formed nuclear pore complexes did not contain structural components of preexisting pores, suggesting that they can form de novo.","lang":"eng"}],"pmid":1,"oa_version":"None","scopus_import":"1","month":"04","intvolume":" 312","date_updated":"2022-07-18T08:57:04Z","extern":"1","_id":"11118","article_type":"original","type":"journal_article","status":"public","keyword":["Multidisciplinary"],"year":"2006","day":"21","publication":"Science","page":"440-443","date_published":"2006-04-21T00:00:00Z","doi":"10.1126/science.1124196","date_created":"2022-04-07T07:56:32Z","quality_controlled":"1","publisher":"American Association for the Advancement of Science","citation":{"ieee":"M. A. D’Angelo, D. J. Anderson, E. Richard, and M. Hetzer, “Nuclear pores form de novo from both sides of the nuclear envelope,” Science, vol. 312, no. 5772. American Association for the Advancement of Science, pp. 440–443, 2006.","short":"M.A. D’Angelo, D.J. Anderson, E. Richard, M. Hetzer, Science 312 (2006) 440–443.","apa":"D’Angelo, M. A., Anderson, D. J., Richard, E., & Hetzer, M. (2006). Nuclear pores form de novo from both sides of the nuclear envelope. Science. American Association for the Advancement of Science. https://doi.org/10.1126/science.1124196","ama":"D’Angelo MA, Anderson DJ, Richard E, Hetzer M. Nuclear pores form de novo from both sides of the nuclear envelope. Science. 2006;312(5772):440-443. doi:10.1126/science.1124196","mla":"D’Angelo, Maximiliano A., et al. “Nuclear Pores Form de Novo from Both Sides of the Nuclear Envelope.” Science, vol. 312, no. 5772, American Association for the Advancement of Science, 2006, pp. 440–43, doi:10.1126/science.1124196.","ista":"D’Angelo MA, Anderson DJ, Richard E, Hetzer M. 2006. Nuclear pores form de novo from both sides of the nuclear envelope. Science. 312(5772), 440–443.","chicago":"D’Angelo, Maximiliano A., Daniel J. Anderson, Erin Richard, and Martin Hetzer. “Nuclear Pores Form de Novo from Both Sides of the Nuclear Envelope.” Science. American Association for the Advancement of Science, 2006. https://doi.org/10.1126/science.1124196."},"user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","author":[{"last_name":"D'Angelo","full_name":"D'Angelo, Maximiliano A.","first_name":"Maximiliano A."},{"full_name":"Anderson, Daniel J.","last_name":"Anderson","first_name":"Daniel J."},{"full_name":"Richard, Erin","last_name":"Richard","first_name":"Erin"},{"first_name":"Martin W","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","orcid":"0000-0002-2111-992X","full_name":"HETZER, Martin W","last_name":"HETZER"}],"article_processing_charge":"No","external_id":{"pmid":["16627745"]},"title":"Nuclear pores form de novo from both sides of the nuclear envelope"},{"user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","citation":{"ista":"Hetzer M, Walther TC, Mattaj IW. 2005. Pushing the envelope: Structure, function, and dynamics of the nuclear periphery. Annual Review of Cell and Developmental Biology. 21, 347–380.","chicago":"Hetzer, Martin, Tobias C. Walther, and Iain W. Mattaj. “Pushing the Envelope: Structure, Function, and Dynamics of the Nuclear Periphery.” Annual Review of Cell and Developmental Biology. Annual Reviews, 2005. https://doi.org/10.1146/annurev.cellbio.21.090704.151152.","apa":"Hetzer, M., Walther, T. C., & Mattaj, I. W. (2005). Pushing the envelope: Structure, function, and dynamics of the nuclear periphery. Annual Review of Cell and Developmental Biology. Annual Reviews. https://doi.org/10.1146/annurev.cellbio.21.090704.151152","ama":"Hetzer M, Walther TC, Mattaj IW. Pushing the envelope: Structure, function, and dynamics of the nuclear periphery. Annual Review of Cell and Developmental Biology. 2005;21:347-380. doi:10.1146/annurev.cellbio.21.090704.151152","short":"M. Hetzer, T.C. Walther, I.W. Mattaj, Annual Review of Cell and Developmental Biology 21 (2005) 347–380.","ieee":"M. Hetzer, T. C. Walther, and I. W. Mattaj, “Pushing the envelope: Structure, function, and dynamics of the nuclear periphery,” Annual Review of Cell and Developmental Biology, vol. 21. Annual Reviews, pp. 347–380, 2005.","mla":"Hetzer, Martin, et al. “Pushing the Envelope: Structure, Function, and Dynamics of the Nuclear Periphery.” Annual Review of Cell and Developmental Biology, vol. 21, Annual Reviews, 2005, pp. 347–80, doi:10.1146/annurev.cellbio.21.090704.151152."},"title":"Pushing the envelope: Structure, function, and dynamics of the nuclear periphery","author":[{"last_name":"HETZER","orcid":"0000-0002-2111-992X","full_name":"HETZER, Martin W","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","first_name":"Martin W"},{"first_name":"Tobias C.","full_name":"Walther, Tobias C.","last_name":"Walther"},{"last_name":"Mattaj","full_name":"Mattaj, Iain W.","first_name":"Iain W."}],"external_id":{"pmid":["16212499"]},"article_processing_charge":"No","publisher":"Annual Reviews","quality_controlled":"1","day":"10","publication":"Annual Review of Cell and Developmental Biology","year":"2005","doi":"10.1146/annurev.cellbio.21.090704.151152","date_published":"2005-11-10T00:00:00Z","date_created":"2022-04-07T07:56:52Z","page":"347-380","_id":"11120","status":"public","keyword":["Cell Biology","Developmental Biology"],"article_type":"original","type":"journal_article","extern":"1","date_updated":"2022-07-18T08:57:34Z","pmid":1,"oa_version":"None","abstract":[{"text":"The nuclear envelope (NE) is a highly specialized membrane that delineates the eukaryotic cell nucleus. It is composed of the inner and outer nuclear membranes, nuclear pore complexes (NPCs) and, in metazoa, the lamina. The NE not only regulates the trafficking of macromolecules between nucleoplasm and cytosol but also provides anchoring sites for chromatin and the cytoskeleton. Through these interactions, the NE helps position the nucleus within the cell and chromosomes within the nucleus, thereby regulating the expression of certain genes. The NE is not static, rather it is continuously remodeled during cell division. The most dramatic example of NE reorganization occurs during mitosis in metazoa when the NE undergoes a complete cycle of disassembly and reformation. Despite the importance of the NE for eukaryotic cell life, relatively little is known about its biogenesis or many of its functions. We thus are far from understanding the molecular etiology of a diverse group of NE-associated diseases.","lang":"eng"}],"month":"11","intvolume":" 21","scopus_import":"1","language":[{"iso":"eng"}],"publication_identifier":{"issn":["1081-0706"],"eissn":["1530-8995"]},"publication_status":"published","volume":21},{"title":"The conserved Nup107-160 complex is critical for nuclear pore complex assembly","article_processing_charge":"No","external_id":{"pmid":["12705868"]},"author":[{"last_name":"Walther","full_name":"Walther, Tobias C.","first_name":"Tobias C."},{"first_name":"Annabelle","full_name":"Alves, Annabelle","last_name":"Alves"},{"last_name":"Pickersgill","full_name":"Pickersgill, Helen","first_name":"Helen"},{"first_name":"Isabelle","last_name":"Loı̈odice","full_name":"Loı̈odice, Isabelle"},{"full_name":"HETZER, Martin W","orcid":"0000-0002-2111-992X","last_name":"HETZER","first_name":"Martin W","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed"},{"first_name":"Vincent","full_name":"Galy, Vincent","last_name":"Galy"},{"last_name":"Hülsmann","full_name":"Hülsmann, Bastian B.","first_name":"Bastian B."},{"first_name":"Thomas","full_name":"Köcher, Thomas","last_name":"Köcher"},{"full_name":"Wilm, Matthias","last_name":"Wilm","first_name":"Matthias"},{"first_name":"Terry","full_name":"Allen, Terry","last_name":"Allen"},{"first_name":"Iain W.","last_name":"Mattaj","full_name":"Mattaj, Iain W."},{"last_name":"Doye","full_name":"Doye, Valérie","first_name":"Valérie"}],"user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","citation":{"ista":"Walther TC, Alves A, Pickersgill H, Loı̈odice I, Hetzer M, Galy V, Hülsmann BB, Köcher T, Wilm M, Allen T, Mattaj IW, Doye V. 2003. The conserved Nup107-160 complex is critical for nuclear pore complex assembly. Cell. 113(2), 195–206.","chicago":"Walther, Tobias C., Annabelle Alves, Helen Pickersgill, Isabelle Loı̈odice, Martin Hetzer, Vincent Galy, Bastian B. Hülsmann, et al. “The Conserved Nup107-160 Complex Is Critical for Nuclear Pore Complex Assembly.” Cell. Elsevier, 2003. https://doi.org/10.1016/s0092-8674(03)00235-6.","short":"T.C. Walther, A. Alves, H. Pickersgill, I. Loı̈odice, M. Hetzer, V. Galy, B.B. Hülsmann, T. Köcher, M. Wilm, T. Allen, I.W. Mattaj, V. Doye, Cell 113 (2003) 195–206.","ieee":"T. C. Walther et al., “The conserved Nup107-160 complex is critical for nuclear pore complex assembly,” Cell, vol. 113, no. 2. Elsevier, pp. 195–206, 2003.","ama":"Walther TC, Alves A, Pickersgill H, et al. The conserved Nup107-160 complex is critical for nuclear pore complex assembly. Cell. 2003;113(2):195-206. doi:10.1016/s0092-8674(03)00235-6","apa":"Walther, T. C., Alves, A., Pickersgill, H., Loı̈odice, I., Hetzer, M., Galy, V., … Doye, V. (2003). The conserved Nup107-160 complex is critical for nuclear pore complex assembly. Cell. Elsevier. https://doi.org/10.1016/s0092-8674(03)00235-6","mla":"Walther, Tobias C., et al. “The Conserved Nup107-160 Complex Is Critical for Nuclear Pore Complex Assembly.” Cell, vol. 113, no. 2, Elsevier, 2003, pp. 195–206, doi:10.1016/s0092-8674(03)00235-6."},"date_created":"2022-04-07T07:57:10Z","date_published":"2003-04-17T00:00:00Z","doi":"10.1016/s0092-8674(03)00235-6","page":"195-206","publication":"Cell","day":"17","year":"2003","publisher":"Elsevier","quality_controlled":"1","extern":"1","date_updated":"2022-07-18T08:57:42Z","keyword":["General Biochemistry","Genetics and Molecular Biology"],"status":"public","type":"journal_article","article_type":"original","_id":"11122","volume":113,"issue":"2","language":[{"iso":"eng"}],"publication_status":"published","publication_identifier":{"issn":["0092-8674"]},"intvolume":" 113","month":"04","scopus_import":"1","oa_version":"Published Version","pmid":1,"abstract":[{"text":"Nuclear pore complexes (NPCs) are large multiprotein assemblies that allow traffic between the cytoplasm and the nucleus. During mitosis in higher eukaryotes, the Nuclear Envelope (NE) breaks down and NPCs disassemble. How NPCs reassemble and incorporate into the NE upon mitotic exit is poorly understood. We demonstrate a function for the conserved Nup107-160 complex in this process. Partial in vivo depletion of Nup133 or Nup107 via RNAi in HeLa cells resulted in reduced levels of multiple nucleoporins and decreased NPC density in the NE. Immunodepletion of the entire Nup107-160 complex from in vitro nuclear assembly reactions produced nuclei with a continuous NE but no NPCs. This phenotype was reversible only if Nup107-160 complex was readded before closed NE formation. Depletion also prevented association of FG-repeat nucleoporins with chromatin. We propose a stepwise model in which postmitotic NPC assembly initiates on chromatin via early recruitment of the Nup107-160 complex.","lang":"eng"}]},{"publisher":"Springer Nature","quality_controlled":"1","year":"2003","publication":"Nature","day":"30","page":"689-694","date_created":"2022-04-07T07:57:02Z","doi":"10.1038/nature01898","date_published":"2003-07-30T00:00:00Z","citation":{"mla":"Walther, Tobias C., et al. “RanGTP Mediates Nuclear Pore Complex Assembly.” Nature, vol. 424, no. 6949, Springer Nature, 2003, pp. 689–94, doi:10.1038/nature01898.","apa":"Walther, T. C., Askjaer, P., Gentzel, M., Habermann, A., Griffiths, G., Wilm, M., … Hetzer, M. (2003). RanGTP mediates nuclear pore complex assembly. Nature. Springer Nature. https://doi.org/10.1038/nature01898","ama":"Walther TC, Askjaer P, Gentzel M, et al. RanGTP mediates nuclear pore complex assembly. Nature. 2003;424(6949):689-694. doi:10.1038/nature01898","short":"T.C. Walther, P. Askjaer, M. Gentzel, A. Habermann, G. Griffiths, M. Wilm, I.W. Mattaj, M. Hetzer, Nature 424 (2003) 689–694.","ieee":"T. C. Walther et al., “RanGTP mediates nuclear pore complex assembly,” Nature, vol. 424, no. 6949. Springer Nature, pp. 689–694, 2003.","chicago":"Walther, Tobias C., Peter Askjaer, Marc Gentzel, Anja Habermann, Gareth Griffiths, Matthias Wilm, Iain W. Mattaj, and Martin Hetzer. “RanGTP Mediates Nuclear Pore Complex Assembly.” Nature. Springer Nature, 2003. https://doi.org/10.1038/nature01898.","ista":"Walther TC, Askjaer P, Gentzel M, Habermann A, Griffiths G, Wilm M, Mattaj IW, Hetzer M. 2003. RanGTP mediates nuclear pore complex assembly. Nature. 424(6949), 689–694."},"user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","external_id":{"pmid":["12894213"]},"article_processing_charge":"No","author":[{"first_name":"Tobias C.","full_name":"Walther, Tobias C.","last_name":"Walther"},{"first_name":"Peter","last_name":"Askjaer","full_name":"Askjaer, Peter"},{"first_name":"Marc","last_name":"Gentzel","full_name":"Gentzel, Marc"},{"full_name":"Habermann, Anja","last_name":"Habermann","first_name":"Anja"},{"full_name":"Griffiths, Gareth","last_name":"Griffiths","first_name":"Gareth"},{"first_name":"Matthias","full_name":"Wilm, Matthias","last_name":"Wilm"},{"full_name":"Mattaj, Iain W.","last_name":"Mattaj","first_name":"Iain W."},{"first_name":"Martin W","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","full_name":"HETZER, Martin W","orcid":"0000-0002-2111-992X","last_name":"HETZER"}],"title":"RanGTP mediates nuclear pore complex assembly","abstract":[{"lang":"eng","text":"In metazoa, the nuclear envelope breaks down and reforms during each cell cycle. Nuclear pore complexes (NPCs), which serve as channels for transport between the nucleus and cytoplasm1, assemble into the reforming nuclear envelope in a sequential process involving association of a subset of NPC proteins, nucleoporins, with chromatin followed by the formation of a closed nuclear envelope fenestrated by NPCs2,3,4,5,6,7. How chromatin recruitment of nucleoporins and NPC assembly are regulated is unknown. Here we demonstrate that RanGTP production is required to dissociate nucleoporins Nup107, Nup153 and Nup358 from Importin β, to target them to chromatin and to induce association between separate NPC subcomplexes. Additionally, either an excess of RanGTP or removal of Importin β induces formation of NPC-containing membrane structures—annulate lamellae—both in vitro in the absence of chromatin and in vivo. Annulate lamellae formation is strongly and specifically inhibited by an excess of Importin β. The data demonstrate that RanGTP triggers distinct steps of NPC assembly, and suggest a mechanism for the spatial restriction of NPC assembly to the surface of chromatin."}],"pmid":1,"oa_version":"None","scopus_import":"1","intvolume":" 424","month":"07","publication_status":"published","publication_identifier":{"issn":["0028-0836"],"eissn":["1476-4687"]},"language":[{"iso":"eng"}],"issue":"6949","volume":424,"_id":"11121","type":"journal_article","article_type":"original","keyword":["Multidisciplinary"],"status":"public","date_updated":"2022-07-18T08:57:40Z","extern":"1"},{"day":"09","publication":"Current Biology","year":"2002","doi":"10.1016/s0960-9822(02)00927-2","date_published":"2002-07-09T00:00:00Z","date_created":"2022-04-07T07:57:31Z","page":"1151-1156","quality_controlled":"1","publisher":"Elsevier BV","oa":1,"user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","citation":{"mla":"Bilbao-Cortés, Daniel, et al. “Ran Binds to Chromatin by Two Distinct Mechanisms.” Current Biology, vol. 12, no. 13, Elsevier BV, 2002, pp. 1151–56, doi:10.1016/s0960-9822(02)00927-2.","apa":"Bilbao-Cortés, D., Hetzer, M., Längst, G., Becker, P. B., & Mattaj, I. W. (2002). Ran binds to chromatin by two distinct mechanisms. Current Biology. Elsevier BV. https://doi.org/10.1016/s0960-9822(02)00927-2","ama":"Bilbao-Cortés D, Hetzer M, Längst G, Becker PB, Mattaj IW. Ran binds to chromatin by two distinct mechanisms. Current Biology. 2002;12(13):1151-1156. doi:10.1016/s0960-9822(02)00927-2","short":"D. Bilbao-Cortés, M. Hetzer, G. Längst, P.B. Becker, I.W. Mattaj, Current Biology 12 (2002) 1151–1156.","ieee":"D. Bilbao-Cortés, M. Hetzer, G. Längst, P. B. Becker, and I. W. Mattaj, “Ran binds to chromatin by two distinct mechanisms,” Current Biology, vol. 12, no. 13. Elsevier BV, pp. 1151–1156, 2002.","chicago":"Bilbao-Cortés, Daniel, Martin Hetzer, Gernot Längst, Peter B. Becker, and Iain W. Mattaj. “Ran Binds to Chromatin by Two Distinct Mechanisms.” Current Biology. Elsevier BV, 2002. https://doi.org/10.1016/s0960-9822(02)00927-2.","ista":"Bilbao-Cortés D, Hetzer M, Längst G, Becker PB, Mattaj IW. 2002. Ran binds to chromatin by two distinct mechanisms. Current Biology. 12(13), 1151–1156."},"title":"Ran binds to chromatin by two distinct mechanisms","author":[{"first_name":"Daniel","full_name":"Bilbao-Cortés, Daniel","last_name":"Bilbao-Cortés"},{"full_name":"HETZER, Martin W","orcid":"0000-0002-2111-992X","last_name":"HETZER","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","first_name":"Martin W"},{"full_name":"Längst, Gernot","last_name":"Längst","first_name":"Gernot"},{"last_name":"Becker","full_name":"Becker, Peter B.","first_name":"Peter B."},{"full_name":"Mattaj, Iain W.","last_name":"Mattaj","first_name":"Iain W."}],"article_processing_charge":"No","external_id":{"pmid":["12121625"]},"language":[{"iso":"eng"}],"publication_identifier":{"issn":["0960-9822"]},"publication_status":"published","volume":12,"issue":"13","oa_version":"Published Version","pmid":1,"abstract":[{"lang":"eng","text":"Ran GTPase plays important roles in nucleocytoplasmic transport in interphase [1, 2] and in both spindle formation and nuclear envelope (NE) assembly during mitosis [3, 4, 5]. The latter functions rely on the presence of high local concentrations of GTP-bound Ran near mitotic chromatin [3, 4, 5]. RanGTP localization has been proposed to result from the association of Ran's GDP/GTP exchange factor, RCC1, with chromatin [6, 7, 8, 9], but Ran is shown here to bind directly to chromatin in two modes, either dependent or independent of RCC1, and, where bound, to increase the affinity of chromatin for NE membranes. We propose that the Ran binding capacity of chromatin contributes to localized spindle and NE assembly."}],"month":"07","intvolume":" 12","scopus_import":"1","main_file_link":[{"url":"https://doi.org/10.1016/S0960-9822(02)00927-2","open_access":"1"}],"extern":"1","date_updated":"2022-07-18T08:58:05Z","_id":"11124","status":"public","keyword":["General Agricultural and Biological Sciences","General Biochemistry","Genetics and Molecular Biology"],"type":"journal_article","article_type":"letter_note"},{"title":"The Ran GTPase as a marker of chromosome position in spindle formation and nuclear envelope assembly","article_processing_charge":"No","external_id":{"pmid":["12105431"]},"author":[{"first_name":"Martin W","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","full_name":"HETZER, Martin W","orcid":"0000-0002-2111-992X","last_name":"HETZER"},{"first_name":"Oliver J.","last_name":"Gruss","full_name":"Gruss, Oliver J."},{"first_name":"Iain W.","full_name":"Mattaj, Iain W.","last_name":"Mattaj"}],"user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","citation":{"mla":"Hetzer, Martin, et al. “The Ran GTPase as a Marker of Chromosome Position in Spindle Formation and Nuclear Envelope Assembly.” Nature Cell Biology, vol. 4, no. 7, Springer Nature, 2002, pp. E177–84, doi:10.1038/ncb0702-e177.","ieee":"M. Hetzer, O. J. Gruss, and I. W. Mattaj, “The Ran GTPase as a marker of chromosome position in spindle formation and nuclear envelope assembly,” Nature Cell Biology, vol. 4, no. 7. Springer Nature, pp. E177–E184, 2002.","short":"M. Hetzer, O.J. Gruss, I.W. Mattaj, Nature Cell Biology 4 (2002) E177–E184.","ama":"Hetzer M, Gruss OJ, Mattaj IW. The Ran GTPase as a marker of chromosome position in spindle formation and nuclear envelope assembly. Nature Cell Biology. 2002;4(7):E177-E184. doi:10.1038/ncb0702-e177","apa":"Hetzer, M., Gruss, O. J., & Mattaj, I. W. (2002). The Ran GTPase as a marker of chromosome position in spindle formation and nuclear envelope assembly. Nature Cell Biology. Springer Nature. https://doi.org/10.1038/ncb0702-e177","chicago":"Hetzer, Martin, Oliver J. Gruss, and Iain W. Mattaj. “The Ran GTPase as a Marker of Chromosome Position in Spindle Formation and Nuclear Envelope Assembly.” Nature Cell Biology. Springer Nature, 2002. https://doi.org/10.1038/ncb0702-e177.","ista":"Hetzer M, Gruss OJ, Mattaj IW. 2002. The Ran GTPase as a marker of chromosome position in spindle formation and nuclear envelope assembly. Nature Cell Biology. 4(7), E177–E184."},"publisher":"Springer Nature","quality_controlled":"1","date_created":"2022-04-07T07:57:19Z","date_published":"2002-07-01T00:00:00Z","doi":"10.1038/ncb0702-e177","page":"E177-E184","publication":"Nature Cell Biology","day":"01","year":"2002","keyword":["Cell Biology"],"status":"public","article_type":"original","type":"journal_article","_id":"11123","extern":"1","date_updated":"2022-07-18T08:58:03Z","intvolume":" 4","month":"07","scopus_import":"1","oa_version":"None","pmid":1,"abstract":[{"lang":"eng","text":"The small GTPase Ran is a key regulator of nucleocytoplasmic transport during interphase. The asymmetric distribution of the GTP-bound form of Ran across the nuclear envelope — that is, large quantities in the nucleus compared with small quantities in the cytoplasm — determines the directionality of many nuclear transport processes. Recent findings that Ran also functions in spindle formation and nuclear envelope assembly during mitosis suggest that Ran has a general role in chromatin-centred processes. Ran functions in these events as a signal for chromosome position."}],"issue":"7","volume":4,"language":[{"iso":"eng"}],"publication_status":"published","publication_identifier":{"issn":["1465-7392"],"eissn":["1476-4679"]}},{"date_updated":"2022-07-18T08:58:07Z","extern":"1","article_type":"original","type":"journal_article","status":"public","keyword":["Cell Biology"],"_id":"11125","volume":3,"issue":"12","publication_identifier":{"eissn":["1476-4679"],"issn":["1465-7392"]},"publication_status":"published","language":[{"iso":"eng"}],"scopus_import":"1","month":"11","intvolume":" 3","abstract":[{"lang":"eng","text":"Although nuclear envelope (NE) assembly is known to require the GTPase Ran, the membrane fusion machinery involved is uncharacterized. NE assembly involves formation of a reticular network on chromatin, fusion of this network into a closed NE and subsequent expansion. Here we show that p97, an AAA-ATPase previously implicated in fusion of Golgi and transitional endoplasmic reticulum (ER) membranes together with the adaptor p47, has two discrete functions in NE assembly. Formation of a closed NE requires the p97–Ufd1–Npl4 complex, not previously implicated in membrane fusion. Subsequent NE growth involves a p97–p47 complex. This study provides the first insights into the molecular mechanisms and specificity of fusion events involved in NE formation."}],"pmid":1,"oa_version":"None","author":[{"first_name":"Martin W","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","full_name":"HETZER, Martin W","orcid":"0000-0002-2111-992X","last_name":"HETZER"},{"last_name":"Meyer","full_name":"Meyer, Hemmo H.","first_name":"Hemmo H."},{"first_name":"Tobias C.","full_name":"Walther, Tobias C.","last_name":"Walther"},{"full_name":"Bilbao-Cortes, Daniel","last_name":"Bilbao-Cortes","first_name":"Daniel"},{"last_name":"Warren","full_name":"Warren, Graham","first_name":"Graham"},{"full_name":"Mattaj, Iain W.","last_name":"Mattaj","first_name":"Iain W."}],"article_processing_charge":"No","external_id":{"pmid":["11781570"]},"title":"Distinct AAA-ATPase p97 complexes function in discrete steps of nuclear assembly","citation":{"short":"M. Hetzer, H.H. Meyer, T.C. Walther, D. Bilbao-Cortes, G. Warren, I.W. Mattaj, Nature Cell Biology 3 (2001) 1086–1091.","ieee":"M. Hetzer, H. H. Meyer, T. C. Walther, D. Bilbao-Cortes, G. Warren, and I. W. Mattaj, “Distinct AAA-ATPase p97 complexes function in discrete steps of nuclear assembly,” Nature Cell Biology, vol. 3, no. 12. Springer Nature, pp. 1086–1091, 2001.","ama":"Hetzer M, Meyer HH, Walther TC, Bilbao-Cortes D, Warren G, Mattaj IW. Distinct AAA-ATPase p97 complexes function in discrete steps of nuclear assembly. Nature Cell Biology. 2001;3(12):1086-1091. doi:10.1038/ncb1201-1086","apa":"Hetzer, M., Meyer, H. H., Walther, T. C., Bilbao-Cortes, D., Warren, G., & Mattaj, I. W. (2001). Distinct AAA-ATPase p97 complexes function in discrete steps of nuclear assembly. Nature Cell Biology. Springer Nature. https://doi.org/10.1038/ncb1201-1086","mla":"Hetzer, Martin, et al. “Distinct AAA-ATPase P97 Complexes Function in Discrete Steps of Nuclear Assembly.” Nature Cell Biology, vol. 3, no. 12, Springer Nature, 2001, pp. 1086–91, doi:10.1038/ncb1201-1086.","ista":"Hetzer M, Meyer HH, Walther TC, Bilbao-Cortes D, Warren G, Mattaj IW. 2001. Distinct AAA-ATPase p97 complexes function in discrete steps of nuclear assembly. Nature Cell Biology. 3(12), 1086–1091.","chicago":"Hetzer, Martin, Hemmo H. Meyer, Tobias C. Walther, Daniel Bilbao-Cortes, Graham Warren, and Iain W. Mattaj. “Distinct AAA-ATPase P97 Complexes Function in Discrete Steps of Nuclear Assembly.” Nature Cell Biology. Springer Nature, 2001. https://doi.org/10.1038/ncb1201-1086."},"user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","page":"1086-1091","date_published":"2001-11-02T00:00:00Z","doi":"10.1038/ncb1201-1086","date_created":"2022-04-07T07:57:42Z","year":"2001","day":"02","publication":"Nature Cell Biology","publisher":"Springer Nature","quality_controlled":"1"},{"publication_status":"published","publication_identifier":{"eissn":["1540-8140"],"issn":["0021-9525"]},"language":[{"iso":"eng"}],"issue":"2","volume":148,"abstract":[{"lang":"eng","text":"Nuclear import of the two uracil-rich small nuclear ribonucleoprotein (U snRNP) components U1A and U2B′′ is mediated by unusually long and complex nuclear localization signals (NLSs). Here we investigate nuclear import of U1A and U2B′′ in vitro and demonstrate that it occurs by an active, saturable process. Several lines of evidence suggest that import of the two proteins occurs by an import mechanism different to those characterized previously. No cross competition is seen with a variety of previously studied NLSs. In contrast to import mediated by members of the importin-β family of nucleocytoplasmic transport receptors, U1A/U2B′′ import is not inhibited by either nonhydrolyzable guanosine triphosphate (GTP) analogues or by a mutant of the GTPase Ran that is incapable of GTP hydrolysis. Adenosine triphosphate is capable of supporting U1A and U2B′′ import, whereas neither nonhydrolyzable adenosine triphosphate analogues nor GTP can do so. U1A and U2B′′ import in vitro does not require the addition of soluble cytosolic proteins, but a factor or factors required for U1A and U2B′′ import remains tightly associated with the nuclear fraction of conventionally permeabilized cells. This activity can be solubilized in the presence of elevated MgCl2. These data suggest that U1A and U2B′′ import into the nucleus occurs by a hitherto uncharacterized mechanism."}],"pmid":1,"oa_version":"None","scopus_import":"1","intvolume":" 148","month":"01","date_updated":"2022-07-18T08:58:29Z","extern":"1","_id":"11126","type":"journal_article","article_type":"original","keyword":["Cell Biology"],"status":"public","year":"2000","publication":"Journal of Cell Biology","day":"24","page":"293-304","date_created":"2022-04-07T07:57:49Z","date_published":"2000-01-24T00:00:00Z","doi":"10.1083/jcb.148.2.293","quality_controlled":"1","publisher":"Rockefeller University Press","citation":{"chicago":"Hetzer, Martin, and Iain W. Mattaj. “An Atp-Dependent, Ran-Independent Mechanism for Nuclear Import of the U1a and U2b′′ Spliceosome Proteins.” Journal of Cell Biology. Rockefeller University Press, 2000. https://doi.org/10.1083/jcb.148.2.293.","ista":"Hetzer M, Mattaj IW. 2000. An Atp-dependent, Ran-independent mechanism for nuclear import of the U1a and U2b′′ spliceosome proteins. Journal of Cell Biology. 148(2), 293–304.","mla":"Hetzer, Martin, and Iain W. Mattaj. “An Atp-Dependent, Ran-Independent Mechanism for Nuclear Import of the U1a and U2b′′ Spliceosome Proteins.” Journal of Cell Biology, vol. 148, no. 2, Rockefeller University Press, 2000, pp. 293–304, doi:10.1083/jcb.148.2.293.","ieee":"M. Hetzer and I. W. Mattaj, “An Atp-dependent, Ran-independent mechanism for nuclear import of the U1a and U2b′′ spliceosome proteins,” Journal of Cell Biology, vol. 148, no. 2. Rockefeller University Press, pp. 293–304, 2000.","short":"M. Hetzer, I.W. Mattaj, Journal of Cell Biology 148 (2000) 293–304.","apa":"Hetzer, M., & Mattaj, I. W. (2000). An Atp-dependent, Ran-independent mechanism for nuclear import of the U1a and U2b′′ spliceosome proteins. Journal of Cell Biology. Rockefeller University Press. https://doi.org/10.1083/jcb.148.2.293","ama":"Hetzer M, Mattaj IW. An Atp-dependent, Ran-independent mechanism for nuclear import of the U1a and U2b′′ spliceosome proteins. Journal of Cell Biology. 2000;148(2):293-304. doi:10.1083/jcb.148.2.293"},"user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","article_processing_charge":"No","external_id":{"pmid":["10648562"]},"author":[{"first_name":"Martin W","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","orcid":"0000-0002-2111-992X","full_name":"HETZER, Martin W","last_name":"HETZER"},{"full_name":"Mattaj, Iain W.","last_name":"Mattaj","first_name":"Iain W."}],"title":"An Atp-dependent, Ran-independent mechanism for nuclear import of the U1a and U2b′′ spliceosome proteins"},{"year":"2000","day":"01","publication":"Molecular Cell","page":"1013-1024","date_published":"2000-06-01T00:00:00Z","doi":"10.1016/s1097-2765(00)80266-x","date_created":"2022-04-07T07:57:59Z","publisher":"Elsevier","quality_controlled":"1","oa":1,"citation":{"mla":"Hetzer, Martin, et al. “GTP Hydrolysis by Ran Is Required for Nuclear Envelope Assembly.” Molecular Cell, vol. 5, no. 6, Elsevier, 2000, pp. 1013–24, doi:10.1016/s1097-2765(00)80266-x.","short":"M. Hetzer, D. Bilbao-Cortés, T.C. Walther, O.J. Gruss, I.W. Mattaj, Molecular Cell 5 (2000) 1013–1024.","ieee":"M. Hetzer, D. Bilbao-Cortés, T. C. Walther, O. J. Gruss, and I. W. Mattaj, “GTP hydrolysis by Ran is required for nuclear envelope assembly,” Molecular Cell, vol. 5, no. 6. Elsevier, pp. 1013–1024, 2000.","apa":"Hetzer, M., Bilbao-Cortés, D., Walther, T. C., Gruss, O. J., & Mattaj, I. W. (2000). GTP hydrolysis by Ran is required for nuclear envelope assembly. Molecular Cell. Elsevier. https://doi.org/10.1016/s1097-2765(00)80266-x","ama":"Hetzer M, Bilbao-Cortés D, Walther TC, Gruss OJ, Mattaj IW. GTP hydrolysis by Ran is required for nuclear envelope assembly. Molecular Cell. 2000;5(6):1013-1024. doi:10.1016/s1097-2765(00)80266-x","chicago":"Hetzer, Martin, Daniel Bilbao-Cortés, Tobias C Walther, Oliver J Gruss, and Iain W Mattaj. “GTP Hydrolysis by Ran Is Required for Nuclear Envelope Assembly.” Molecular Cell. Elsevier, 2000. https://doi.org/10.1016/s1097-2765(00)80266-x.","ista":"Hetzer M, Bilbao-Cortés D, Walther TC, Gruss OJ, Mattaj IW. 2000. GTP hydrolysis by Ran is required for nuclear envelope assembly. Molecular Cell. 5(6), 1013–1024."},"user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","author":[{"id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","first_name":"Martin W","last_name":"HETZER","orcid":"0000-0002-2111-992X","full_name":"HETZER, Martin W"},{"first_name":"Daniel","last_name":"Bilbao-Cortés","full_name":"Bilbao-Cortés, Daniel"},{"full_name":"Walther, Tobias C","last_name":"Walther","first_name":"Tobias C"},{"first_name":"Oliver J","last_name":"Gruss","full_name":"Gruss, Oliver J"},{"first_name":"Iain W","last_name":"Mattaj","full_name":"Mattaj, Iain W"}],"external_id":{"pmid":["10911995"]},"article_processing_charge":"No","title":"GTP hydrolysis by Ran is required for nuclear envelope assembly","publication_identifier":{"issn":["1097-2765"]},"publication_status":"published","language":[{"iso":"eng"}],"volume":5,"issue":"6","abstract":[{"text":"Nuclear formation in Xenopus egg extracts requires cytosol and is inhibited by GTPγS, indicating a requirement for GTPase activity. Nuclear envelope (NE) vesicle fusion is extensively inhibited by GTPγS and two mutant forms of the Ran GTPase, Q69L and T24N. Depletion of either Ran or RCC1, the exchange factor for Ran, from the assembly reaction also inhibits this step of NE formation. Ran depletion can be complemented by the addition of Ran loaded with either GTP or GDP but not with GTPγS. RCC1 depletion is only complemented by RCC1 itself or by RanGTP. Thus, generation of RanGTP by RCC1 and GTP hydrolysis by Ran are both required for the extensive membrane fusion events that lead to NE formation.","lang":"eng"}],"oa_version":"Published Version","pmid":1,"scopus_import":"1","main_file_link":[{"open_access":"1","url":"https://doi.org/10.1016/S1097-2765(00)80266-X"}],"month":"06","intvolume":" 5","date_updated":"2022-07-18T08:58:31Z","extern":"1","_id":"11127","type":"journal_article","article_type":"original","status":"public","keyword":["Cell Biology","Molecular Biology"]}]