[{"publication":"Journal of Cell Biology","intvolume":"       205","external_id":{"pmid":["24751535"]},"doi":"10.1083/jcb.201402003","date_updated":"2024-10-14T11:23:23Z","title":"Breaching the nuclear envelope in development and disease","citation":{"ama":"Hatch E, Hetzer M. Breaching the nuclear envelope in development and disease. <i>Journal of Cell Biology</i>. 2014;205(2):133-141. doi:<a href=\"https://doi.org/10.1083/jcb.201402003\">10.1083/jcb.201402003</a>","mla":"Hatch, Emily, and Martin Hetzer. “Breaching the Nuclear Envelope in Development and Disease.” <i>Journal of Cell Biology</i>, vol. 205, no. 2, Rockefeller University Press, 2014, pp. 133–41, doi:<a href=\"https://doi.org/10.1083/jcb.201402003\">10.1083/jcb.201402003</a>.","apa":"Hatch, E., &#38; Hetzer, M. (2014). Breaching the nuclear envelope in development and disease. <i>Journal of Cell Biology</i>. Rockefeller University Press. <a href=\"https://doi.org/10.1083/jcb.201402003\">https://doi.org/10.1083/jcb.201402003</a>","short":"E. Hatch, M. Hetzer, Journal of Cell Biology 205 (2014) 133–141.","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.” <i>Journal of Cell Biology</i>. Rockefeller University Press, 2014. <a href=\"https://doi.org/10.1083/jcb.201402003\">https://doi.org/10.1083/jcb.201402003</a>.","ieee":"E. Hatch and M. Hetzer, “Breaching the nuclear envelope in development and disease,” <i>Journal of Cell Biology</i>, vol. 205, no. 2. Rockefeller University Press, pp. 133–141, 2014."},"language":[{"iso":"eng"}],"day":"21","article_type":"review","pmid":1,"scopus_import":"1","date_created":"2022-04-07T07:50:13Z","status":"public","volume":205,"publisher":"Rockefeller University Press","extern":"1","oa":1,"keyword":["Cell Biology"],"year":"2014","issue":"2","abstract":[{"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.","lang":"eng"}],"page":"133-141","author":[{"first_name":"Emily","last_name":"Hatch","full_name":"Hatch, Emily"},{"id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","last_name":"HETZER","first_name":"Martin W","orcid":"0000-0002-2111-992X","full_name":"HETZER, Martin W"}],"article_processing_charge":"No","main_file_link":[{"open_access":"1","url":"https://doi.org/10.1083/jcb.201402003"}],"publication_identifier":{"issn":["1540-8140","0021-9525"]},"_id":"11081","date_published":"2014-04-21T00:00:00Z","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","oa_version":"Published Version","publication_status":"published","month":"04","quality_controlled":"1","type":"journal_article"},{"citation":{"ieee":"A. L. Buchwalter, Y. Liang, and M. Hetzer, “Nup50 is required for cell differentiation and exhibits transcription-dependent dynamics,” <i>Molecular Biology of the Cell</i>, vol. 25, no. 16. American Society for Cell Biology, pp. 2472–2484, 2014.","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.","short":"A.L. Buchwalter, Y. Liang, M. Hetzer, Molecular Biology of the Cell 25 (2014) 2472–2484.","chicago":"Buchwalter, Abigail L., Yun Liang, and Martin Hetzer. “Nup50 Is Required for Cell Differentiation and Exhibits Transcription-Dependent Dynamics.” <i>Molecular Biology of the Cell</i>. American Society for Cell Biology, 2014. <a href=\"https://doi.org/10.1091/mbc.e14-04-0865\">https://doi.org/10.1091/mbc.e14-04-0865</a>.","apa":"Buchwalter, A. L., Liang, Y., &#38; Hetzer, M. (2014). Nup50 is required for cell differentiation and exhibits transcription-dependent dynamics. <i>Molecular Biology of the Cell</i>. American Society for Cell Biology. <a href=\"https://doi.org/10.1091/mbc.e14-04-0865\">https://doi.org/10.1091/mbc.e14-04-0865</a>","mla":"Buchwalter, Abigail L., et al. “Nup50 Is Required for Cell Differentiation and Exhibits Transcription-Dependent Dynamics.” <i>Molecular Biology of the Cell</i>, vol. 25, no. 16, American Society for Cell Biology, 2014, pp. 2472–84, doi:<a href=\"https://doi.org/10.1091/mbc.e14-04-0865\">10.1091/mbc.e14-04-0865</a>.","ama":"Buchwalter AL, Liang Y, Hetzer M. Nup50 is required for cell differentiation and exhibits transcription-dependent dynamics. <i>Molecular Biology of the Cell</i>. 2014;25(16):2472-2484. doi:<a href=\"https://doi.org/10.1091/mbc.e14-04-0865\">10.1091/mbc.e14-04-0865</a>"},"doi":"10.1091/mbc.e14-04-0865","date_updated":"2024-10-14T11:23:34Z","title":"Nup50 is required for cell differentiation and exhibits transcription-dependent dynamics","publication":"Molecular Biology of the Cell","intvolume":"        25","volume":25,"publisher":"American Society for Cell Biology","extern":"1","date_created":"2022-04-07T07:50:24Z","status":"public","scopus_import":"1","language":[{"iso":"eng"}],"day":"15","article_type":"original","publication_identifier":{"issn":["1059-1524","1939-4586"]},"article_processing_charge":"No","main_file_link":[{"open_access":"1","url":"https://doi.org/10.1091/mbc.e14-04-0865"}],"issue":"16","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"}],"page":"2472-2484","author":[{"full_name":"Buchwalter, Abigail L.","last_name":"Buchwalter","first_name":"Abigail L."},{"full_name":"Liang, Yun","first_name":"Yun","last_name":"Liang"},{"last_name":"HETZER","first_name":"Martin W","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","full_name":"HETZER, Martin W","orcid":"0000-0002-2111-992X"}],"oa":1,"keyword":["Cell Biology","Molecular Biology"],"year":"2014","quality_controlled":"1","type":"journal_article","oa_version":"Published Version","month":"08","publication_status":"published","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","_id":"11082","date_published":"2014-08-15T00:00:00Z"},{"year":"2013","keyword":["Cell Biology"],"abstract":[{"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.","lang":"eng"}],"issue":"3","author":[{"last_name":"Franks","first_name":"Tobias M.","full_name":"Franks, Tobias M."},{"first_name":"Martin W","last_name":"HETZER","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","full_name":"HETZER, Martin W","orcid":"0000-0002-2111-992X"}],"page":"112-117","article_processing_charge":"No","publication_identifier":{"issn":["0962-8924"]},"date_published":"2013-03-01T00:00:00Z","_id":"11083","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","month":"03","publication_status":"published","oa_version":"None","quality_controlled":"1","type":"journal_article","publication":"Trends in Cell Biology","external_id":{"pmid":["23246429"]},"intvolume":"        23","date_updated":"2024-10-14T11:23:44Z","title":"The role of Nup98 in transcription regulation in healthy and diseased cells","doi":"10.1016/j.tcb.2012.10.013","citation":{"ama":"Franks TM, Hetzer M. The role of Nup98 in transcription regulation in healthy and diseased cells. <i>Trends in Cell Biology</i>. 2013;23(3):112-117. doi:<a href=\"https://doi.org/10.1016/j.tcb.2012.10.013\">10.1016/j.tcb.2012.10.013</a>","mla":"Franks, Tobias M., and Martin Hetzer. “The Role of Nup98 in Transcription Regulation in Healthy and Diseased Cells.” <i>Trends in Cell Biology</i>, vol. 23, no. 3, Elsevier, 2013, pp. 112–17, doi:<a href=\"https://doi.org/10.1016/j.tcb.2012.10.013\">10.1016/j.tcb.2012.10.013</a>.","apa":"Franks, T. M., &#38; Hetzer, M. (2013). The role of Nup98 in transcription regulation in healthy and diseased cells. <i>Trends in Cell Biology</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.tcb.2012.10.013\">https://doi.org/10.1016/j.tcb.2012.10.013</a>","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.","short":"T.M. Franks, M. Hetzer, Trends in Cell Biology 23 (2013) 112–117.","chicago":"Franks, Tobias M., and Martin Hetzer. “The Role of Nup98 in Transcription Regulation in Healthy and Diseased Cells.” <i>Trends in Cell Biology</i>. Elsevier, 2013. <a href=\"https://doi.org/10.1016/j.tcb.2012.10.013\">https://doi.org/10.1016/j.tcb.2012.10.013</a>.","ieee":"T. M. Franks and M. Hetzer, “The role of Nup98 in transcription regulation in healthy and diseased cells,” <i>Trends in Cell Biology</i>, vol. 23, no. 3. Elsevier, pp. 112–117, 2013."},"day":"01","language":[{"iso":"eng"}],"article_type":"letter_note","pmid":1,"scopus_import":"1","date_created":"2022-04-07T07:50:33Z","status":"public","volume":23,"publisher":"Elsevier","extern":"1"},{"publisher":"Springer Nature","extern":"1","volume":14,"status":"public","date_created":"2022-04-07T07:50:43Z","scopus_import":"1","pmid":1,"article_type":"original","language":[{"iso":"eng"}],"day":"01","citation":{"apa":"Toyama, B. H., &#38; Hetzer, M. (2013). Protein homeostasis: Live long, won’t prosper. <i>Nature Reviews Molecular Cell Biology</i>. Springer Nature. <a href=\"https://doi.org/10.1038/nrm3496\">https://doi.org/10.1038/nrm3496</a>","mla":"Toyama, Brandon H., and Martin Hetzer. “Protein Homeostasis: Live Long, Won’t Prosper.” <i>Nature Reviews Molecular Cell Biology</i>, vol. 14, Springer Nature, 2013, pp. 55–61, doi:<a href=\"https://doi.org/10.1038/nrm3496\">10.1038/nrm3496</a>.","ama":"Toyama BH, Hetzer M. Protein homeostasis: Live long, won’t prosper. <i>Nature Reviews Molecular Cell Biology</i>. 2013;14:55-61. doi:<a href=\"https://doi.org/10.1038/nrm3496\">10.1038/nrm3496</a>","ieee":"B. H. Toyama and M. Hetzer, “Protein homeostasis: Live long, won’t prosper,” <i>Nature Reviews Molecular Cell Biology</i>, vol. 14. Springer Nature, pp. 55–61, 2013.","chicago":"Toyama, Brandon H., and Martin Hetzer. “Protein Homeostasis: Live Long, Won’t Prosper.” <i>Nature Reviews Molecular Cell Biology</i>. Springer Nature, 2013. <a href=\"https://doi.org/10.1038/nrm3496\">https://doi.org/10.1038/nrm3496</a>.","short":"B.H. Toyama, M. Hetzer, Nature Reviews Molecular Cell Biology 14 (2013) 55–61.","ista":"Toyama BH, Hetzer M. 2013. Protein homeostasis: Live long, won’t prosper. Nature Reviews Molecular Cell Biology. 14, 55–61."},"date_updated":"2024-10-14T11:24:09Z","title":"Protein homeostasis: Live long, won't prosper","doi":"10.1038/nrm3496","external_id":{"pmid":["23258296"]},"intvolume":"        14","publication":"Nature Reviews Molecular Cell Biology","type":"journal_article","quality_controlled":"1","month":"01","publication_status":"published","oa_version":"None","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","date_published":"2013-01-01T00:00:00Z","_id":"11084","publication_identifier":{"issn":["1471-0072","1471-0080"]},"article_processing_charge":"No","author":[{"first_name":"Brandon H.","last_name":"Toyama","full_name":"Toyama, Brandon H."},{"full_name":"HETZER, Martin W","orcid":"0000-0002-2111-992X","first_name":"Martin W","last_name":"HETZER","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed"}],"page":"55-61","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"}],"year":"2013","keyword":["Cell Biology","Molecular Biology"]},{"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","date_published":"2012-12-01T00:00:00Z","_id":"11089","quality_controlled":"1","type":"journal_article","publication_status":"published","month":"12","oa_version":"None","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."}],"issue":"6","author":[{"first_name":"J Sebastian","last_name":"Gomez-Cavazos","full_name":"Gomez-Cavazos, J Sebastian"},{"first_name":"Martin W","last_name":"HETZER","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","full_name":"HETZER, Martin W","orcid":"0000-0002-2111-992X"}],"page":"775-783","year":"2012","keyword":["Cell Biology"],"publication_identifier":{"issn":["0955-0674"]},"article_processing_charge":"No","pmid":1,"scopus_import":"1","language":[{"iso":"eng"}],"day":"01","article_type":"original","volume":24,"publisher":"Elsevier","extern":"1","date_created":"2022-04-07T07:51:37Z","status":"public","date_updated":"2024-10-14T11:25:04Z","title":"Outfits for different occasions: tissue-specific roles of Nuclear Envelope proteins","doi":"10.1016/j.ceb.2012.08.008","publication":"Current Opinion in Cell Biology","external_id":{"pmid":["22995343"]},"intvolume":"        24","citation":{"ieee":"J. S. Gomez-Cavazos and M. Hetzer, “Outfits for different occasions: tissue-specific roles of Nuclear Envelope proteins,” <i>Current Opinion in Cell Biology</i>, vol. 24, no. 6. Elsevier, pp. 775–783, 2012.","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.","short":"J.S. Gomez-Cavazos, M. Hetzer, Current Opinion in Cell Biology 24 (2012) 775–783.","chicago":"Gomez-Cavazos, J Sebastian, and Martin Hetzer. “Outfits for Different Occasions: Tissue-Specific Roles of Nuclear Envelope Proteins.” <i>Current Opinion in Cell Biology</i>. Elsevier, 2012. <a href=\"https://doi.org/10.1016/j.ceb.2012.08.008\">https://doi.org/10.1016/j.ceb.2012.08.008</a>.","mla":"Gomez-Cavazos, J. Sebastian, and Martin Hetzer. “Outfits for Different Occasions: Tissue-Specific Roles of Nuclear Envelope Proteins.” <i>Current Opinion in Cell Biology</i>, vol. 24, no. 6, Elsevier, 2012, pp. 775–83, doi:<a href=\"https://doi.org/10.1016/j.ceb.2012.08.008\">10.1016/j.ceb.2012.08.008</a>.","ama":"Gomez-Cavazos JS, Hetzer M. Outfits for different occasions: tissue-specific roles of Nuclear Envelope proteins. <i>Current Opinion in Cell Biology</i>. 2012;24(6):775-783. doi:<a href=\"https://doi.org/10.1016/j.ceb.2012.08.008\">10.1016/j.ceb.2012.08.008</a>","apa":"Gomez-Cavazos, J. S., &#38; Hetzer, M. (2012). Outfits for different occasions: tissue-specific roles of Nuclear Envelope proteins. <i>Current Opinion in Cell Biology</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.ceb.2012.08.008\">https://doi.org/10.1016/j.ceb.2012.08.008</a>"}},{"page":"88-100","author":[{"full_name":"Vargas, Jesse D.","last_name":"Vargas","first_name":"Jesse D."},{"last_name":"Hatch","first_name":"Emily M.","full_name":"Hatch, Emily M."},{"full_name":"Anderson, Daniel J.","first_name":"Daniel J.","last_name":"Anderson"},{"last_name":"HETZER","first_name":"Martin W","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","orcid":"0000-0002-2111-992X","full_name":"HETZER, Martin W"}],"issue":"1","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"}],"year":"2012","keyword":["Cell Biology"],"publication_identifier":{"issn":["1949-1034"],"eissn":["1949-1042"]},"article_processing_charge":"No","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","date_published":"2012-01-01T00:00:00Z","_id":"11091","type":"journal_article","quality_controlled":"1","month":"01","publication_status":"published","oa_version":"None","date_updated":"2024-10-14T11:25:37Z","title":"Transient nuclear envelope rupturing during interphase in human cancer cells","doi":"10.4161/nucl.18954","external_id":{"pmid":["22567193"]},"intvolume":"         3","publication":"Nucleus","citation":{"ieee":"J. D. Vargas, E. M. Hatch, D. J. Anderson, and M. Hetzer, “Transient nuclear envelope rupturing during interphase in human cancer cells,” <i>Nucleus</i>, vol. 3, no. 1. Taylor &#38; Francis, pp. 88–100, 2012.","short":"J.D. Vargas, E.M. Hatch, D.J. Anderson, M. Hetzer, Nucleus 3 (2012) 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.” <i>Nucleus</i>. Taylor &#38; Francis, 2012. <a href=\"https://doi.org/10.4161/nucl.18954\">https://doi.org/10.4161/nucl.18954</a>.","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.","mla":"Vargas, Jesse D., et al. “Transient Nuclear Envelope Rupturing during Interphase in Human Cancer Cells.” <i>Nucleus</i>, vol. 3, no. 1, Taylor &#38; Francis, 2012, pp. 88–100, doi:<a href=\"https://doi.org/10.4161/nucl.18954\">10.4161/nucl.18954</a>.","ama":"Vargas JD, Hatch EM, Anderson DJ, Hetzer M. Transient nuclear envelope rupturing during interphase in human cancer cells. <i>Nucleus</i>. 2012;3(1):88-100. doi:<a href=\"https://doi.org/10.4161/nucl.18954\">10.4161/nucl.18954</a>","apa":"Vargas, J. D., Hatch, E. M., Anderson, D. J., &#38; Hetzer, M. (2012). Transient nuclear envelope rupturing during interphase in human cancer cells. <i>Nucleus</i>. Taylor &#38; Francis. <a href=\"https://doi.org/10.4161/nucl.18954\">https://doi.org/10.4161/nucl.18954</a>"},"scopus_import":"1","pmid":1,"article_type":"original","language":[{"iso":"eng"}],"day":"01","publisher":"Taylor & Francis","extern":"1","volume":3,"status":"public","date_created":"2022-04-07T07:51:53Z"},{"oa":1,"year":"2012","keyword":["Developmental Biology","Cell Biology","General Biochemistry","Genetics and Molecular Biology","Molecular Biology"],"issue":"2","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."}],"author":[{"first_name":"Maximiliano A.","last_name":"D'Angelo","full_name":"D'Angelo, Maximiliano A."},{"full_name":"Gomez-Cavazos, J. Sebastian","first_name":"J. Sebastian","last_name":"Gomez-Cavazos"},{"first_name":"Arianna","last_name":"Mei","full_name":"Mei, Arianna"},{"full_name":"Lackner, Daniel H.","last_name":"Lackner","first_name":"Daniel H."},{"full_name":"HETZER, Martin W","orcid":"0000-0002-2111-992X","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","last_name":"HETZER","first_name":"Martin W"}],"page":"446-458","article_processing_charge":"No","main_file_link":[{"open_access":"1","url":"https://doi.org/10.1016/j.devcel.2011.11.021"}],"publication_identifier":{"issn":["1534-5807"]},"date_published":"2012-01-19T00:00:00Z","_id":"11093","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","publication_status":"published","month":"01","oa_version":"Published Version","quality_controlled":"1","type":"journal_article","publication":"Developmental Cell","external_id":{"pmid":["22264802"]},"intvolume":"        22","date_updated":"2024-10-14T11:26:00Z","title":"A change in nuclear pore complex composition regulates cell differentiation","doi":"10.1016/j.devcel.2011.11.021","citation":{"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,” <i>Developmental Cell</i>, vol. 22, no. 2. Elsevier, pp. 446–458, 2012.","short":"M.A. D’Angelo, J.S. Gomez-Cavazos, A. Mei, D.H. Lackner, M. Hetzer, Developmental Cell 22 (2012) 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.” <i>Developmental Cell</i>. Elsevier, 2012. <a href=\"https://doi.org/10.1016/j.devcel.2011.11.021\">https://doi.org/10.1016/j.devcel.2011.11.021</a>.","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.","mla":"D’Angelo, Maximiliano A., et al. “A Change in Nuclear Pore Complex Composition Regulates Cell Differentiation.” <i>Developmental Cell</i>, vol. 22, no. 2, Elsevier, 2012, pp. 446–58, doi:<a href=\"https://doi.org/10.1016/j.devcel.2011.11.021\">10.1016/j.devcel.2011.11.021</a>.","ama":"D’Angelo MA, Gomez-Cavazos JS, Mei A, Lackner DH, Hetzer M. A change in nuclear pore complex composition regulates cell differentiation. <i>Developmental Cell</i>. 2012;22(2):446-458. doi:<a href=\"https://doi.org/10.1016/j.devcel.2011.11.021\">10.1016/j.devcel.2011.11.021</a>","apa":"D’Angelo, M. A., Gomez-Cavazos, J. S., Mei, A., Lackner, D. H., &#38; Hetzer, M. (2012). A change in nuclear pore complex composition regulates cell differentiation. <i>Developmental Cell</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.devcel.2011.11.021\">https://doi.org/10.1016/j.devcel.2011.11.021</a>"},"day":"19","language":[{"iso":"eng"}],"article_type":"original","pmid":1,"scopus_import":"1","date_created":"2022-04-07T07:52:10Z","status":"public","volume":22,"extern":"1","publisher":"Elsevier"},{"_id":"11094","date_published":"2011-07-04T00:00:00Z","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","oa_version":"Published Version","publication_status":"published","month":"07","quality_controlled":"1","type":"journal_article","oa":1,"keyword":["Cell Biology"],"year":"2011","issue":"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."}],"author":[{"full_name":"Talamas, Jessica A.","first_name":"Jessica A.","last_name":"Talamas"},{"orcid":"0000-0002-2111-992X","full_name":"HETZER, Martin W","last_name":"HETZER","first_name":"Martin W","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed"}],"page":"27-37","article_processing_charge":"No","main_file_link":[{"url":"https://doi.org/10.1083/jcb.201012154","open_access":"1"}],"publication_identifier":{"issn":["0021-9525"],"eissn":["1540-8140"]},"language":[{"iso":"eng"}],"day":"04","article_type":"original","pmid":1,"scopus_import":"1","date_created":"2022-04-07T07:52:18Z","status":"public","volume":194,"extern":"1","publisher":"Rockefeller University Press","publication":"Journal of Cell Biology","intvolume":"       194","external_id":{"pmid":["21727197"]},"doi":"10.1083/jcb.201012154","title":"POM121 and Sun1 play a role in early steps of interphase NPC assembly","date_updated":"2024-10-14T11:26:10Z","citation":{"ama":"Talamas JA, Hetzer M. POM121 and Sun1 play a role in early steps of interphase NPC assembly. <i>Journal of Cell Biology</i>. 2011;194(1):27-37. doi:<a href=\"https://doi.org/10.1083/jcb.201012154\">10.1083/jcb.201012154</a>","mla":"Talamas, Jessica A., and Martin Hetzer. “POM121 and Sun1 Play a Role in Early Steps of Interphase NPC Assembly.” <i>Journal of Cell Biology</i>, vol. 194, no. 1, Rockefeller University Press, 2011, pp. 27–37, doi:<a href=\"https://doi.org/10.1083/jcb.201012154\">10.1083/jcb.201012154</a>.","apa":"Talamas, J. A., &#38; Hetzer, M. (2011). POM121 and Sun1 play a role in early steps of interphase NPC assembly. <i>Journal of Cell Biology</i>. Rockefeller University Press. <a href=\"https://doi.org/10.1083/jcb.201012154\">https://doi.org/10.1083/jcb.201012154</a>","chicago":"Talamas, Jessica A., and Martin Hetzer. “POM121 and Sun1 Play a Role in Early Steps of Interphase NPC Assembly.” <i>Journal of Cell Biology</i>. Rockefeller University Press, 2011. <a href=\"https://doi.org/10.1083/jcb.201012154\">https://doi.org/10.1083/jcb.201012154</a>.","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.","short":"J.A. Talamas, M. Hetzer, Journal of Cell Biology 194 (2011) 27–37.","ieee":"J. A. Talamas and M. Hetzer, “POM121 and Sun1 play a role in early steps of interphase NPC assembly,” <i>Journal of Cell Biology</i>, vol. 194, no. 1. Rockefeller University Press, pp. 27–37, 2011."}},{"publication":"Current Opinion in Cell Biology","external_id":{"pmid":["21592757"]},"intvolume":"        23","title":"Editorial overview","date_updated":"2024-10-14T11:26:20Z","doi":"10.1016/j.ceb.2011.04.013","citation":{"mla":"Hetzer, Martin, and Giacomo Cavalli. “Editorial Overview.” <i>Current Opinion in Cell Biology</i>, vol. 23, no. 3, Elsevier, 2011, pp. 255–57, doi:<a href=\"https://doi.org/10.1016/j.ceb.2011.04.013\">10.1016/j.ceb.2011.04.013</a>.","ama":"Hetzer M, Cavalli G. Editorial overview. <i>Current Opinion in Cell Biology</i>. 2011;23(3):255-257. doi:<a href=\"https://doi.org/10.1016/j.ceb.2011.04.013\">10.1016/j.ceb.2011.04.013</a>","apa":"Hetzer, M., &#38; Cavalli, G. (2011). Editorial overview. <i>Current Opinion in Cell Biology</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.ceb.2011.04.013\">https://doi.org/10.1016/j.ceb.2011.04.013</a>","ieee":"M. Hetzer and G. Cavalli, “Editorial overview,” <i>Current Opinion in Cell Biology</i>, vol. 23, no. 3. Elsevier, pp. 255–257, 2011.","ista":"Hetzer M, Cavalli G. 2011. Editorial overview. Current Opinion in Cell Biology. 23(3), 255–257.","chicago":"Hetzer, Martin, and Giacomo Cavalli. “Editorial Overview.” <i>Current Opinion in Cell Biology</i>. Elsevier, 2011. <a href=\"https://doi.org/10.1016/j.ceb.2011.04.013\">https://doi.org/10.1016/j.ceb.2011.04.013</a>.","short":"M. Hetzer, G. Cavalli, Current Opinion in Cell Biology 23 (2011) 255–257."},"language":[{"iso":"eng"}],"day":"01","article_type":"letter_note","pmid":1,"scopus_import":"1","date_created":"2022-04-07T07:52:27Z","status":"public","volume":23,"publisher":"Elsevier","extern":"1","year":"2011","keyword":["Cell Biology"],"issue":"3","author":[{"id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","last_name":"HETZER","first_name":"Martin W","orcid":"0000-0002-2111-992X","full_name":"HETZER, Martin W"},{"full_name":"Cavalli, Giacomo","first_name":"Giacomo","last_name":"Cavalli"}],"page":"255-257","article_processing_charge":"No","publication_identifier":{"issn":["0955-0674"]},"date_published":"2011-06-01T00:00:00Z","_id":"11095","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","publication_status":"published","month":"06","oa_version":"None","quality_controlled":"1","type":"journal_article"},{"type":"journal_article","quality_controlled":"1","month":"02","publication_status":"published","oa_version":"None","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","date_published":"2011-02-01T00:00:00Z","_id":"11096","publication_identifier":{"issn":["0955-0674"]},"article_processing_charge":"No","page":"65-70","author":[{"first_name":"Yun","last_name":"Liang","full_name":"Liang, Yun"},{"id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","last_name":"HETZER","first_name":"Martin W","full_name":"HETZER, Martin W","orcid":"0000-0002-2111-992X"}],"abstract":[{"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.","lang":"eng"}],"issue":"1","year":"2011","keyword":["Cell Biology"],"publisher":"Elsevier","extern":"1","volume":23,"status":"public","date_created":"2022-04-07T07:52:37Z","scopus_import":"1","pmid":1,"article_type":"original","language":[{"iso":"eng"}],"day":"01","citation":{"mla":"Liang, Yun, and Martin Hetzer. “Functional Interactions between Nucleoporins and Chromatin.” <i>Current Opinion in Cell Biology</i>, vol. 23, no. 1, Elsevier, 2011, pp. 65–70, doi:<a href=\"https://doi.org/10.1016/j.ceb.2010.09.008\">10.1016/j.ceb.2010.09.008</a>.","ama":"Liang Y, Hetzer M. Functional interactions between nucleoporins and chromatin. <i>Current Opinion in Cell Biology</i>. 2011;23(1):65-70. doi:<a href=\"https://doi.org/10.1016/j.ceb.2010.09.008\">10.1016/j.ceb.2010.09.008</a>","apa":"Liang, Y., &#38; Hetzer, M. (2011). Functional interactions between nucleoporins and chromatin. <i>Current Opinion in Cell Biology</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.ceb.2010.09.008\">https://doi.org/10.1016/j.ceb.2010.09.008</a>","ieee":"Y. Liang and M. Hetzer, “Functional interactions between nucleoporins and chromatin,” <i>Current Opinion in Cell Biology</i>, vol. 23, no. 1. Elsevier, pp. 65–70, 2011.","chicago":"Liang, Yun, and Martin Hetzer. “Functional Interactions between Nucleoporins and Chromatin.” <i>Current Opinion in Cell Biology</i>. Elsevier, 2011. <a href=\"https://doi.org/10.1016/j.ceb.2010.09.008\">https://doi.org/10.1016/j.ceb.2010.09.008</a>.","short":"Y. Liang, M. Hetzer, Current Opinion in Cell Biology 23 (2011) 65–70.","ista":"Liang Y, Hetzer M. 2011. Functional interactions between nucleoporins and chromatin. Current Opinion in Cell Biology. 23(1), 65–70."},"date_updated":"2024-10-14T11:26:31Z","title":"Functional interactions between nucleoporins and chromatin","doi":"10.1016/j.ceb.2010.09.008","external_id":{"pmid":["21030234"]},"intvolume":"        23","publication":"Current Opinion in Cell Biology"},{"volume":2,"extern":"1","publisher":"Impact Journals","date_created":"2022-04-07T07:52:58Z","status":"public","pmid":1,"scopus_import":"1","day":"01","language":[{"iso":"eng"}],"article_type":"original","citation":{"ieee":"M. Hetzer, “The role of the nuclear pore complex in aging of post-mitotic cells,” <i>Aging</i>, vol. 2, no. 2. Impact Journals, pp. 74–75, 2010.","chicago":"Hetzer, Martin. “The Role of the Nuclear Pore Complex in Aging of Post-Mitotic Cells.” <i>Aging</i>. Impact Journals, 2010. <a href=\"https://doi.org/10.18632/aging.100125\">https://doi.org/10.18632/aging.100125</a>.","ista":"Hetzer M. 2010. The role of the nuclear pore complex in aging of post-mitotic cells. Aging. 2(2), 74–75.","short":"M. Hetzer, Aging 2 (2010) 74–75.","mla":"Hetzer, Martin. “The Role of the Nuclear Pore Complex in Aging of Post-Mitotic Cells.” <i>Aging</i>, vol. 2, no. 2, Impact Journals, 2010, pp. 74–75, doi:<a href=\"https://doi.org/10.18632/aging.100125\">10.18632/aging.100125</a>.","ama":"Hetzer M. The role of the nuclear pore complex in aging of post-mitotic cells. <i>Aging</i>. 2010;2(2):74-75. doi:<a href=\"https://doi.org/10.18632/aging.100125\">10.18632/aging.100125</a>","apa":"Hetzer, M. (2010). The role of the nuclear pore complex in aging of post-mitotic cells. <i>Aging</i>. Impact Journals. <a href=\"https://doi.org/10.18632/aging.100125\">https://doi.org/10.18632/aging.100125</a>"},"doi":"10.18632/aging.100125","date_updated":"2024-10-14T11:26:51Z","title":"The role of the nuclear pore complex in aging of post-mitotic cells","publication":"Aging","intvolume":"         2","external_id":{"pmid":["20354266"]},"quality_controlled":"1","type":"journal_article","oa_version":"Published Version","month":"02","publication_status":"published","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","_id":"11098","date_published":"2010-02-01T00:00:00Z","publication_identifier":{"issn":["1945-4589"]},"article_processing_charge":"No","main_file_link":[{"url":"https://doi.org/10.18632/aging.100125","open_access":"1"}],"issue":"2","page":"74-75","author":[{"orcid":"0000-0002-2111-992X","full_name":"HETZER, Martin W","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","first_name":"Martin W","last_name":"HETZER"}],"oa":1,"keyword":["Cell Biology","Aging"],"year":"2010"},{"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","_id":"8473","article_type":"original","date_published":"2010-02-19T00:00:00Z","day":"19","language":[{"iso":"eng"}],"extern":"1","type":"journal_article","publisher":"American Society for Biochemistry & Molecular Biology","quality_controlled":"1","volume":285,"oa_version":"None","status":"public","month":"02","publication_status":"published","date_created":"2020-09-18T10:11:23Z","doi":"10.1074/jbc.m109.061168","author":[{"first_name":"Alessandra","last_name":"Corazza","full_name":"Corazza, Alessandra"},{"full_name":"Rennella, Enrico","last_name":"Rennella","first_name":"Enrico"},{"last_name":"Schanda","first_name":"Paul","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","orcid":"0000-0002-9350-7606","full_name":"Schanda, Paul"},{"last_name":"Mimmi","first_name":"Maria Chiara","full_name":"Mimmi, Maria Chiara"},{"last_name":"Cutuil","first_name":"Thomas","full_name":"Cutuil, Thomas"},{"full_name":"Raimondi, Sara","first_name":"Sara","last_name":"Raimondi"},{"full_name":"Giorgetti, Sofia","last_name":"Giorgetti","first_name":"Sofia"},{"first_name":"Federico","last_name":"Fogolari","full_name":"Fogolari, Federico"},{"last_name":"Viglino","first_name":"Paolo","full_name":"Viglino, Paolo"},{"first_name":"Lucio","last_name":"Frydman","full_name":"Frydman, Lucio"},{"first_name":"Maayan","last_name":"Gal","full_name":"Gal, Maayan"},{"last_name":"Bellotti","first_name":"Vittorio","full_name":"Bellotti, Vittorio"},{"last_name":"Brutscher","first_name":"Bernhard","full_name":"Brutscher, Bernhard"},{"last_name":"Esposito","first_name":"Gennaro","full_name":"Esposito, Gennaro"}],"page":"5827-5835","date_updated":"2021-01-12T08:19:31Z","title":"Native-unlike long-lived intermediates along the folding pathway of the amyloidogenic protein β2-Microglobulin revealed by real-time two-dimensional NMR","abstract":[{"lang":"eng","text":"β2-microglobulin (β2m), the light chain of class I major histocompatibility complex, is responsible for the dialysis-related amyloidosis and, in patients undergoing long term dialysis, the full-length and chemically unmodified β2m converts into amyloid fibrils. The protein, belonging to the immunoglobulin superfamily, in common to other members of this family, experiences during its folding a long-lived intermediate associated to the trans-to-cis isomerization of Pro-32 that has been addressed as the precursor of the amyloid fibril formation. In this respect, previous studies on the W60G β2m mutant, showing that the lack of Trp-60 prevents fibril formation in mild aggregating condition, prompted us to reinvestigate the refolding kinetics of wild type and W60G β2m at atomic resolution by real-time NMR. The analysis, conducted at ambient temperature by the band selective flip angle short transient real-time two-dimensional NMR techniques and probing the β2m states every 15 s, revealed a more complex folding energy landscape than previously reported for wild type β2m, involving more than a single intermediate species, and shedding new light into the fibrillogenic pathway. Moreover, a significant difference in the kinetic scheme previously characterized by optical spectroscopic methods was discovered for the W60G β2m mutant."}],"issue":"8","intvolume":"       285","keyword":["Cell Biology","Biochemistry","Molecular Biology"],"year":"2010","publication":"Journal of Biological Chemistry","publication_identifier":{"issn":["0021-9258","1083-351X"]},"citation":{"apa":"Corazza, A., Rennella, E., Schanda, P., Mimmi, M. C., Cutuil, T., Raimondi, S., … Esposito, G. (2010). Native-unlike long-lived intermediates along the folding pathway of the amyloidogenic protein β2-Microglobulin revealed by real-time two-dimensional NMR. <i>Journal of Biological Chemistry</i>. American Society for Biochemistry &#38; Molecular Biology. <a href=\"https://doi.org/10.1074/jbc.m109.061168\">https://doi.org/10.1074/jbc.m109.061168</a>","ama":"Corazza A, Rennella E, Schanda P, et al. Native-unlike long-lived intermediates along the folding pathway of the amyloidogenic protein β2-Microglobulin revealed by real-time two-dimensional NMR. <i>Journal of Biological Chemistry</i>. 2010;285(8):5827-5835. doi:<a href=\"https://doi.org/10.1074/jbc.m109.061168\">10.1074/jbc.m109.061168</a>","mla":"Corazza, Alessandra, et al. “Native-Unlike Long-Lived Intermediates along the Folding Pathway of the Amyloidogenic Protein Β2-Microglobulin Revealed by Real-Time Two-Dimensional NMR.” <i>Journal of Biological Chemistry</i>, vol. 285, no. 8, American Society for Biochemistry &#38; Molecular Biology, 2010, pp. 5827–35, doi:<a href=\"https://doi.org/10.1074/jbc.m109.061168\">10.1074/jbc.m109.061168</a>.","ista":"Corazza A, Rennella E, Schanda P, Mimmi MC, Cutuil T, Raimondi S, Giorgetti S, Fogolari F, Viglino P, Frydman L, Gal M, Bellotti V, Brutscher B, Esposito G. 2010. Native-unlike long-lived intermediates along the folding pathway of the amyloidogenic protein β2-Microglobulin revealed by real-time two-dimensional NMR. Journal of Biological Chemistry. 285(8), 5827–5835.","chicago":"Corazza, Alessandra, Enrico Rennella, Paul Schanda, Maria Chiara Mimmi, Thomas Cutuil, Sara Raimondi, Sofia Giorgetti, et al. “Native-Unlike Long-Lived Intermediates along the Folding Pathway of the Amyloidogenic Protein Β2-Microglobulin Revealed by Real-Time Two-Dimensional NMR.” <i>Journal of Biological Chemistry</i>. American Society for Biochemistry &#38; Molecular Biology, 2010. <a href=\"https://doi.org/10.1074/jbc.m109.061168\">https://doi.org/10.1074/jbc.m109.061168</a>.","short":"A. Corazza, E. Rennella, P. Schanda, M.C. Mimmi, T. Cutuil, S. Raimondi, S. Giorgetti, F. Fogolari, P. Viglino, L. Frydman, M. Gal, V. Bellotti, B. Brutscher, G. Esposito, Journal of Biological Chemistry 285 (2010) 5827–5835.","ieee":"A. Corazza <i>et al.</i>, “Native-unlike long-lived intermediates along the folding pathway of the amyloidogenic protein β2-Microglobulin revealed by real-time two-dimensional NMR,” <i>Journal of Biological Chemistry</i>, vol. 285, no. 8. American Society for Biochemistry &#38; Molecular Biology, pp. 5827–5835, 2010."},"article_processing_charge":"No"},{"date_created":"2022-04-07T07:53:45Z","status":"public","volume":17,"extern":"1","publisher":"Elsevier","day":"17","language":[{"iso":"eng"}],"article_type":"review","pmid":1,"scopus_import":"1","citation":{"ama":"Hetzer M, Wente SR. Border control at the nucleus: Biogenesis and organization of the nuclear membrane and pore complexes. <i>Developmental Cell</i>. 2009;17(5):606-616. doi:<a href=\"https://doi.org/10.1016/j.devcel.2009.10.007\">10.1016/j.devcel.2009.10.007</a>","mla":"Hetzer, Martin, and Susan R. Wente. “Border Control at the Nucleus: Biogenesis and Organization of the Nuclear Membrane and Pore Complexes.” <i>Developmental Cell</i>, vol. 17, no. 5, Elsevier, 2009, pp. 606–16, doi:<a href=\"https://doi.org/10.1016/j.devcel.2009.10.007\">10.1016/j.devcel.2009.10.007</a>.","apa":"Hetzer, M., &#38; Wente, S. R. (2009). Border control at the nucleus: Biogenesis and organization of the nuclear membrane and pore complexes. <i>Developmental Cell</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.devcel.2009.10.007\">https://doi.org/10.1016/j.devcel.2009.10.007</a>","short":"M. Hetzer, S.R. Wente, Developmental Cell 17 (2009) 606–616.","chicago":"Hetzer, Martin, and Susan R. Wente. “Border Control at the Nucleus: Biogenesis and Organization of the Nuclear Membrane and Pore Complexes.” <i>Developmental Cell</i>. Elsevier, 2009. <a href=\"https://doi.org/10.1016/j.devcel.2009.10.007\">https://doi.org/10.1016/j.devcel.2009.10.007</a>.","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.","ieee":"M. Hetzer and S. R. Wente, “Border control at the nucleus: Biogenesis and organization of the nuclear membrane and pore complexes,” <i>Developmental Cell</i>, vol. 17, no. 5. Elsevier, pp. 606–616, 2009."},"publication":"Developmental Cell","intvolume":"        17","external_id":{"pmid":["19922866"]},"doi":"10.1016/j.devcel.2009.10.007","date_updated":"2024-10-14T11:28:25Z","title":"Border control at the nucleus: Biogenesis and organization of the nuclear membrane and pore complexes","oa_version":"Published Version","publication_status":"published","month":"11","quality_controlled":"1","type":"journal_article","_id":"11103","date_published":"2009-11-17T00:00:00Z","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","article_processing_charge":"No","main_file_link":[{"url":"https://doi.org/10.1016/j.devcel.2009.10.007","open_access":"1"}],"publication_identifier":{"issn":["1534-5807"]},"oa":1,"keyword":["Developmental Biology","Cell Biology","General Biochemistry","Genetics and Molecular Biology","Molecular Biology"],"year":"2009","issue":"5","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"}],"author":[{"orcid":"0000-0002-2111-992X","full_name":"HETZER, Martin W","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","first_name":"Martin W","last_name":"HETZER"},{"full_name":"Wente, Susan R.","last_name":"Wente","first_name":"Susan R."}],"page":"606-616"},{"date_updated":"2024-10-14T11:28:48Z","title":"Recruitment of functionally distinct membrane proteins to chromatin mediates nuclear envelope formation in vivo","doi":"10.1083/jcb.200901106","external_id":{"pmid":["19620630"]},"intvolume":"       186","publication":"Journal of Cell Biology","citation":{"apa":"Anderson, D. J., Vargas, J. D., Hsiao, J. P., &#38; Hetzer, M. (2009). Recruitment of functionally distinct membrane proteins to chromatin mediates nuclear envelope formation in vivo. <i>Journal of Cell Biology</i>. Rockefeller University Press. <a href=\"https://doi.org/10.1083/jcb.200901106\">https://doi.org/10.1083/jcb.200901106</a>","mla":"Anderson, Daniel J., et al. “Recruitment of Functionally Distinct Membrane Proteins to Chromatin Mediates Nuclear Envelope Formation in Vivo.” <i>Journal of Cell Biology</i>, vol. 186, no. 2, Rockefeller University Press, 2009, pp. 183–91, doi:<a href=\"https://doi.org/10.1083/jcb.200901106\">10.1083/jcb.200901106</a>.","ama":"Anderson DJ, Vargas JD, Hsiao JP, Hetzer M. Recruitment of functionally distinct membrane proteins to chromatin mediates nuclear envelope formation in vivo. <i>Journal of Cell Biology</i>. 2009;186(2):183-191. doi:<a href=\"https://doi.org/10.1083/jcb.200901106\">10.1083/jcb.200901106</a>","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,” <i>Journal of Cell Biology</i>, vol. 186, no. 2. Rockefeller University Press, pp. 183–191, 2009.","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.","short":"D.J. Anderson, J.D. Vargas, J.P. Hsiao, M. Hetzer, Journal of Cell Biology 186 (2009) 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.” <i>Journal of Cell Biology</i>. Rockefeller University Press, 2009. <a href=\"https://doi.org/10.1083/jcb.200901106\">https://doi.org/10.1083/jcb.200901106</a>."},"scopus_import":"1","pmid":1,"article_type":"original","language":[{"iso":"eng"}],"related_material":{"link":[{"url":"https://doi.org/10.1083/jcb.20090110620090903c","relation":"erratum"}]},"day":"20","extern":"1","publisher":"Rockefeller University Press","volume":186,"status":"public","date_created":"2022-04-07T07:54:18Z","page":"183-191","author":[{"full_name":"Anderson, Daniel J.","first_name":"Daniel J.","last_name":"Anderson"},{"last_name":"Vargas","first_name":"Jesse D.","full_name":"Vargas, Jesse D."},{"full_name":"Hsiao, Joshua P.","first_name":"Joshua P.","last_name":"Hsiao"},{"full_name":"HETZER, Martin W","orcid":"0000-0002-2111-992X","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","first_name":"Martin W","last_name":"HETZER"}],"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."}],"issue":"2","year":"2009","keyword":["Cell Biology"],"oa":1,"publication_identifier":{"eissn":["1540-8140"],"issn":["0021-9525"]},"main_file_link":[{"open_access":"1","url":"https://doi.org/10.1083/jcb.200901106"}],"article_processing_charge":"No","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","date_published":"2009-07-20T00:00:00Z","_id":"11106","type":"journal_article","quality_controlled":"1","month":"07","publication_status":"published","oa_version":"Published Version"},{"day":"09","language":[{"iso":"eng"}],"article_type":"original","pmid":1,"scopus_import":"1","date_created":"2022-04-07T07:54:44Z","status":"public","volume":184,"publisher":"Rockefeller University Press","extern":"1","publication":"Journal of Cell Biology","external_id":{"pmid":["19273614"]},"intvolume":"       184","title":"ER membrane–bending proteins are necessary for de novo nuclear pore formation","date_updated":"2022-07-18T08:55:05Z","doi":"10.1083/jcb.200806174","citation":{"apa":"Dawson, T. R., Lazarus, M. D., Hetzer, M., &#38; Wente, S. R. (2009). ER membrane–bending proteins are necessary for de novo nuclear pore formation. <i>Journal of Cell Biology</i>. Rockefeller University Press. <a href=\"https://doi.org/10.1083/jcb.200806174\">https://doi.org/10.1083/jcb.200806174</a>","ama":"Dawson TR, Lazarus MD, Hetzer M, Wente SR. ER membrane–bending proteins are necessary for de novo nuclear pore formation. <i>Journal of Cell Biology</i>. 2009;184(5):659-675. doi:<a href=\"https://doi.org/10.1083/jcb.200806174\">10.1083/jcb.200806174</a>","mla":"Dawson, T. Renee, et al. “ER Membrane–Bending Proteins Are Necessary for de Novo Nuclear Pore Formation.” <i>Journal of Cell Biology</i>, vol. 184, no. 5, Rockefeller University Press, 2009, pp. 659–75, doi:<a href=\"https://doi.org/10.1083/jcb.200806174\">10.1083/jcb.200806174</a>.","short":"T.R. Dawson, M.D. Lazarus, M. Hetzer, S.R. Wente, Journal of Cell Biology 184 (2009) 659–675.","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.” <i>Journal of Cell Biology</i>. Rockefeller University Press, 2009. <a href=\"https://doi.org/10.1083/jcb.200806174\">https://doi.org/10.1083/jcb.200806174</a>.","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,” <i>Journal of Cell Biology</i>, vol. 184, no. 5. Rockefeller University Press, pp. 659–675, 2009."},"date_published":"2009-03-09T00:00:00Z","_id":"11107","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","month":"03","publication_status":"published","oa_version":"Published Version","quality_controlled":"1","type":"journal_article","oa":1,"year":"2009","keyword":["Cell Biology"],"abstract":[{"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.","lang":"eng"}],"issue":"5","page":"659-675","author":[{"full_name":"Dawson, T. Renee","first_name":"T. Renee","last_name":"Dawson"},{"first_name":"Michelle D.","last_name":"Lazarus","full_name":"Lazarus, Michelle D."},{"full_name":"HETZER, Martin W","orcid":"0000-0002-2111-992X","first_name":"Martin W","last_name":"HETZER","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed"},{"full_name":"Wente, Susan R.","last_name":"Wente","first_name":"Susan R."}],"article_processing_charge":"No","main_file_link":[{"open_access":"1","url":"https://doi.org/10.1083/jcb.200806174"}],"publication_identifier":{"eissn":["1540-8140"],"issn":["0021-9525"]}},{"doi":"10.1016/j.ceb.2008.09.010","date_updated":"2024-10-14T11:29:10Z","title":"Reorganization of the nuclear envelope during open mitosis","intvolume":"        20","external_id":{"pmid":["18938243"]},"publication":"Current Opinion in Cell Biology","citation":{"mla":"Kutay, Ulrike, and Martin Hetzer. “Reorganization of the Nuclear Envelope during Open Mitosis.” <i>Current Opinion in Cell Biology</i>, vol. 20, no. 6, Elsevier, 2008, pp. 669–77, doi:<a href=\"https://doi.org/10.1016/j.ceb.2008.09.010\">10.1016/j.ceb.2008.09.010</a>.","ama":"Kutay U, Hetzer M. Reorganization of the nuclear envelope during open mitosis. <i>Current Opinion in Cell Biology</i>. 2008;20(6):669-677. doi:<a href=\"https://doi.org/10.1016/j.ceb.2008.09.010\">10.1016/j.ceb.2008.09.010</a>","apa":"Kutay, U., &#38; Hetzer, M. (2008). Reorganization of the nuclear envelope during open mitosis. <i>Current Opinion in Cell Biology</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.ceb.2008.09.010\">https://doi.org/10.1016/j.ceb.2008.09.010</a>","ieee":"U. Kutay and M. Hetzer, “Reorganization of the nuclear envelope during open mitosis,” <i>Current Opinion in Cell Biology</i>, vol. 20, no. 6. Elsevier, pp. 669–677, 2008.","chicago":"Kutay, Ulrike, and Martin Hetzer. “Reorganization of the Nuclear Envelope during Open Mitosis.” <i>Current Opinion in Cell Biology</i>. Elsevier, 2008. <a href=\"https://doi.org/10.1016/j.ceb.2008.09.010\">https://doi.org/10.1016/j.ceb.2008.09.010</a>.","short":"U. Kutay, M. Hetzer, Current Opinion in Cell Biology 20 (2008) 669–677.","ista":"Kutay U, Hetzer M. 2008. Reorganization of the nuclear envelope during open mitosis. Current Opinion in Cell Biology. 20(6), 669–677."},"scopus_import":"1","pmid":1,"article_type":"original","language":[{"iso":"eng"}],"day":"01","extern":"1","publisher":"Elsevier","volume":20,"status":"public","date_created":"2022-04-07T07:55:00Z","author":[{"first_name":"Ulrike","last_name":"Kutay","full_name":"Kutay, Ulrike"},{"id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","last_name":"HETZER","first_name":"Martin W","orcid":"0000-0002-2111-992X","full_name":"HETZER, Martin W"}],"page":"669-677","issue":"6","abstract":[{"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.","lang":"eng"}],"keyword":["Cell Biology"],"year":"2008","publication_identifier":{"issn":["0955-0674"]},"article_processing_charge":"No","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","_id":"11109","date_published":"2008-12-01T00:00:00Z","type":"journal_article","quality_controlled":"1","oa_version":"None","month":"12","publication_status":"published"},{"date_created":"2022-04-07T07:55:10Z","status":"public","volume":18,"extern":"1","publisher":"Elsevier","language":[{"iso":"eng"}],"day":"01","article_type":"review","pmid":1,"scopus_import":"1","citation":{"ama":"D’Angelo MA, Hetzer M. Structure, dynamics and function of nuclear pore complexes. <i>Trends in Cell Biology</i>. 2008;18(10):456-466. doi:<a href=\"https://doi.org/10.1016/j.tcb.2008.07.009\">10.1016/j.tcb.2008.07.009</a>","mla":"D’Angelo, Maximiliano A., and Martin Hetzer. “Structure, Dynamics and Function of Nuclear Pore Complexes.” <i>Trends in Cell Biology</i>, vol. 18, no. 10, Elsevier, 2008, pp. 456–66, doi:<a href=\"https://doi.org/10.1016/j.tcb.2008.07.009\">10.1016/j.tcb.2008.07.009</a>.","apa":"D’Angelo, M. A., &#38; Hetzer, M. (2008). Structure, dynamics and function of nuclear pore complexes. <i>Trends in Cell Biology</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.tcb.2008.07.009\">https://doi.org/10.1016/j.tcb.2008.07.009</a>","chicago":"D’Angelo, Maximiliano A., and Martin Hetzer. “Structure, Dynamics and Function of Nuclear Pore Complexes.” <i>Trends in Cell Biology</i>. Elsevier, 2008. <a href=\"https://doi.org/10.1016/j.tcb.2008.07.009\">https://doi.org/10.1016/j.tcb.2008.07.009</a>.","ista":"D’Angelo MA, Hetzer M. 2008. Structure, dynamics and function of nuclear pore complexes. Trends in Cell Biology. 18(10), 456–466.","short":"M.A. D’Angelo, M. Hetzer, Trends in Cell Biology 18 (2008) 456–466.","ieee":"M. A. D’Angelo and M. Hetzer, “Structure, dynamics and function of nuclear pore complexes,” <i>Trends in Cell Biology</i>, vol. 18, no. 10. Elsevier, pp. 456–466, 2008."},"publication":"Trends in Cell Biology","intvolume":"        18","external_id":{"pmid":["18786826"]},"doi":"10.1016/j.tcb.2008.07.009","title":"Structure, dynamics and function of nuclear pore complexes","date_updated":"2024-10-14T11:29:21Z","oa_version":"None","month":"10","publication_status":"published","quality_controlled":"1","type":"journal_article","_id":"11110","date_published":"2008-10-01T00:00:00Z","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","article_processing_charge":"No","publication_identifier":{"issn":["0962-8924"]},"keyword":["Cell Biology"],"year":"2008","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"}],"issue":"10","author":[{"full_name":"D’Angelo, Maximiliano A.","last_name":"D’Angelo","first_name":"Maximiliano A."},{"id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","first_name":"Martin W","last_name":"HETZER","orcid":"0000-0002-2111-992X","full_name":"HETZER, Martin W"}],"page":"456-466"},{"volume":182,"publisher":"Rockefeller University Press","extern":"1","date_created":"2022-04-07T07:55:23Z","status":"public","pmid":1,"scopus_import":"1","day":"08","language":[{"iso":"eng"}],"article_type":"original","citation":{"short":"D.J. Anderson, M. Hetzer, Journal of Cell Biology 182 (2008) 911–924.","chicago":"Anderson, Daniel J., and Martin Hetzer. “Reshaping of the Endoplasmic Reticulum Limits the Rate for Nuclear Envelope Formation.” <i>Journal of Cell Biology</i>. Rockefeller University Press, 2008. <a href=\"https://doi.org/10.1083/jcb.200805140\">https://doi.org/10.1083/jcb.200805140</a>.","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.","ieee":"D. J. Anderson and M. Hetzer, “Reshaping of the endoplasmic reticulum limits the rate for nuclear envelope formation,” <i>Journal of Cell Biology</i>, vol. 182, no. 5. Rockefeller University Press, pp. 911–924, 2008.","apa":"Anderson, D. J., &#38; Hetzer, M. (2008). Reshaping of the endoplasmic reticulum limits the rate for nuclear envelope formation. <i>Journal of Cell Biology</i>. Rockefeller University Press. <a href=\"https://doi.org/10.1083/jcb.200805140\">https://doi.org/10.1083/jcb.200805140</a>","ama":"Anderson DJ, Hetzer M. Reshaping of the endoplasmic reticulum limits the rate for nuclear envelope formation. <i>Journal of Cell Biology</i>. 2008;182(5):911-924. doi:<a href=\"https://doi.org/10.1083/jcb.200805140\">10.1083/jcb.200805140</a>","mla":"Anderson, Daniel J., and Martin Hetzer. “Reshaping of the Endoplasmic Reticulum Limits the Rate for Nuclear Envelope Formation.” <i>Journal of Cell Biology</i>, vol. 182, no. 5, Rockefeller University Press, 2008, pp. 911–24, doi:<a href=\"https://doi.org/10.1083/jcb.200805140\">10.1083/jcb.200805140</a>."},"doi":"10.1083/jcb.200805140","title":"Reshaping of the endoplasmic reticulum limits the rate for nuclear envelope formation","date_updated":"2024-10-14T11:29:29Z","publication":"Journal of Cell Biology","intvolume":"       182","external_id":{"pmid":["18779370"]},"quality_controlled":"1","type":"journal_article","oa_version":"None","month":"09","publication_status":"published","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","_id":"11111","date_published":"2008-09-08T00:00:00Z","publication_identifier":{"eissn":["1540-8140"],"issn":["0021-9525"]},"article_processing_charge":"No","issue":"5","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"}],"page":"911-924","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","orcid":"0000-0002-2111-992X","full_name":"HETZER, Martin W"}],"keyword":["Cell Biology"],"year":"2008"},{"date_published":"2008-08-01T00:00:00Z","_id":"11112","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","publication_status":"published","month":"08","oa_version":"None","quality_controlled":"1","type":"journal_article","year":"2008","keyword":["Cell Biology"],"abstract":[{"lang":"eng","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."}],"issue":"4","page":"386-392","author":[{"last_name":"Anderson","first_name":"Daniel J","full_name":"Anderson, 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"}],"article_processing_charge":"No","publication_identifier":{"issn":["0955-0674"]},"language":[{"iso":"eng"}],"day":"01","article_type":"original","pmid":1,"scopus_import":"1","date_created":"2022-04-07T07:55:34Z","status":"public","volume":20,"extern":"1","publisher":"Elsevier","publication":"Current Opinion in Cell Biology","external_id":{"pmid":["18495454"]},"intvolume":"        20","title":"The life cycle of the metazoan nuclear envelope","date_updated":"2024-10-14T11:29:38Z","doi":"10.1016/j.ceb.2008.03.016","citation":{"apa":"Anderson, D. J., &#38; Hetzer, M. (2008). The life cycle of the metazoan nuclear envelope. <i>Current Opinion in Cell Biology</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.ceb.2008.03.016\">https://doi.org/10.1016/j.ceb.2008.03.016</a>","ama":"Anderson DJ, Hetzer M. The life cycle of the metazoan nuclear envelope. <i>Current Opinion in Cell Biology</i>. 2008;20(4):386-392. doi:<a href=\"https://doi.org/10.1016/j.ceb.2008.03.016\">10.1016/j.ceb.2008.03.016</a>","mla":"Anderson, Daniel J., and Martin Hetzer. “The Life Cycle of the Metazoan Nuclear Envelope.” <i>Current Opinion in Cell Biology</i>, vol. 20, no. 4, Elsevier, 2008, pp. 386–92, doi:<a href=\"https://doi.org/10.1016/j.ceb.2008.03.016\">10.1016/j.ceb.2008.03.016</a>.","ista":"Anderson DJ, Hetzer M. 2008. The life cycle of the metazoan nuclear envelope. Current Opinion in Cell Biology. 20(4), 386–392.","chicago":"Anderson, Daniel J, and Martin Hetzer. “The Life Cycle of the Metazoan Nuclear Envelope.” <i>Current Opinion in Cell Biology</i>. Elsevier, 2008. <a href=\"https://doi.org/10.1016/j.ceb.2008.03.016\">https://doi.org/10.1016/j.ceb.2008.03.016</a>.","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,” <i>Current Opinion in Cell Biology</i>, vol. 20, no. 4. Elsevier, pp. 386–392, 2008."}},{"quality_controlled":"1","type":"journal_article","publication_status":"published","month":"01","oa_version":"Published Version","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","date_published":"2008-01-15T00:00:00Z","_id":"11113","publication_identifier":{"issn":["0021-9533"],"eissn":["1477-9137"]},"article_processing_charge":"No","main_file_link":[{"url":"https://doi.org/10.1242/jcs.005777","open_access":"1"}],"issue":"2","abstract":[{"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.","lang":"eng"}],"author":[{"first_name":"Daniel J.","last_name":"Anderson","full_name":"Anderson, Daniel J."},{"orcid":"0000-0002-2111-992X","full_name":"HETZER, Martin W","first_name":"Martin W","last_name":"HETZER","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed"}],"page":"137-142","oa":1,"year":"2008","keyword":["Cell Biology"],"volume":121,"extern":"1","publisher":"The Company of Biologists","date_created":"2022-04-07T07:55:46Z","status":"public","pmid":1,"scopus_import":"1","language":[{"iso":"eng"}],"day":"15","article_type":"letter_note","citation":{"ista":"Anderson DJ, Hetzer M. 2008. Shaping the endoplasmic reticulum into the nuclear envelope. Journal of Cell Science. 121(2), 137–142.","short":"D.J. Anderson, M. Hetzer, Journal of Cell Science 121 (2008) 137–142.","chicago":"Anderson, Daniel J., and Martin Hetzer. “Shaping the Endoplasmic Reticulum into the Nuclear Envelope.” <i>Journal of Cell Science</i>. The Company of Biologists, 2008. <a href=\"https://doi.org/10.1242/jcs.005777\">https://doi.org/10.1242/jcs.005777</a>.","ieee":"D. J. Anderson and M. Hetzer, “Shaping the endoplasmic reticulum into the nuclear envelope,” <i>Journal of Cell Science</i>, vol. 121, no. 2. The Company of Biologists, pp. 137–142, 2008.","apa":"Anderson, D. J., &#38; Hetzer, M. (2008). Shaping the endoplasmic reticulum into the nuclear envelope. <i>Journal of Cell Science</i>. The Company of Biologists. <a href=\"https://doi.org/10.1242/jcs.005777\">https://doi.org/10.1242/jcs.005777</a>","ama":"Anderson DJ, Hetzer M. Shaping the endoplasmic reticulum into the nuclear envelope. <i>Journal of Cell Science</i>. 2008;121(2):137-142. doi:<a href=\"https://doi.org/10.1242/jcs.005777\">10.1242/jcs.005777</a>","mla":"Anderson, Daniel J., and Martin Hetzer. “Shaping the Endoplasmic Reticulum into the Nuclear Envelope.” <i>Journal of Cell Science</i>, vol. 121, no. 2, The Company of Biologists, 2008, pp. 137–42, doi:<a href=\"https://doi.org/10.1242/jcs.005777\">10.1242/jcs.005777</a>."},"title":"Shaping the endoplasmic reticulum into the nuclear envelope","date_updated":"2024-10-14T11:29:47Z","doi":"10.1242/jcs.005777","publication":"Journal of Cell Science","external_id":{"pmid":["18187447"]},"intvolume":"       121"}]