[{"isi":1,"user_id":"317138e5-6ab7-11ef-aa6d-ffef3953e345","file":[{"success":1,"checksum":"90d1984a93660735e506c2a304bc3f73","file_name":"2024_JCB_Zens.pdf","date_updated":"2024-03-25T12:52:04Z","content_type":"application/pdf","creator":"dernst","date_created":"2024-03-25T12:52:04Z","access_level":"open_access","file_id":"15188","file_size":11907016,"relation":"main_file"}],"oa":1,"article_type":"original","publication_status":"published","project":[{"name":"Structure and isoform diversity of the Arp2/3 complex","grant_number":"P33367","_id":"9B954C5C-BA93-11EA-9121-9846C619BF3A"},{"name":"In Situ Actin Structures via Hybrid Cryo-electron Microscopy","grant_number":"E435","_id":"7bd318a1-9f16-11ee-852c-cc9217763180"},{"_id":"25FE9508-B435-11E9-9278-68D0E5697425","grant_number":"724373","name":"Cellular Navigation Along Spatial Gradients","call_identifier":"H2020"},{"_id":"059B463C-7A3F-11EA-A408-12923DDC885E","name":"NÖ-Fonds Preis für die Jungforscherin des Jahres am IST Austria"},{"name":"Spatiotemporal regulation of chemokine-induced signalling in leukocyte chemotaxis","_id":"2615199A-B435-11E9-9278-68D0E5697425","grant_number":"21317"},{"grant_number":"CZI01","_id":"62909c6f-2b32-11ec-9570-e1476aab5308","name":"CryoMinflux-guided in-situ visual proteomics and structure determination"}],"author":[{"full_name":"Zens, Bettina","id":"45FD126C-F248-11E8-B48F-1D18A9856A87","first_name":"Bettina","orcid":"0000-0002-9561-1239","last_name":"Zens"},{"orcid":"0000-0001-7149-769X","last_name":"Fäßler","first_name":"Florian","id":"404F5528-F248-11E8-B48F-1D18A9856A87","full_name":"Fäßler, Florian"},{"last_name":"Hansen","orcid":"0000-0001-7967-2085","first_name":"Jesse","id":"1063c618-6f9b-11ec-9123-f912fccded63","full_name":"Hansen, Jesse"},{"first_name":"Robert","id":"4E01D6B4-F248-11E8-B48F-1D18A9856A87","full_name":"Hauschild, Robert","orcid":"0000-0001-9843-3522","last_name":"Hauschild"},{"orcid":"0000-0002-3616-8580","last_name":"Datler","first_name":"Julia","id":"3B12E2E6-F248-11E8-B48F-1D18A9856A87","full_name":"Datler, Julia"},{"last_name":"Hodirnau","orcid":"0000-0003-3904-947X","first_name":"Victor-Valentin","full_name":"Hodirnau, Victor-Valentin","id":"3661B498-F248-11E8-B48F-1D18A9856A87"},{"last_name":"Zheden","orcid":"0000-0002-9438-4783","full_name":"Zheden, Vanessa","id":"39C5A68A-F248-11E8-B48F-1D18A9856A87","first_name":"Vanessa"},{"id":"2CC12E8C-F248-11E8-B48F-1D18A9856A87","full_name":"Alanko, Jonna H","first_name":"Jonna H","last_name":"Alanko","orcid":"0000-0002-7698-3061"},{"first_name":"Michael K","full_name":"Sixt, Michael K","id":"41E9FBEA-F248-11E8-B48F-1D18A9856A87","last_name":"Sixt","orcid":"0000-0002-6620-9179"},{"first_name":"Florian KM","id":"48AD8942-F248-11E8-B48F-1D18A9856A87","full_name":"Schur, Florian KM","last_name":"Schur","orcid":"0000-0003-4790-8078"}],"ddc":["570"],"acknowledgement":"Open Access funding provided by IST Austria. We thank Armel Nicolas and his team at the ISTA proteomics facility, Alois Schloegl, Stefano Elefante, and colleagues at the ISTA Scientific Computing facility, Tommaso Constanzo and Ludek Lovicar at the Electron Microsocpy Facility (EMF), and Thomas Menner at the Miba Machine shop for their support. We also thank Wanda Kukulski (University of Bern) as well as Darío Porley, Andreas Thader, and other members of the Schur group for helpful discussions. Matt Swulius and Jessica Heebner provided great support in using Dragonfly. We thank Dorotea Fracciolla (Art & Science) for support in figure illustration.\r\n\r\nThis research was supported by the Scientific Service Units of ISTA through resources provided by Scientific Computing, the Lab Support Facility, and the Electron Microscopy Facility. We acknowledge funding support from the following sources: Austrian Science Fund (FWF) grant P33367 (to F.K.M. Schur), the Federation of European Biochemical Societies (to F.K.M. Schur), Niederösterreich (NÖ) Fonds (to B. Zens), FWF grant E435 (to J.M. Hansen), European Research Council under the European Union’s Horizon 2020 research (grant agreement No. 724373) (to M. Sixt), and Jenny and Antti Wihuri Foundation (to J. Alanko). This publication has been made possible in part by CZI grant DAF2021-234754 and grant DOI https://doi.org/10.37921/812628ebpcwg from the Chan Zuckerberg Initiative DAF, an advised fund of Silicon Valley Community Foundation (to F.K.M. Schur).","date_published":"2024-03-20T00:00:00Z","abstract":[{"lang":"eng","text":"The extracellular matrix (ECM) serves as a scaffold for cells and plays an essential role in regulating numerous cellular processes, including cell migration and proliferation. Due to limitations in specimen preparation for conventional room-temperature electron microscopy, we lack structural knowledge on how ECM components are secreted, remodeled, and interact with surrounding cells. We have developed a 3D-ECM platform compatible with sample thinning by cryo-focused ion beam milling, the lift-out extraction procedure, and cryo-electron tomography. Our workflow implements cell-derived matrices (CDMs) grown on EM grids, resulting in a versatile tool closely mimicking ECM environments. This allows us to visualize ECM for the first time in its hydrated, native context. Our data reveal an intricate network of extracellular fibers, their positioning relative to matrix-secreting cells, and previously unresolved structural entities. Our workflow and results add to the structural atlas of the ECM, providing novel insights into its secretion and assembly."}],"scopus_import":"1","status":"public","pmid":1,"month":"03","article_processing_charge":"Yes (via OA deal)","title":"Lift-out cryo-FIBSEM and cryo-ET reveal the ultrastructural landscape of extracellular matrix","_id":"15146","issue":"6","year":"2024","oa_version":"Published Version","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)"},"acknowledged_ssus":[{"_id":"LifeSc"},{"_id":"ScienComp"},{"_id":"EM-Fac"},{"_id":"M-Shop"}],"date_created":"2024-03-21T06:45:51Z","file_date_updated":"2024-03-25T12:52:04Z","department":[{"_id":"FlSc"},{"_id":"MiSi"},{"_id":"Bio"},{"_id":"EM-Fac"}],"article_number":"e202309125","has_accepted_license":"1","date_updated":"2025-09-04T13:17:16Z","corr_author":"1","external_id":{"isi":["001264190100001"],"pmid":["38506714"]},"quality_controlled":"1","language":[{"iso":"eng"}],"intvolume":"       223","publication_identifier":{"eissn":["1540-8140"],"issn":["0021-9525"]},"publication":"Journal of Cell Biology","publisher":"Rockefeller University Press","day":"20","doi":"10.1083/jcb.202309125","ec_funded":1,"type":"journal_article","citation":{"chicago":"Zens, Bettina, Florian Fäßler, Jesse Hansen, Robert Hauschild, Julia Datler, Victor-Valentin Hodirnau, Vanessa Zheden, Jonna H Alanko, Michael K Sixt, and Florian KM Schur. “Lift-out Cryo-FIBSEM and Cryo-ET Reveal the Ultrastructural Landscape of Extracellular Matrix.” <i>Journal of Cell Biology</i>. Rockefeller University Press, 2024. <a href=\"https://doi.org/10.1083/jcb.202309125\">https://doi.org/10.1083/jcb.202309125</a>.","ama":"Zens B, Fäßler F, Hansen J, et al. Lift-out cryo-FIBSEM and cryo-ET reveal the ultrastructural landscape of extracellular matrix. <i>Journal of Cell Biology</i>. 2024;223(6). doi:<a href=\"https://doi.org/10.1083/jcb.202309125\">10.1083/jcb.202309125</a>","ieee":"B. Zens <i>et al.</i>, “Lift-out cryo-FIBSEM and cryo-ET reveal the ultrastructural landscape of extracellular matrix,” <i>Journal of Cell Biology</i>, vol. 223, no. 6. Rockefeller University Press, 2024.","ista":"Zens B, Fäßler F, Hansen J, Hauschild R, Datler J, Hodirnau V-V, Zheden V, Alanko JH, Sixt MK, Schur FK. 2024. Lift-out cryo-FIBSEM and cryo-ET reveal the ultrastructural landscape of extracellular matrix. Journal of Cell Biology. 223(6), e202309125.","mla":"Zens, Bettina, et al. “Lift-out Cryo-FIBSEM and Cryo-ET Reveal the Ultrastructural Landscape of Extracellular Matrix.” <i>Journal of Cell Biology</i>, vol. 223, no. 6, e202309125, Rockefeller University Press, 2024, doi:<a href=\"https://doi.org/10.1083/jcb.202309125\">10.1083/jcb.202309125</a>.","apa":"Zens, B., Fäßler, F., Hansen, J., Hauschild, R., Datler, J., Hodirnau, V.-V., … Schur, F. K. (2024). Lift-out cryo-FIBSEM and cryo-ET reveal the ultrastructural landscape of extracellular matrix. <i>Journal of Cell Biology</i>. Rockefeller University Press. <a href=\"https://doi.org/10.1083/jcb.202309125\">https://doi.org/10.1083/jcb.202309125</a>","short":"B. Zens, F. Fäßler, J. Hansen, R. Hauschild, J. Datler, V.-V. Hodirnau, V. Zheden, J.H. Alanko, M.K. Sixt, F.K. Schur, Journal of Cell Biology 223 (2024)."},"volume":223},{"publication_status":"published","article_type":"original","author":[{"last_name":"Mund","full_name":"Mund, Markus","first_name":"Markus"},{"last_name":"Tschanz","full_name":"Tschanz, Aline","first_name":"Aline"},{"last_name":"Wu","full_name":"Wu, Yu-Le","first_name":"Yu-Le"},{"full_name":"Frey, Felix F","id":"a0270b37-8f1a-11ec-95c7-8e710c59a4f3","first_name":"Felix F","last_name":"Frey","orcid":"0000-0001-8501-6017"},{"last_name":"Mehl","full_name":"Mehl, Johanna L.","first_name":"Johanna L."},{"last_name":"Kaksonen","first_name":"Marko","full_name":"Kaksonen, Marko"},{"full_name":"Avinoam, Ori","first_name":"Ori","last_name":"Avinoam"},{"last_name":"Schwarz","full_name":"Schwarz, Ulrich S.","first_name":"Ulrich S."},{"last_name":"Ries","first_name":"Jonas","full_name":"Ries, Jonas"}],"file":[{"date_updated":"2024-01-16T10:15:09Z","file_name":"2023_JCB_Mund.pdf","success":1,"checksum":"505d5cac36c14b073b68c7fed1a92bd3","file_id":"14811","file_size":5678069,"relation":"main_file","content_type":"application/pdf","access_level":"open_access","date_created":"2024-01-16T10:15:09Z","creator":"dernst"}],"isi":1,"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","oa":1,"date_published":"2023-02-03T00:00:00Z","abstract":[{"text":"Eukaryotic cells use clathrin-mediated endocytosis to take up a large range of extracellular cargo. During endocytosis, a clathrin coat forms on the plasma membrane, but it remains controversial when and how it is remodeled into a spherical vesicle.\r\nHere, we use 3D superresolution microscopy to determine the precise geometry of the clathrin coat at large numbers of endocytic sites. Through pseudo-temporal sorting, we determine the average trajectory of clathrin remodeling during endocytosis. We find that clathrin coats assemble first on flat membranes to 50% of the coat area before they become rapidly and continuously bent, and this mechanism is confirmed in three cell lines. We introduce the cooperative curvature model, which is based on positive feedback for curvature generation. It accurately describes the measured shapes and dynamics of the clathrin coat and could represent a general mechanism for clathrin coat remodeling on the plasma membrane.","lang":"eng"}],"status":"public","acknowledgement":"We thank the entire Ries and Kaksonen labs for fruitful discussions and support. This work was supported by the European Research Council (ERC CoG-724489 to J. Ries), the National Institutes of Health Common Fund 4D Nucleome Program (Grant U01 to J. Ries), the Human Frontier Science Program (RGY0065/2017 to J. Ries), the EMBL Interdisciplinary Postdoc Programme (EIPOD) under Marie Curie Actions COFUND (Grant 229597 to O. Avinoam), the European Molecular Biology Laboratory (M. Mund, A. Tschanz, Y.-L. Wu and J. Ries), and the Swiss National Science Foundation (grant 310030B_182825 and NCCR Chemical Biology to M. Kaksonen). O. Avinoam is an incumbent of the Miriam Berman Presidential Development Chair.","ddc":["570"],"article_processing_charge":"No","pmid":1,"month":"02","year":"2023","issue":"3","_id":"14788","oa_version":"Published Version","title":"Clathrin coats partially preassemble and subsequently bend during endocytosis","keyword":["Cell Biology"],"date_created":"2024-01-10T10:45:55Z","file_date_updated":"2024-01-16T10:15:09Z","article_number":"e202206038","department":[{"_id":"AnSa"}],"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)"},"intvolume":"       222","language":[{"iso":"eng"}],"quality_controlled":"1","publication_identifier":{"eissn":["1540-8140"],"issn":["0021-9525"]},"date_updated":"2024-01-16T10:17:05Z","has_accepted_license":"1","external_id":{"pmid":["36734980"],"isi":["000978065000001"]},"publication":"Journal of Cell Biology","citation":{"ieee":"M. Mund <i>et al.</i>, “Clathrin coats partially preassemble and subsequently bend during endocytosis,” <i>Journal of Cell Biology</i>, vol. 222, no. 3. Rockefeller University Press, 2023.","ista":"Mund M, Tschanz A, Wu Y-L, Frey FF, Mehl JL, Kaksonen M, Avinoam O, Schwarz US, Ries J. 2023. Clathrin coats partially preassemble and subsequently bend during endocytosis. Journal of Cell Biology. 222(3), e202206038.","mla":"Mund, Markus, et al. “Clathrin Coats Partially Preassemble and Subsequently Bend during Endocytosis.” <i>Journal of Cell Biology</i>, vol. 222, no. 3, e202206038, Rockefeller University Press, 2023, doi:<a href=\"https://doi.org/10.1083/jcb.202206038\">10.1083/jcb.202206038</a>.","apa":"Mund, M., Tschanz, A., Wu, Y.-L., Frey, F. F., Mehl, J. L., Kaksonen, M., … Ries, J. (2023). Clathrin coats partially preassemble and subsequently bend during endocytosis. <i>Journal of Cell Biology</i>. Rockefeller University Press. <a href=\"https://doi.org/10.1083/jcb.202206038\">https://doi.org/10.1083/jcb.202206038</a>","short":"M. Mund, A. Tschanz, Y.-L. Wu, F.F. Frey, J.L. Mehl, M. Kaksonen, O. Avinoam, U.S. Schwarz, J. Ries, Journal of Cell Biology 222 (2023).","chicago":"Mund, Markus, Aline Tschanz, Yu-Le Wu, Felix F Frey, Johanna L. Mehl, Marko Kaksonen, Ori Avinoam, Ulrich S. Schwarz, and Jonas Ries. “Clathrin Coats Partially Preassemble and Subsequently Bend during Endocytosis.” <i>Journal of Cell Biology</i>. Rockefeller University Press, 2023. <a href=\"https://doi.org/10.1083/jcb.202206038\">https://doi.org/10.1083/jcb.202206038</a>.","ama":"Mund M, Tschanz A, Wu Y-L, et al. Clathrin coats partially preassemble and subsequently bend during endocytosis. <i>Journal of Cell Biology</i>. 2023;222(3). doi:<a href=\"https://doi.org/10.1083/jcb.202206038\">10.1083/jcb.202206038</a>"},"volume":222,"doi":"10.1083/jcb.202206038","publisher":"Rockefeller University Press","day":"03","type":"journal_article"},{"month":"12","pmid":1,"article_processing_charge":"No","title":"Plant autophagosomes mature into amphisomes prior to their delivery to the central vacuole","keyword":["Cell Biology"],"oa_version":"Published Version","year":"2022","_id":"12121","issue":"12","oa":1,"file":[{"file_size":10365777,"relation":"main_file","file_id":"12342","creator":"dernst","date_created":"2023-01-23T10:30:11Z","access_level":"open_access","content_type":"application/pdf","file_name":"2022_JCB_Zhao.pdf","date_updated":"2023-01-23T10:30:11Z","checksum":"050b5cc4b25e6b94fe3e3cbfe0f5c06b","success":1}],"user_id":"4359f0d1-fa6c-11eb-b949-802e58b17ae8","isi":1,"author":[{"first_name":"Jierui","full_name":"Zhao, Jierui","last_name":"Zhao"},{"last_name":"Bui","full_name":"Bui, Mai Thu","first_name":"Mai Thu"},{"first_name":"Juncai","full_name":"Ma, Juncai","last_name":"Ma"},{"last_name":"Künzl","first_name":"Fabian","full_name":"Künzl, Fabian"},{"full_name":"Picchianti, Lorenzo","first_name":"Lorenzo","last_name":"Picchianti"},{"full_name":"De La Concepcion, Juan Carlos","first_name":"Juan Carlos","last_name":"De La Concepcion"},{"last_name":"Chen","first_name":"Yixuan","full_name":"Chen, Yixuan"},{"full_name":"Petsangouraki, Sofia","first_name":"Sofia","last_name":"Petsangouraki"},{"first_name":"Azadeh","full_name":"Mohseni, Azadeh","last_name":"Mohseni"},{"last_name":"García-Leon","full_name":"García-Leon, Marta","first_name":"Marta"},{"last_name":"Gomez","full_name":"Gomez, Marta Salas","first_name":"Marta Salas"},{"id":"e3fdddd5-f6e0-11ea-865d-ca99ee6367f4","full_name":"Giannini, Caterina","first_name":"Caterina","last_name":"Giannini"},{"last_name":"Gwennogan","full_name":"Gwennogan, Dubois","first_name":"Dubois"},{"last_name":"Kobylinska","first_name":"Roksolana","full_name":"Kobylinska, Roksolana"},{"last_name":"Clavel","full_name":"Clavel, Marion","first_name":"Marion"},{"last_name":"Schellmann","first_name":"Swen","full_name":"Schellmann, Swen"},{"last_name":"Jaillais","full_name":"Jaillais, Yvon","first_name":"Yvon"},{"full_name":"Friml, Jiří","id":"4159519E-F248-11E8-B48F-1D18A9856A87","first_name":"Jiří","last_name":"Friml","orcid":"0000-0002-8302-7596"},{"last_name":"Kang","first_name":"Byung-Ho","full_name":"Kang, Byung-Ho"},{"last_name":"Dagdas","full_name":"Dagdas, Yasin","first_name":"Yasin"}],"article_type":"original","publication_status":"published","acknowledgement":"We thank Suayip Ustün, Karin Schumacher, Erika Isono, Gerd Juergens, Takashi Ueda, Daniel Hofius, and Liwen Jiang for sharing published materials.\r\nWe acknowledge funding from Austrian Academy of Sciences, Austrian Science Fund (FWF, P 32355, P 34944), Austrian Science Fund (FWF-SFB F79), Vienna Science and Technology\r\nFund (WWTF, LS17-047) to Y. Dagdas; Austrian Academy of Sciences DOC Fellowship to J. Zhao, Marie Curie VIP2 Fellowship to J.C. De La Concepcion and M. Clavel; Hong Kong Research Grant Council (GRF14121019, 14113921, AoE/M-05/12, C4002-17G) to B.-H. Kang. We thank Vienna Biocenter Core Facilities (VBCF) Protein Chemistry, Biooptics, Plant Sciences, Molecular Biology, and Protein Technologies. We thank J. Matthew Watson\r\nand members of the Dagdas lab for the critical reading and editing of the manuscript.","ddc":["580"],"status":"public","date_published":"2022-12-01T00:00:00Z","abstract":[{"text":"Autophagosomes are double-membraned vesicles that traffic harmful or unwanted cellular macromolecules to the vacuole for recycling. Although autophagosome biogenesis has been extensively studied, autophagosome maturation, i.e., delivery and fusion with the vacuole, remains largely unknown in plants. Here, we have identified an autophagy adaptor, CFS1, that directly interacts with the autophagosome marker ATG8 and localizes on both membranes of the autophagosome. Autophagosomes form normally in Arabidopsis thaliana cfs1 mutants, but their delivery to the vacuole is disrupted. CFS1’s function is evolutionarily conserved in plants, as it also localizes to the autophagosomes and plays a role in autophagic flux in the liverwort Marchantia polymorpha. CFS1 regulates autophagic flux by bridging autophagosomes with the multivesicular body-localized ESCRT-I component VPS23A, leading to the formation of amphisomes. Similar to CFS1-ATG8 interaction, disrupting the CFS1-VPS23A interaction blocks autophagic flux and renders plants sensitive to nitrogen starvation. Altogether, our results reveal a conserved vacuolar sorting hub that regulates autophagic flux in plants.","lang":"eng"}],"scopus_import":"1","publication":"Journal of Cell Biology","type":"journal_article","doi":"10.1083/jcb.202203139","publisher":"Rockefeller University Press","day":"01","volume":221,"citation":{"apa":"Zhao, J., Bui, M. T., Ma, J., Künzl, F., Picchianti, L., De La Concepcion, J. C., … Dagdas, Y. (2022). Plant autophagosomes mature into amphisomes prior to their delivery to the central vacuole. <i>Journal of Cell Biology</i>. Rockefeller University Press. <a href=\"https://doi.org/10.1083/jcb.202203139\">https://doi.org/10.1083/jcb.202203139</a>","mla":"Zhao, Jierui, et al. “Plant Autophagosomes Mature into Amphisomes Prior to Their Delivery to the Central Vacuole.” <i>Journal of Cell Biology</i>, vol. 221, no. 12, e202203139, Rockefeller University Press, 2022, doi:<a href=\"https://doi.org/10.1083/jcb.202203139\">10.1083/jcb.202203139</a>.","ista":"Zhao J, Bui MT, Ma J, Künzl F, Picchianti L, De La Concepcion JC, Chen Y, Petsangouraki S, Mohseni A, García-Leon M, Gomez MS, Giannini C, Gwennogan D, Kobylinska R, Clavel M, Schellmann S, Jaillais Y, Friml J, Kang B-H, Dagdas Y. 2022. Plant autophagosomes mature into amphisomes prior to their delivery to the central vacuole. Journal of Cell Biology. 221(12), e202203139.","ieee":"J. Zhao <i>et al.</i>, “Plant autophagosomes mature into amphisomes prior to their delivery to the central vacuole,” <i>Journal of Cell Biology</i>, vol. 221, no. 12. Rockefeller University Press, 2022.","short":"J. Zhao, M.T. Bui, J. Ma, F. Künzl, L. Picchianti, J.C. De La Concepcion, Y. Chen, S. Petsangouraki, A. Mohseni, M. García-Leon, M.S. Gomez, C. Giannini, D. Gwennogan, R. Kobylinska, M. Clavel, S. Schellmann, Y. Jaillais, J. Friml, B.-H. Kang, Y. Dagdas, Journal of Cell Biology 221 (2022).","chicago":"Zhao, Jierui, Mai Thu Bui, Juncai Ma, Fabian Künzl, Lorenzo Picchianti, Juan Carlos De La Concepcion, Yixuan Chen, et al. “Plant Autophagosomes Mature into Amphisomes Prior to Their Delivery to the Central Vacuole.” <i>Journal of Cell Biology</i>. Rockefeller University Press, 2022. <a href=\"https://doi.org/10.1083/jcb.202203139\">https://doi.org/10.1083/jcb.202203139</a>.","ama":"Zhao J, Bui MT, Ma J, et al. Plant autophagosomes mature into amphisomes prior to their delivery to the central vacuole. <i>Journal of Cell Biology</i>. 2022;221(12). doi:<a href=\"https://doi.org/10.1083/jcb.202203139\">10.1083/jcb.202203139</a>"},"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_number":"e202203139","department":[{"_id":"JiFr"}],"file_date_updated":"2023-01-23T10:30:11Z","date_created":"2023-01-12T11:57:10Z","external_id":{"isi":["000932958800001"],"pmid":["36260289"]},"date_updated":"2023-08-03T14:20:15Z","has_accepted_license":"1","publication_identifier":{"eissn":["1540-8140"],"issn":["0021-9525"]},"intvolume":"       221","language":[{"iso":"eng"}],"quality_controlled":"1"},{"volume":221,"citation":{"ama":"Weier A-K, Homrich M, Ebbinghaus S, et al. Multiple centrosomes enhance migration and immune cell effector functions of mature dendritic cells. <i>Journal of Cell Biology</i>. 2022;221(12). doi:<a href=\"https://doi.org/10.1083/jcb.202107134\">10.1083/jcb.202107134</a>","chicago":"Weier, Ann-Kathrin, Mirka Homrich, Stephanie Ebbinghaus, Pavel Juda, Eliška Miková, Robert Hauschild, Lili Zhang, et al. “Multiple Centrosomes Enhance Migration and Immune Cell Effector Functions of Mature Dendritic Cells.” <i>Journal of Cell Biology</i>. Rockefeller University Press, 2022. <a href=\"https://doi.org/10.1083/jcb.202107134\">https://doi.org/10.1083/jcb.202107134</a>.","short":"A.-K. Weier, M. Homrich, S. Ebbinghaus, P. Juda, E. Miková, R. Hauschild, L. Zhang, T. Quast, E. Mass, A. Schlitzer, W. Kolanus, S. Burgdorf, O.J. Gruß, M. Hons, S. Wieser, E. Kiermaier, Journal of Cell Biology 221 (2022).","ista":"Weier A-K, Homrich M, Ebbinghaus S, Juda P, Miková E, Hauschild R, Zhang L, Quast T, Mass E, Schlitzer A, Kolanus W, Burgdorf S, Gruß OJ, Hons M, Wieser S, Kiermaier E. 2022. Multiple centrosomes enhance migration and immune cell effector functions of mature dendritic cells. Journal of Cell Biology. 221(12), e202107134.","apa":"Weier, A.-K., Homrich, M., Ebbinghaus, S., Juda, P., Miková, E., Hauschild, R., … Kiermaier, E. (2022). Multiple centrosomes enhance migration and immune cell effector functions of mature dendritic cells. <i>Journal of Cell Biology</i>. Rockefeller University Press. <a href=\"https://doi.org/10.1083/jcb.202107134\">https://doi.org/10.1083/jcb.202107134</a>","mla":"Weier, Ann-Kathrin, et al. “Multiple Centrosomes Enhance Migration and Immune Cell Effector Functions of Mature Dendritic Cells.” <i>Journal of Cell Biology</i>, vol. 221, no. 12, e202107134, Rockefeller University Press, 2022, doi:<a href=\"https://doi.org/10.1083/jcb.202107134\">10.1083/jcb.202107134</a>.","ieee":"A.-K. Weier <i>et al.</i>, “Multiple centrosomes enhance migration and immune cell effector functions of mature dendritic cells,” <i>Journal of Cell Biology</i>, vol. 221, no. 12. Rockefeller University Press, 2022."},"type":"journal_article","day":"05","publisher":"Rockefeller University Press","doi":"10.1083/jcb.202107134","publication":"Journal of Cell Biology","publication_identifier":{"issn":["0021-9525"],"eissn":["1540-8140"]},"language":[{"iso":"eng"}],"quality_controlled":"1","intvolume":"       221","external_id":{"isi":["000932941400001"],"pmid":["36214847 "]},"has_accepted_license":"1","date_updated":"2025-04-15T08:37:41Z","department":[{"_id":"Bio"}],"article_number":"e202107134","file_date_updated":"2023-08-16T11:24:53Z","date_created":"2023-01-12T12:01:09Z","tmp":{"legal_code_url":"https://creativecommons.org/licenses/by-nc-sa/4.0/legalcode","short":"CC BY-NC-SA (4.0)","image":"/images/cc_by_nc_sa.png","name":"Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)"},"oa_version":"Published Version","_id":"12122","issue":"12","year":"2022","keyword":["Cell Biology"],"title":"Multiple centrosomes enhance migration and immune cell effector functions of mature dendritic cells","article_processing_charge":"No","month":"12","pmid":1,"status":"public","scopus_import":"1","abstract":[{"lang":"eng","text":"Centrosomes play a crucial role during immune cell interactions and initiation of the immune response. In proliferating cells, centrosome numbers are tightly controlled and generally limited to one in G1 and two prior to mitosis. Defects in regulating centrosome numbers have been associated with cell transformation and tumorigenesis. Here, we report the emergence of extra centrosomes in leukocytes during immune activation. Upon antigen encounter, dendritic cells pass through incomplete mitosis and arrest in the subsequent G1 phase leading to tetraploid cells with accumulated centrosomes. In addition, cell stimulation increases expression of polo-like kinase 2, resulting in diploid cells with two centrosomes in G1-arrested cells. During cell migration, centrosomes tightly cluster and act as functional microtubule-organizing centers allowing for increased persistent locomotion along gradients of chemotactic cues. Moreover, dendritic cells with extra centrosomes display enhanced secretion of inflammatory cytokines and optimized T cell responses. Together, these results demonstrate a previously unappreciated role of extra centrosomes for regular cell and tissue homeostasis."}],"date_published":"2022-12-05T00:00:00Z","ddc":["570"],"acknowledgement":"We thank Markéta Dalecká and Irena Krejzová for their support with FIB-SEM imaging, the Imaging Methods Core Facility at BIOCEV supported by the Ministry of Education, Youth and Sports Czech Republic (Large RI Project LM2018129 Czech-BioImaging), and European Regional Development Fund (project No. CZ.02.1.01/0.0/0.0/18_046/0016045) for their support with obtaining imaging data presented in this paper. The authors further thank Andreas Villunger, Florian Gärtner, Frank Bradke, and Sarah Förster for helpful discussions; Andy Zielinski for help with statistics; and Björn Weiershausen for assisting with figure illustration.\r\n\r\nThis work was funded by a fellowship of the Ministry of Innovation, Science and Research of North-Rhine-Westphalia (AZ: 421-8.03.03.02-137069) to E. Kiermaier and the Deutsche Forschungsgemeinschaft (German Research Foundation) under Germany’s Excellence Strategy – EXC 2151 – 390873048. R. Hauschild was funded by grant number 2020-225401 from the Chan Zuckerberg Initiative Donor-Advised Fund, an advised fund of Silicon Valley Community Foundation. M. Hons is supported by Czech Science Foundation GACR 20-24603Y and Charles University PRIMUS/20/MED/013.","author":[{"last_name":"Weier","full_name":"Weier, Ann-Kathrin","first_name":"Ann-Kathrin"},{"full_name":"Homrich, Mirka","first_name":"Mirka","last_name":"Homrich"},{"last_name":"Ebbinghaus","full_name":"Ebbinghaus, Stephanie","first_name":"Stephanie"},{"full_name":"Juda, Pavel","first_name":"Pavel","last_name":"Juda"},{"last_name":"Miková","first_name":"Eliška","full_name":"Miková, Eliška"},{"first_name":"Robert","full_name":"Hauschild, Robert","id":"4E01D6B4-F248-11E8-B48F-1D18A9856A87","orcid":"0000-0001-9843-3522","last_name":"Hauschild"},{"last_name":"Zhang","first_name":"Lili","full_name":"Zhang, Lili"},{"first_name":"Thomas","full_name":"Quast, Thomas","last_name":"Quast"},{"last_name":"Mass","first_name":"Elvira","full_name":"Mass, Elvira"},{"first_name":"Andreas","full_name":"Schlitzer, Andreas","last_name":"Schlitzer"},{"last_name":"Kolanus","first_name":"Waldemar","full_name":"Kolanus, Waldemar"},{"last_name":"Burgdorf","first_name":"Sven","full_name":"Burgdorf, Sven"},{"first_name":"Oliver J.","full_name":"Gruß, Oliver J.","last_name":"Gruß"},{"last_name":"Hons","first_name":"Miroslav","full_name":"Hons, Miroslav"},{"last_name":"Wieser","first_name":"Stefan","full_name":"Wieser, Stefan"},{"last_name":"Kiermaier","full_name":"Kiermaier, Eva","first_name":"Eva"}],"publication_status":"published","article_type":"original","project":[{"name":"Tools for automation and feedback microscopy","_id":"c08e9ad1-5a5b-11eb-8a69-9d1cf3b07473","grant_number":"CZI01"}],"oa":1,"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","isi":1,"file":[{"content_type":"application/pdf","date_created":"2023-08-16T11:24:53Z","creator":"dernst","access_level":"open_access","file_id":"14065","file_size":11090179,"relation":"main_file","success":1,"checksum":"0c9af38f82af30c6ce528f2caece4246","file_name":"2023_JCB_Weier.pdf","date_updated":"2023-08-16T11:24:53Z"}]},{"type":"journal_article","doi":"10.1083/jcb.202112138","day":"19","publisher":"Rockefeller University Press","volume":221,"citation":{"ieee":"M. Enshoji <i>et al.</i>, “Eps15/Pan1p is a master regulator of the late stages of the endocytic pathway,” <i>Journal of Cell Biology</i>, vol. 221, no. 10. Rockefeller University Press, 2022.","ista":"Enshoji M, Miyano Y, Yoshida N, Nagano M, Watanabe M, Kunihiro M, Siekhaus DE, Toshima JY, Toshima J. 2022. Eps15/Pan1p is a master regulator of the late stages of the endocytic pathway. Journal of Cell Biology. 221(10), e202112138.","apa":"Enshoji, M., Miyano, Y., Yoshida, N., Nagano, M., Watanabe, M., Kunihiro, M., … Toshima, J. (2022). Eps15/Pan1p is a master regulator of the late stages of the endocytic pathway. <i>Journal of Cell Biology</i>. Rockefeller University Press. <a href=\"https://doi.org/10.1083/jcb.202112138\">https://doi.org/10.1083/jcb.202112138</a>","mla":"Enshoji, Mariko, et al. “Eps15/Pan1p Is a Master Regulator of the Late Stages of the Endocytic Pathway.” <i>Journal of Cell Biology</i>, vol. 221, no. 10, e202112138, Rockefeller University Press, 2022, doi:<a href=\"https://doi.org/10.1083/jcb.202112138\">10.1083/jcb.202112138</a>.","short":"M. Enshoji, Y. Miyano, N. Yoshida, M. Nagano, M. Watanabe, M. Kunihiro, D.E. Siekhaus, J.Y. Toshima, J. Toshima, Journal of Cell Biology 221 (2022).","chicago":"Enshoji, Mariko, Yoshiko Miyano, Nao Yoshida, Makoto Nagano, Minami Watanabe, Mayumi Kunihiro, Daria E Siekhaus, Junko Y. Toshima, and Jiro Toshima. “Eps15/Pan1p Is a Master Regulator of the Late Stages of the Endocytic Pathway.” <i>Journal of Cell Biology</i>. Rockefeller University Press, 2022. <a href=\"https://doi.org/10.1083/jcb.202112138\">https://doi.org/10.1083/jcb.202112138</a>.","ama":"Enshoji M, Miyano Y, Yoshida N, et al. Eps15/Pan1p is a master regulator of the late stages of the endocytic pathway. <i>Journal of Cell Biology</i>. 2022;221(10). doi:<a href=\"https://doi.org/10.1083/jcb.202112138\">10.1083/jcb.202112138</a>"},"publication":"Journal of Cell Biology","external_id":{"pmid":["35984332"],"isi":["000932770500001"]},"has_accepted_license":"1","date_updated":"2023-08-03T13:49:07Z","publication_identifier":{"eissn":["1540-8140"],"issn":["0021-9525"]},"language":[{"iso":"eng"}],"quality_controlled":"1","intvolume":"       221","tmp":{"legal_code_url":"https://creativecommons.org/licenses/by-nc-sa/4.0/legalcode","short":"CC BY-NC-SA (4.0)","image":"/images/cc_by_nc_sa.png","name":"Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)"},"department":[{"_id":"DaSi"}],"article_number":"e202112138","file_date_updated":"2023-02-21T23:30:39Z","date_created":"2022-09-11T22:01:54Z","title":"Eps15/Pan1p is a master regulator of the late stages of the endocytic pathway","oa_version":"Published Version","issue":"10","_id":"12080","year":"2022","month":"08","pmid":1,"article_processing_charge":"No","ddc":["570"],"acknowledgement":"This work was supported by JSPS KAKENHI GRANT #18K062291, and the Takeda Science Foundation to J.Y. Toshima, as well as JSPS KAKENHI GRANT #19K065710, the Uehara Memorial Foundation, and Life Science Foundation of JAPAN to J. Toshima.","status":"public","date_published":"2022-08-19T00:00:00Z","abstract":[{"text":"Endocytosis is a multistep process involving the sequential recruitment and action of numerous proteins. This process can be divided into two phases: an early phase, in which sites of endocytosis are formed, and a late phase in which clathrin-coated vesicles are formed and internalized into the cytosol, but how these phases link to each other remains unclear. In this study, we demonstrate that anchoring the yeast Eps15-like protein Pan1p to the peroxisome triggers most of the events occurring during the late phase at the peroxisome. At this ectopic location, Pan1p recruits most proteins that function in the late phases—including actin nucleation promoting factors—and then initiates actin polymerization. Pan1p also recruited Prk1 kinase and actin depolymerizing factors, thereby triggering disassembly immediately after actin assembly and inducing dissociation of endocytic proteins from the peroxisome. These observations suggest that Pan1p is a key regulator for initiating, processing, and completing the late phase of endocytosis.","lang":"eng"}],"scopus_import":"1","oa":1,"user_id":"4359f0d1-fa6c-11eb-b949-802e58b17ae8","isi":1,"file":[{"relation":"main_file","file_size":7816875,"file_id":"12321","access_level":"open_access","date_created":"2023-01-20T09:32:53Z","creator":"dernst","content_type":"application/pdf","date_updated":"2023-02-21T23:30:39Z","file_name":"2022_JCB_Enshoji.pdf","embargo":"2023-02-20","checksum":"f2e581e66b5cdab9df81b56e850b3eaa"}],"author":[{"full_name":"Enshoji, Mariko","first_name":"Mariko","last_name":"Enshoji"},{"last_name":"Miyano","full_name":"Miyano, Yoshiko","first_name":"Yoshiko"},{"first_name":"Nao","full_name":"Yoshida, Nao","last_name":"Yoshida"},{"last_name":"Nagano","first_name":"Makoto","full_name":"Nagano, Makoto"},{"last_name":"Watanabe","full_name":"Watanabe, Minami","first_name":"Minami"},{"full_name":"Kunihiro, Mayumi","first_name":"Mayumi","last_name":"Kunihiro"},{"first_name":"Daria E","full_name":"Siekhaus, Daria E","id":"3D224B9E-F248-11E8-B48F-1D18A9856A87","orcid":"0000-0001-8323-8353","last_name":"Siekhaus"},{"last_name":"Toshima","first_name":"Junko Y.","full_name":"Toshima, Junko Y."},{"full_name":"Toshima, Jiro","first_name":"Jiro","last_name":"Toshima"}],"article_type":"original","publication_status":"published"},{"tmp":{"legal_code_url":"https://creativecommons.org/licenses/by-nc-sa/4.0/legalcode","short":"CC BY-NC-SA (4.0)","image":"/images/cc_by_nc_sa.png","name":"Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)"},"article_number":"e202206127","department":[{"_id":"MiSi"}],"file_date_updated":"2023-01-30T10:39:34Z","date_created":"2023-01-16T10:01:08Z","external_id":{"isi":["000874717200001"],"pmid":["35856919"]},"corr_author":"1","date_updated":"2026-05-04T22:30:27Z","has_accepted_license":"1","publication_identifier":{"eissn":["1540-8140"],"issn":["0021-9525"]},"intvolume":"       221","language":[{"iso":"eng"}],"quality_controlled":"1","publication":"Journal of Cell Biology","related_material":{"record":[{"status":"public","id":"14697","relation":"dissertation_contains"}]},"type":"journal_article","day":"20","doi":"10.1083/jcb.202206127","publisher":"Rockefeller University Press","volume":221,"citation":{"chicago":"Stopp, Julian A, and Michael K Sixt. “Plan Your Trip before You Leave: The Neutrophils’ Search-and-Run Journey.” <i>Journal of Cell Biology</i>. Rockefeller University Press, 2022. <a href=\"https://doi.org/10.1083/jcb.202206127\">https://doi.org/10.1083/jcb.202206127</a>.","ama":"Stopp JA, Sixt MK. Plan your trip before you leave: The neutrophils’ search-and-run journey. <i>Journal of Cell Biology</i>. 2022;221(8). doi:<a href=\"https://doi.org/10.1083/jcb.202206127\">10.1083/jcb.202206127</a>","ieee":"J. A. Stopp and M. K. Sixt, “Plan your trip before you leave: The neutrophils’ search-and-run journey,” <i>Journal of Cell Biology</i>, vol. 221, no. 8. Rockefeller University Press, 2022.","apa":"Stopp, J. A., &#38; Sixt, M. K. (2022). Plan your trip before you leave: The neutrophils’ search-and-run journey. <i>Journal of Cell Biology</i>. Rockefeller University Press. <a href=\"https://doi.org/10.1083/jcb.202206127\">https://doi.org/10.1083/jcb.202206127</a>","ista":"Stopp JA, Sixt MK. 2022. Plan your trip before you leave: The neutrophils’ search-and-run journey. Journal of Cell Biology. 221(8), e202206127.","mla":"Stopp, Julian A., and Michael K. Sixt. “Plan Your Trip before You Leave: The Neutrophils’ Search-and-Run Journey.” <i>Journal of Cell Biology</i>, vol. 221, no. 8, e202206127, Rockefeller University Press, 2022, doi:<a href=\"https://doi.org/10.1083/jcb.202206127\">10.1083/jcb.202206127</a>.","short":"J.A. Stopp, M.K. Sixt, Journal of Cell Biology 221 (2022)."},"oa":1,"file":[{"access_level":"open_access","creator":"dernst","date_created":"2023-01-30T10:39:34Z","content_type":"application/pdf","file_size":969969,"relation":"main_file","file_id":"12451","checksum":"6b1620743669679b48b9389bb40f5a11","success":1,"date_updated":"2023-01-30T10:39:34Z","file_name":"2022_JourCellBiology_Stopp.pdf"}],"isi":1,"user_id":"4359f0d1-fa6c-11eb-b949-802e58b17ae8","author":[{"first_name":"Julian A","full_name":"Stopp, Julian A","id":"489E3F00-F248-11E8-B48F-1D18A9856A87","last_name":"Stopp"},{"first_name":"Michael K","full_name":"Sixt, Michael K","id":"41E9FBEA-F248-11E8-B48F-1D18A9856A87","orcid":"0000-0002-6620-9179","last_name":"Sixt"}],"article_type":"original","publication_status":"published","ddc":["570"],"status":"public","scopus_import":"1","date_published":"2022-07-20T00:00:00Z","abstract":[{"lang":"eng","text":"Reading, interpreting and crawling along gradients of chemotactic cues is one of the most complex questions in cell biology. In this issue, Georgantzoglou et al. (2022. J. Cell. Biol.https://doi.org/10.1083/jcb.202103207) use in vivo models to map the temporal sequence of how neutrophils respond to an acutely arising gradient of chemoattractant."}],"month":"07","pmid":1,"article_processing_charge":"No","title":"Plan your trip before you leave: The neutrophils’ search-and-run journey","keyword":["Cell Biology"],"oa_version":"Published Version","year":"2022","issue":"8","_id":"12272"},{"title":"PLCγ1 promotes phase separation of T cell signaling components","keyword":["cell biology"],"oa_version":"None","year":"2021","_id":"10337","issue":"6","month":"04","pmid":1,"article_processing_charge":"No","acknowledgement":"Charles H. Hood Foundation (NO AWARD) ; Rally Foundation (NO AWARD)","status":"public","abstract":[{"lang":"eng","text":"The T cell receptor (TCR) pathway receives, processes, and amplifies the signal from pathogenic antigens to the activation of T cells. Although major components in this pathway have been identified, the knowledge on how individual components cooperate to effectively transduce signals remains limited. Phase separation emerges as a biophysical principle in organizing signaling molecules into liquid-like condensates. Here, we report that phospholipase Cγ1 (PLCγ1) promotes phase separation of LAT, a key adaptor protein in the TCR pathway. PLCγ1 directly cross-links LAT through its two SH2 domains. PLCγ1 also protects LAT from dephosphorylation by the phosphatase CD45 and promotes LAT-dependent ERK activation and SLP76 phosphorylation. Intriguingly, a nonmonotonic effect of PLCγ1 on LAT clustering was discovered. Computer simulations, based on patchy particles, revealed how the cluster size is regulated by protein compositions. Together, these results define a critical function of PLCγ1 in promoting phase separation of the LAT complex and TCR signal transduction."}],"scopus_import":"1","date_published":"2021-04-30T00:00:00Z","user_id":"8b945eb4-e2f2-11eb-945a-df72226e66a9","author":[{"full_name":"Zeng, Longhui","first_name":"Longhui","last_name":"Zeng"},{"last_name":"Palaia","first_name":"Ivan","full_name":"Palaia, Ivan"},{"last_name":"Šarić","orcid":"0000-0002-7854-2139","full_name":"Šarić, Anđela","id":"bf63d406-f056-11eb-b41d-f263a6566d8b","first_name":"Anđela"},{"full_name":"Su, Xiaolei","first_name":"Xiaolei","last_name":"Su"}],"publication_status":"published","article_type":"original","type":"journal_article","publisher":"Rockefeller University Press","doi":"10.1083/jcb.202009154","day":"30","volume":220,"citation":{"short":"L. Zeng, I. Palaia, A. Šarić, X. Su, Journal of Cell Biology 220 (2021).","ieee":"L. Zeng, I. Palaia, A. Šarić, and X. Su, “PLCγ1 promotes phase separation of T cell signaling components,” <i>Journal of Cell Biology</i>, vol. 220, no. 6. Rockefeller University Press, 2021.","mla":"Zeng, Longhui, et al. “PLCγ1 Promotes Phase Separation of T Cell Signaling Components.” <i>Journal of Cell Biology</i>, vol. 220, no. 6, e202009154, Rockefeller University Press, 2021, doi:<a href=\"https://doi.org/10.1083/jcb.202009154\">10.1083/jcb.202009154</a>.","ista":"Zeng L, Palaia I, Šarić A, Su X. 2021. PLCγ1 promotes phase separation of T cell signaling components. Journal of Cell Biology. 220(6), e202009154.","apa":"Zeng, L., Palaia, I., Šarić, A., &#38; Su, X. (2021). PLCγ1 promotes phase separation of T cell signaling components. <i>Journal of Cell Biology</i>. Rockefeller University Press. <a href=\"https://doi.org/10.1083/jcb.202009154\">https://doi.org/10.1083/jcb.202009154</a>","ama":"Zeng L, Palaia I, Šarić A, Su X. PLCγ1 promotes phase separation of T cell signaling components. <i>Journal of Cell Biology</i>. 2021;220(6). doi:<a href=\"https://doi.org/10.1083/jcb.202009154\">10.1083/jcb.202009154</a>","chicago":"Zeng, Longhui, Ivan Palaia, Anđela Šarić, and Xiaolei Su. “PLCγ1 Promotes Phase Separation of T Cell Signaling Components.” <i>Journal of Cell Biology</i>. Rockefeller University Press, 2021. <a href=\"https://doi.org/10.1083/jcb.202009154\">https://doi.org/10.1083/jcb.202009154</a>."},"extern":"1","publication":"Journal of Cell Biology","external_id":{"pmid":["33929486"]},"date_updated":"2021-11-25T15:33:08Z","publication_identifier":{"issn":["0021-9525"],"eissn":["1540-8140"]},"intvolume":"       220","language":[{"iso":"eng"}],"quality_controlled":"1","tmp":{"legal_code_url":"https://creativecommons.org/licenses/by-nc-sa/4.0/legalcode","short":"CC BY-NC-SA (4.0)","image":"/images/cc_by_nc_sa.png","name":"Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)"},"article_number":"e202009154","date_created":"2021-11-25T15:21:30Z"},{"file_date_updated":"2022-05-12T14:16:21Z","date_created":"2021-02-05T10:08:04Z","department":[{"_id":"MiSi"}],"article_number":"e202006081","tmp":{"legal_code_url":"https://creativecommons.org/licenses/by-nc-sa/4.0/legalcode","short":"CC BY-NC-SA (4.0)","image":"/images/cc_by_nc_sa.png","name":"Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)"},"quality_controlled":"1","language":[{"iso":"eng"}],"intvolume":"       220","publication_identifier":{"eissn":["1540-8140"],"issn":["0021-9525"]},"has_accepted_license":"1","date_updated":"2024-10-09T21:00:23Z","corr_author":"1","external_id":{"isi":["000626365700001"],"pmid":["33533935"]},"publication":"Journal of Cell Biology","citation":{"ama":"Leithner AF, Altenburger L, Hauschild R, et al. Dendritic cell actin dynamics control contact duration and priming efficiency at the immunological synapse. <i>Journal of Cell Biology</i>. 2021;220(4). doi:<a href=\"https://doi.org/10.1083/jcb.202006081\">10.1083/jcb.202006081</a>","chicago":"Leithner, Alexander F, LM Altenburger, R Hauschild, Frank P Assen, K Rottner, Stradal TEB, A Diz-Muñoz, JV Stein, and Michael K Sixt. “Dendritic Cell Actin Dynamics Control Contact Duration and Priming Efficiency at the Immunological Synapse.” <i>Journal of Cell Biology</i>. Rockefeller University Press, 2021. <a href=\"https://doi.org/10.1083/jcb.202006081\">https://doi.org/10.1083/jcb.202006081</a>.","short":"A.F. Leithner, L. Altenburger, R. Hauschild, F.P. Assen, K. Rottner, S. TEB, A. Diz-Muñoz, J. Stein, M.K. Sixt, Journal of Cell Biology 220 (2021).","ieee":"A. F. Leithner <i>et al.</i>, “Dendritic cell actin dynamics control contact duration and priming efficiency at the immunological synapse,” <i>Journal of Cell Biology</i>, vol. 220, no. 4. Rockefeller University Press, 2021.","mla":"Leithner, Alexander F., et al. “Dendritic Cell Actin Dynamics Control Contact Duration and Priming Efficiency at the Immunological Synapse.” <i>Journal of Cell Biology</i>, vol. 220, no. 4, e202006081, Rockefeller University Press, 2021, doi:<a href=\"https://doi.org/10.1083/jcb.202006081\">10.1083/jcb.202006081</a>.","ista":"Leithner AF, Altenburger L, Hauschild R, Assen FP, Rottner K, TEB S, Diz-Muñoz A, Stein J, Sixt MK. 2021. Dendritic cell actin dynamics control contact duration and priming efficiency at the immunological synapse. Journal of Cell Biology. 220(4), e202006081.","apa":"Leithner, A. F., Altenburger, L., Hauschild, R., Assen, F. P., Rottner, K., TEB, S., … Sixt, M. K. (2021). Dendritic cell actin dynamics control contact duration and priming efficiency at the immunological synapse. <i>Journal of Cell Biology</i>. Rockefeller University Press. <a href=\"https://doi.org/10.1083/jcb.202006081\">https://doi.org/10.1083/jcb.202006081</a>"},"volume":220,"day":"05","doi":"10.1083/jcb.202006081","publisher":"Rockefeller University Press","type":"journal_article","publication_status":"published","article_type":"original","author":[{"orcid":"0000-0002-1073-744X","last_name":"Leithner","first_name":"Alexander F","id":"3B1B77E4-F248-11E8-B48F-1D18A9856A87","full_name":"Leithner, Alexander F"},{"first_name":"LM","full_name":"Altenburger, LM","last_name":"Altenburger"},{"full_name":"Hauschild, R","first_name":"R","last_name":"Hauschild"},{"orcid":"0000-0003-3470-6119","last_name":"Assen","full_name":"Assen, Frank P","id":"3A8E7F24-F248-11E8-B48F-1D18A9856A87","first_name":"Frank P"},{"first_name":"K","full_name":"Rottner, K","last_name":"Rottner"},{"last_name":"TEB","first_name":"Stradal","full_name":"TEB, Stradal"},{"last_name":"Diz-Muñoz","first_name":"A","full_name":"Diz-Muñoz, A"},{"first_name":"JV","full_name":"Stein, JV","last_name":"Stein"},{"orcid":"0000-0002-6620-9179","last_name":"Sixt","first_name":"Michael K","full_name":"Sixt, Michael K","id":"41E9FBEA-F248-11E8-B48F-1D18A9856A87"}],"isi":1,"user_id":"c635000d-4b10-11ee-a964-aac5a93f6ac1","file":[{"relation":"main_file","file_size":5102328,"file_id":"11367","access_level":"open_access","creator":"dernst","date_created":"2022-05-12T14:16:21Z","content_type":"application/pdf","date_updated":"2022-05-12T14:16:21Z","file_name":"2021_JournCellBiology_Leithner.pdf","checksum":"843ebc153847c8626e13c9c5ce71d533","success":1}],"oa":1,"date_published":"2021-04-05T00:00:00Z","abstract":[{"text":"Dendritic cells (DCs) are crucial for the priming of naive T cells and the initiation of adaptive immunity. Priming is initiated at a heterologous cell–cell contact, the immunological synapse (IS). While it is established that F-actin dynamics regulates signaling at the T cell side of the contact, little is known about the cytoskeletal contribution on the DC side. Here, we show that the DC actin cytoskeleton is decisive for the formation of a multifocal synaptic structure, which correlates with T cell priming efficiency. DC actin at the IS appears in transient foci that are dynamized by the WAVE regulatory complex (WRC). The absence of the WRC in DCs leads to stabilized contacts with T cells, caused by an increase in ICAM1-integrin–mediated cell–cell adhesion. This results in lower numbers of activated and proliferating T cells, demonstrating an important role for DC actin in the regulation of immune synapse functionality.","lang":"eng"}],"scopus_import":"1","status":"public","ddc":["570"],"article_processing_charge":"No","pmid":1,"month":"04","_id":"9094","issue":"4","year":"2021","oa_version":"Published Version","title":"Dendritic cell actin dynamics control contact duration and priming efficiency at the immunological synapse"},{"volume":220,"citation":{"chicago":"Dobramysl, Ulrich, Iris Katharina Jarsch, Yoshiko Inoue, Hanae Shimo, Benjamin Richier, Jonathan R. Gadsby, Julia Mason, et al. “Stochastic Combinations of Actin Regulatory Proteins Are Sufficient to Drive Filopodia Formation.” <i>Journal of Cell Biology</i>. Rockefeller University Press, 2021. <a href=\"https://doi.org/10.1083/jcb.202003052\">https://doi.org/10.1083/jcb.202003052</a>.","ama":"Dobramysl U, Jarsch IK, Inoue Y, et al. Stochastic combinations of actin regulatory proteins are sufficient to drive filopodia formation. <i>Journal of Cell Biology</i>. 2021;220(4). doi:<a href=\"https://doi.org/10.1083/jcb.202003052\">10.1083/jcb.202003052</a>","ieee":"U. Dobramysl <i>et al.</i>, “Stochastic combinations of actin regulatory proteins are sufficient to drive filopodia formation,” <i>Journal of Cell Biology</i>, vol. 220, no. 4. Rockefeller University Press, 2021.","apa":"Dobramysl, U., Jarsch, I. K., Inoue, Y., Shimo, H., Richier, B., Gadsby, J. R., … Gallop, J. L. (2021). Stochastic combinations of actin regulatory proteins are sufficient to drive filopodia formation. <i>Journal of Cell Biology</i>. Rockefeller University Press. <a href=\"https://doi.org/10.1083/jcb.202003052\">https://doi.org/10.1083/jcb.202003052</a>","ista":"Dobramysl U, Jarsch IK, Inoue Y, Shimo H, Richier B, Gadsby JR, Mason J, Szałapak A, Ioannou PS, Correia GP, Walrant A, Butler R, Hannezo EB, Simons BD, Gallop JL. 2021. Stochastic combinations of actin regulatory proteins are sufficient to drive filopodia formation. Journal of Cell Biology. 220(4), e202003052.","mla":"Dobramysl, Ulrich, et al. “Stochastic Combinations of Actin Regulatory Proteins Are Sufficient to Drive Filopodia Formation.” <i>Journal of Cell Biology</i>, vol. 220, no. 4, e202003052, Rockefeller University Press, 2021, doi:<a href=\"https://doi.org/10.1083/jcb.202003052\">10.1083/jcb.202003052</a>.","short":"U. Dobramysl, I.K. Jarsch, Y. Inoue, H. Shimo, B. Richier, J.R. Gadsby, J. Mason, A. Szałapak, P.S. Ioannou, G.P. Correia, A. Walrant, R. Butler, E.B. Hannezo, B.D. Simons, J.L. Gallop, Journal of Cell Biology 220 (2021)."},"type":"journal_article","publisher":"Rockefeller University Press","doi":"10.1083/jcb.202003052","day":"19","publication":"Journal of Cell Biology","publication_identifier":{"eissn":["1540-8140"]},"intvolume":"       220","quality_controlled":"1","language":[{"iso":"eng"}],"external_id":{"isi":["000663160600002"],"pmid":["33740033"]},"date_updated":"2026-04-02T13:59:43Z","has_accepted_license":"1","article_number":"e202003052","department":[{"_id":"EdHa"}],"date_created":"2021-04-04T22:01:21Z","file_date_updated":"2021-04-06T10:39:08Z","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)"},"oa_version":"Published Version","year":"2021","_id":"9306","issue":"4","title":"Stochastic combinations of actin regulatory proteins are sufficient to drive filopodia formation","article_processing_charge":"No","month":"03","pmid":1,"status":"public","date_published":"2021-03-19T00:00:00Z","abstract":[{"text":"Assemblies of actin and its regulators underlie the dynamic morphology of all eukaryotic cells. To understand how actin regulatory proteins work together to generate actin-rich structures such as filopodia, we analyzed the localization of diverse actin regulators within filopodia in Drosophila embryos and in a complementary in vitro system of filopodia-like structures (FLSs). We found that the composition of the regulatory protein complex where actin is incorporated (the filopodial tip complex) is remarkably heterogeneous both in vivo and in vitro. Our data reveal that different pairs of proteins correlate with each other and with actin bundle length, suggesting the presence of functional subcomplexes. This is consistent with a theoretical framework where three or more redundant subcomplexes join the tip complex stochastically, with any two being sufficient to drive filopodia formation. We provide an explanation for the observed heterogeneity and suggest that a mechanism based on multiple components allows stereotypical filopodial dynamics to arise from diverse upstream signaling pathways.","lang":"eng"}],"scopus_import":"1","acknowledgement":"This work was supported by European Research Council grant 281971, Wellcome Trust Research Career Development Fellowship WT095829AIA and Wellcome Trust Senior Research\r\nFellowship 219482/Z/19/Z to J.L. Gallop, a Wellcome Trust Senior Investigator Award 098357 to B.D. Simons, and an Austrian Science Fund grant (P31639) to E. Hannezo. We acknowledge\r\ncore funding by the Wellcome Trust (092096) and Cancer Research UK (C6946/A14492). U. Dobramysl was supported by a Wellcome Trust Junior Interdisciplinary Fellowship grant\r\n(105602/Z/14/Z) and a Herchel Smith Postdoctoral Fellowship. H. Shimo was supported by a Funai Foundation Overseas scholarship.","ddc":["576"],"author":[{"full_name":"Dobramysl, Ulrich","first_name":"Ulrich","last_name":"Dobramysl"},{"last_name":"Jarsch","full_name":"Jarsch, Iris Katharina","first_name":"Iris Katharina"},{"full_name":"Inoue, Yoshiko","first_name":"Yoshiko","last_name":"Inoue"},{"first_name":"Hanae","full_name":"Shimo, Hanae","last_name":"Shimo"},{"last_name":"Richier","full_name":"Richier, Benjamin","first_name":"Benjamin"},{"last_name":"Gadsby","first_name":"Jonathan R.","full_name":"Gadsby, Jonathan R."},{"last_name":"Mason","first_name":"Julia","full_name":"Mason, Julia"},{"last_name":"Szałapak","full_name":"Szałapak, Alicja","first_name":"Alicja"},{"full_name":"Ioannou, Pantelis Savvas","first_name":"Pantelis Savvas","last_name":"Ioannou"},{"full_name":"Correia, Guilherme Pereira","first_name":"Guilherme Pereira","last_name":"Correia"},{"first_name":"Astrid","full_name":"Walrant, Astrid","last_name":"Walrant"},{"full_name":"Butler, Richard","first_name":"Richard","last_name":"Butler"},{"last_name":"Hannezo","orcid":"0000-0001-6005-1561","id":"3A9DB764-F248-11E8-B48F-1D18A9856A87","full_name":"Hannezo, Edouard B","first_name":"Edouard B"},{"full_name":"Simons, Benjamin D.","first_name":"Benjamin D.","last_name":"Simons"},{"first_name":"Jennifer L.","full_name":"Gallop, Jennifer L.","last_name":"Gallop"}],"project":[{"name":"Active mechano-chemical description of the cell cytoskeleton","call_identifier":"FWF","_id":"268294B6-B435-11E9-9278-68D0E5697425","grant_number":"P31639"}],"publication_status":"published","article_type":"original","oa":1,"file":[{"date_updated":"2021-04-06T10:39:08Z","file_name":"2021_JCB_Dobramysl.pdf","checksum":"4739ffd90f2c7e05ac5b00f057c58aa2","success":1,"file_size":9019720,"relation":"main_file","file_id":"9310","access_level":"open_access","creator":"dernst","date_created":"2021-04-06T10:39:08Z","content_type":"application/pdf"}],"isi":1,"user_id":"ba8df636-2132-11f1-aed0-ed93e2281fdd"},{"user_id":"4359f0d1-fa6c-11eb-b949-802e58b17ae8","isi":1,"file":[{"creator":"dernst","date_created":"2020-11-24T13:25:13Z","access_level":"open_access","content_type":"application/pdf","relation":"main_file","file_size":7536712,"file_id":"8801","checksum":"cb0b9c77842ae1214caade7b77e4d82d","success":1,"file_name":"2020_JCellBiol_Kopf.pdf","date_updated":"2020-11-24T13:25:13Z"}],"oa":1,"publication_status":"published","article_type":"original","project":[{"_id":"25A603A2-B435-11E9-9278-68D0E5697425","grant_number":"281556","name":"Cytoskeletal force generation and force transduction of migrating leukocytes","call_identifier":"FP7"},{"call_identifier":"H2020","name":"Cellular Navigation Along Spatial Gradients","grant_number":"724373","_id":"25FE9508-B435-11E9-9278-68D0E5697425"},{"_id":"26018E70-B435-11E9-9278-68D0E5697425","grant_number":"P29911","name":"Mechanical adaptation of lamellipodial actin","call_identifier":"FWF"},{"name":"Nano-Analytics of Cellular Systems","call_identifier":"FWF","_id":"252C3B08-B435-11E9-9278-68D0E5697425","grant_number":"W1250-B20"},{"call_identifier":"FP7","name":"International IST Postdoc Fellowship Programme","grant_number":"291734","_id":"25681D80-B435-11E9-9278-68D0E5697425"},{"name":"Molecular and system level view of immune cell migration","grant_number":"ALTF 1396-2014","_id":"25A48D24-B435-11E9-9278-68D0E5697425"}],"author":[{"id":"31DAC7B6-F248-11E8-B48F-1D18A9856A87","full_name":"Kopf, Aglaja","first_name":"Aglaja","last_name":"Kopf","orcid":"0000-0002-2187-6656"},{"orcid":"0000-0003-2856-3369","last_name":"Renkawitz","first_name":"Jörg","id":"3F0587C8-F248-11E8-B48F-1D18A9856A87","full_name":"Renkawitz, Jörg"},{"orcid":"0000-0001-9843-3522","last_name":"Hauschild","first_name":"Robert","full_name":"Hauschild, Robert","id":"4E01D6B4-F248-11E8-B48F-1D18A9856A87"},{"first_name":"Irute","full_name":"Girkontaite, Irute","last_name":"Girkontaite"},{"last_name":"Tedford","full_name":"Tedford, Kerry","first_name":"Kerry"},{"first_name":"Jack","full_name":"Merrin, Jack","id":"4515C308-F248-11E8-B48F-1D18A9856A87","last_name":"Merrin","orcid":"0000-0001-5145-4609"},{"last_name":"Thorn-Seshold","full_name":"Thorn-Seshold, Oliver","first_name":"Oliver"},{"last_name":"Trauner","full_name":"Trauner, Dirk","id":"E8F27F48-3EBA-11E9-92A1-B709E6697425","first_name":"Dirk"},{"last_name":"Häcker","full_name":"Häcker, Hans","first_name":"Hans"},{"first_name":"Klaus Dieter","full_name":"Fischer, Klaus Dieter","last_name":"Fischer"},{"last_name":"Kiermaier","orcid":"0000-0001-6165-5738","first_name":"Eva","full_name":"Kiermaier, Eva","id":"3EB04B78-F248-11E8-B48F-1D18A9856A87"},{"full_name":"Sixt, Michael K","id":"41E9FBEA-F248-11E8-B48F-1D18A9856A87","first_name":"Michael K","last_name":"Sixt","orcid":"0000-0002-6620-9179"}],"ddc":["570"],"acknowledgement":"The authors thank the Scientific Service Units (Life Sciences, Bioimaging, Preclinical) of the Institute of Science and Technology Austria for excellent support. This work was funded by the European Research Council (ERC StG 281556 and CoG 724373), two grants from the Austrian\r\nScience Fund (FWF; P29911 and DK Nanocell W1250-B20 to M. Sixt) and by the German Research Foundation (DFG SFB1032 project B09) to O. Thorn-Seshold and D. Trauner. J. Renkawitz was supported by ISTFELLOW funding from the People Program (Marie Curie Actions) of the European Union’s Seventh Framework Programme (FP7/2007-2013) under the Research Executive Agency grant agreement (291734) and a European Molecular Biology Organization long-term fellowship (ALTF 1396-2014) co-funded by the European Commission (LTFCOFUND2013, GA-2013-609409), E. Kiermaier by the Deutsche Forschungsgemeinschaft (DFG, German Research Foundation) under Germany’s Excellence Strategy—EXC 2151—390873048, and H. Hacker by the American Lebanese Syrian Associated ¨Charities. K.-D. Fischer was supported by the Analysis, Imaging and Modelling of Neuronal and Inflammatory Processes graduate school funded by the Ministry of Economics, Science, and Digitisation of the State Saxony-Anhalt and by the European Funds for Social and Regional Development.","abstract":[{"lang":"eng","text":"Cells navigating through complex tissues face a fundamental challenge: while multiple protrusions explore different paths, the cell needs to avoid entanglement. How a cell surveys and then corrects its own shape is poorly understood. Here, we demonstrate that spatially distinct microtubule dynamics regulate amoeboid cell migration by locally promoting the retraction of protrusions. In migrating dendritic cells, local microtubule depolymerization within protrusions remote from the microtubule organizing center triggers actomyosin contractility controlled by RhoA and its exchange factor Lfc. Depletion of Lfc leads to aberrant myosin localization, thereby causing two effects that rate-limit locomotion: (1) impaired cell edge coordination during path finding and (2) defective adhesion resolution. Compromised shape control is particularly hindering in geometrically complex microenvironments, where it leads to entanglement and ultimately fragmentation of the cell body. We thus demonstrate that microtubules can act as a proprioceptive device: they sense cell shape and control actomyosin retraction to sustain cellular coherence."}],"scopus_import":"1","date_published":"2020-06-01T00:00:00Z","status":"public","pmid":1,"month":"06","article_processing_charge":"No","title":"Microtubules control cellular shape and coherence in amoeboid migrating cells","issue":"6","_id":"7875","year":"2020","oa_version":"Published Version","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)"},"acknowledged_ssus":[{"_id":"LifeSc"},{"_id":"Bio"},{"_id":"PreCl"}],"file_date_updated":"2020-11-24T13:25:13Z","date_created":"2020-05-24T22:00:56Z","department":[{"_id":"MiSi"},{"_id":"Bio"},{"_id":"NanoFab"}],"article_number":"e201907154","has_accepted_license":"1","date_updated":"2025-04-14T13:10:03Z","corr_author":"1","external_id":{"isi":["000538141100020"],"pmid":["32379884"]},"quality_controlled":"1","language":[{"iso":"eng"}],"intvolume":"       219","publication_identifier":{"eissn":["1540-8140"]},"publication":"The Journal of Cell Biology","publisher":"Rockefeller University Press","day":"01","doi":"10.1083/jcb.201907154","type":"journal_article","ec_funded":1,"citation":{"chicago":"Kopf, Aglaja, Jörg Renkawitz, Robert Hauschild, Irute Girkontaite, Kerry Tedford, Jack Merrin, Oliver Thorn-Seshold, et al. “Microtubules Control Cellular Shape and Coherence in Amoeboid Migrating Cells.” <i>The Journal of Cell Biology</i>. Rockefeller University Press, 2020. <a href=\"https://doi.org/10.1083/jcb.201907154\">https://doi.org/10.1083/jcb.201907154</a>.","ama":"Kopf A, Renkawitz J, Hauschild R, et al. Microtubules control cellular shape and coherence in amoeboid migrating cells. <i>The Journal of Cell Biology</i>. 2020;219(6). doi:<a href=\"https://doi.org/10.1083/jcb.201907154\">10.1083/jcb.201907154</a>","mla":"Kopf, Aglaja, et al. “Microtubules Control Cellular Shape and Coherence in Amoeboid Migrating Cells.” <i>The Journal of Cell Biology</i>, vol. 219, no. 6, e201907154, Rockefeller University Press, 2020, doi:<a href=\"https://doi.org/10.1083/jcb.201907154\">10.1083/jcb.201907154</a>.","ista":"Kopf A, Renkawitz J, Hauschild R, Girkontaite I, Tedford K, Merrin J, Thorn-Seshold O, Trauner D, Häcker H, Fischer KD, Kiermaier E, Sixt MK. 2020. Microtubules control cellular shape and coherence in amoeboid migrating cells. The Journal of Cell Biology. 219(6), e201907154.","apa":"Kopf, A., Renkawitz, J., Hauschild, R., Girkontaite, I., Tedford, K., Merrin, J., … Sixt, M. K. (2020). Microtubules control cellular shape and coherence in amoeboid migrating cells. <i>The Journal of Cell Biology</i>. Rockefeller University Press. <a href=\"https://doi.org/10.1083/jcb.201907154\">https://doi.org/10.1083/jcb.201907154</a>","ieee":"A. Kopf <i>et al.</i>, “Microtubules control cellular shape and coherence in amoeboid migrating cells,” <i>The Journal of Cell Biology</i>, vol. 219, no. 6. Rockefeller University Press, 2020.","short":"A. Kopf, J. Renkawitz, R. Hauschild, I. Girkontaite, K. Tedford, J. Merrin, O. Thorn-Seshold, D. Trauner, H. Häcker, K.D. Fischer, E. Kiermaier, M.K. Sixt, The Journal of Cell Biology 219 (2020)."},"volume":219},{"article_type":"letter_note","publication_status":"published","author":[{"first_name":"Michael K","full_name":"Sixt, Michael K","id":"41E9FBEA-F248-11E8-B48F-1D18A9856A87","orcid":"0000-0002-6620-9179","last_name":"Sixt"},{"full_name":"Huttenlocher, Anna","first_name":"Anna","last_name":"Huttenlocher"}],"isi":1,"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","file":[{"date_created":"2020-08-04T13:11:52Z","creator":"dernst","access_level":"open_access","content_type":"application/pdf","relation":"main_file","file_size":830725,"file_id":"8200","checksum":"30016d778d266b8e17d01094917873b8","file_name":"2020_JCB_Sixt.pdf","date_updated":"2021-02-02T23:30:03Z","embargo":"2021-02-01"}],"oa":1,"date_published":"2020-07-22T00:00:00Z","scopus_import":"1","status":"public","ddc":["570"],"article_processing_charge":"No","pmid":1,"month":"07","issue":"8","_id":"8190","year":"2020","oa_version":"Published Version","title":"Zena Werb (1945-2020): Cell biology in context","file_date_updated":"2021-02-02T23:30:03Z","date_created":"2020-08-02T22:00:57Z","department":[{"_id":"MiSi"}],"article_number":"e202007029","tmp":{"legal_code_url":"https://creativecommons.org/licenses/by-nc-sa/4.0/legalcode","short":"CC BY-NC-SA (4.0)","image":"/images/cc_by_nc_sa.png","name":"Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)"},"language":[{"iso":"eng"}],"intvolume":"       219","publication_identifier":{"eissn":["1540-8140"]},"has_accepted_license":"1","date_updated":"2025-06-12T07:34:40Z","external_id":{"isi":["000573631000004"],"pmid":["32699885"]},"publication":"The Journal of Cell Biology","citation":{"mla":"Sixt, Michael K., and Anna Huttenlocher. “Zena Werb (1945-2020): Cell Biology in Context.” <i>The Journal of Cell Biology</i>, vol. 219, no. 8, e202007029, Rockefeller University Press, 2020, doi:<a href=\"https://doi.org/10.1083/jcb.202007029\">10.1083/jcb.202007029</a>.","ista":"Sixt MK, Huttenlocher A. 2020. Zena Werb (1945-2020): Cell biology in context. The Journal of Cell Biology. 219(8), e202007029.","apa":"Sixt, M. K., &#38; Huttenlocher, A. (2020). Zena Werb (1945-2020): Cell biology in context. <i>The Journal of Cell Biology</i>. Rockefeller University Press. <a href=\"https://doi.org/10.1083/jcb.202007029\">https://doi.org/10.1083/jcb.202007029</a>","ieee":"M. K. Sixt and A. Huttenlocher, “Zena Werb (1945-2020): Cell biology in context,” <i>The Journal of Cell Biology</i>, vol. 219, no. 8. Rockefeller University Press, 2020.","short":"M.K. Sixt, A. Huttenlocher, The Journal of Cell Biology 219 (2020).","chicago":"Sixt, Michael K, and Anna Huttenlocher. “Zena Werb (1945-2020): Cell Biology in Context.” <i>The Journal of Cell Biology</i>. Rockefeller University Press, 2020. <a href=\"https://doi.org/10.1083/jcb.202007029\">https://doi.org/10.1083/jcb.202007029</a>.","ama":"Sixt MK, Huttenlocher A. Zena Werb (1945-2020): Cell biology in context. <i>The Journal of Cell Biology</i>. 2020;219(8). doi:<a href=\"https://doi.org/10.1083/jcb.202007029\">10.1083/jcb.202007029</a>"},"volume":219,"doi":"10.1083/jcb.202007029","publisher":"Rockefeller University Press","day":"22","type":"journal_article"},{"article_processing_charge":"No","pmid":1,"month":"02","_id":"11061","issue":"2","year":"2019","oa_version":"Published Version","keyword":["Cell Biology"],"title":"Visualization of long-lived proteins reveals age mosaicism within nuclei of postmitotic cells","article_type":"original","publication_status":"published","author":[{"full_name":"Toyama, Brandon H.","first_name":"Brandon H.","last_name":"Toyama"},{"first_name":"Rafael","full_name":"Arrojo e Drigo, Rafael","last_name":"Arrojo e Drigo"},{"last_name":"Lev-Ram","full_name":"Lev-Ram, Varda","first_name":"Varda"},{"first_name":"Ranjan","full_name":"Ramachandra, Ranjan","last_name":"Ramachandra"},{"last_name":"Deerinck","full_name":"Deerinck, Thomas J.","first_name":"Thomas J."},{"last_name":"Lechene","full_name":"Lechene, Claude","first_name":"Claude"},{"last_name":"Ellisman","first_name":"Mark H.","full_name":"Ellisman, Mark H."},{"last_name":"HETZER","orcid":"0000-0002-2111-992X","full_name":"HETZER, Martin W","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","first_name":"Martin W"}],"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","file":[{"access_level":"open_access","date_created":"2022-04-08T08:26:32Z","creator":"dernst","content_type":"application/pdf","relation":"main_file","file_size":2503838,"file_id":"11139","checksum":"7964ebbf833b0b35f9fba840eea9531d","success":1,"date_updated":"2022-04-08T08:26:32Z","file_name":"2019_JCB_Toyama.pdf"}],"oa":1,"scopus_import":"1","abstract":[{"lang":"eng","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."}],"date_published":"2019-02-04T00:00:00Z","status":"public","ddc":["570"],"publication":"Journal of Cell Biology","extern":"1","citation":{"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.” <i>Journal of Cell Biology</i>. Rockefeller University Press, 2019. <a href=\"https://doi.org/10.1083/jcb.201809123\">https://doi.org/10.1083/jcb.201809123</a>.","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. <i>Journal of Cell Biology</i>. 2019;218(2):433-444. doi:<a href=\"https://doi.org/10.1083/jcb.201809123\">10.1083/jcb.201809123</a>","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.","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. <i>Journal of Cell Biology</i>. Rockefeller University Press. <a href=\"https://doi.org/10.1083/jcb.201809123\">https://doi.org/10.1083/jcb.201809123</a>","mla":"Toyama, Brandon H., et al. “Visualization of Long-Lived Proteins Reveals Age Mosaicism within Nuclei of Postmitotic Cells.” <i>Journal of Cell Biology</i>, vol. 218, no. 2, Rockefeller University Press, 2019, pp. 433–44, doi:<a href=\"https://doi.org/10.1083/jcb.201809123\">10.1083/jcb.201809123</a>.","ieee":"B. H. Toyama <i>et al.</i>, “Visualization of long-lived proteins reveals age mosaicism within nuclei of postmitotic cells,” <i>Journal of Cell Biology</i>, 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."},"volume":218,"publisher":"Rockefeller University Press","day":"04","doi":"10.1083/jcb.201809123","page":"433-444","type":"journal_article","file_date_updated":"2022-04-08T08:26:32Z","date_created":"2022-04-07T07:45:11Z","tmp":{"legal_code_url":"https://creativecommons.org/licenses/by-nc-sa/4.0/legalcode","short":"CC BY-NC-SA (4.0)","image":"/images/cc_by_nc_sa.png","name":"Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)"},"quality_controlled":"1","language":[{"iso":"eng"}],"intvolume":"       218","publication_identifier":{"issn":["0021-9525"],"eissn":["1540-8140"]},"has_accepted_license":"1","date_updated":"2024-10-14T11:19:21Z","external_id":{"pmid":["30552100"]}},{"type":"journal_article","publisher":"Rockefeller University Press","day":"16","doi":"10.1083/jcb.201410047","page":"671-681","volume":208,"citation":{"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,” <i>Journal of Cell Biology</i>, vol. 208, no. 6. Rockefeller University Press, pp. 671–681, 2015.","apa":"Gomez-Cavazos, J. S., &#38; Hetzer, M. (2015). The nucleoporin gp210/Nup210 controls muscle differentiation by regulating nuclear envelope/ER homeostasis. <i>Journal of Cell Biology</i>. Rockefeller University Press. <a href=\"https://doi.org/10.1083/jcb.201410047\">https://doi.org/10.1083/jcb.201410047</a>","mla":"Gomez-Cavazos, J. Sebastian, and Martin Hetzer. “The Nucleoporin Gp210/Nup210 Controls Muscle Differentiation by Regulating Nuclear Envelope/ER Homeostasis.” <i>Journal of Cell Biology</i>, vol. 208, no. 6, Rockefeller University Press, 2015, pp. 671–81, doi:<a href=\"https://doi.org/10.1083/jcb.201410047\">10.1083/jcb.201410047</a>.","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.","ama":"Gomez-Cavazos JS, Hetzer M. The nucleoporin gp210/Nup210 controls muscle differentiation by regulating nuclear envelope/ER homeostasis. <i>Journal of Cell Biology</i>. 2015;208(6):671-681. doi:<a href=\"https://doi.org/10.1083/jcb.201410047\">10.1083/jcb.201410047</a>","chicago":"Gomez-Cavazos, J. Sebastian, and Martin Hetzer. “The Nucleoporin Gp210/Nup210 Controls Muscle Differentiation by Regulating Nuclear Envelope/ER Homeostasis.” <i>Journal of Cell Biology</i>. Rockefeller University Press, 2015. <a href=\"https://doi.org/10.1083/jcb.201410047\">https://doi.org/10.1083/jcb.201410047</a>."},"extern":"1","publication":"Journal of Cell Biology","external_id":{"pmid":["25778917"]},"date_updated":"2024-10-14T11:22:26Z","publication_identifier":{"issn":["0021-9525"],"eissn":["1540-8140"]},"quality_controlled":"1","language":[{"iso":"eng"}],"intvolume":"       208","date_created":"2022-04-07T07:49:10Z","keyword":["Cell Biology"],"title":"The nucleoporin gp210/Nup210 controls muscle differentiation by regulating nuclear envelope/ER homeostasis","oa_version":"Published Version","issue":"6","_id":"11075","year":"2015","month":"03","pmid":1,"article_processing_charge":"No","status":"public","abstract":[{"lang":"eng","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."}],"scopus_import":"1","date_published":"2015-03-16T00:00:00Z","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","author":[{"full_name":"Gomez-Cavazos, J. Sebastian","first_name":"J. Sebastian","last_name":"Gomez-Cavazos"},{"first_name":"Martin W","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","full_name":"HETZER, Martin W","orcid":"0000-0002-2111-992X","last_name":"HETZER"}],"publication_status":"published","article_type":"original"},{"main_file_link":[{"open_access":"1","url":"https://doi.org/10.1083/jcb.201012154"}],"extern":"1","publication":"Journal of Cell Biology","type":"journal_article","publisher":"Rockefeller University Press","day":"04","doi":"10.1083/jcb.201012154","page":"27-37","volume":194,"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>","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>.","short":"J.A. Talamas, M. Hetzer, Journal of Cell Biology 194 (2011) 27–37.","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.","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>","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."},"date_created":"2022-04-07T07:52:18Z","external_id":{"pmid":["21727197"]},"date_updated":"2024-10-14T11:26:10Z","publication_identifier":{"eissn":["1540-8140"],"issn":["0021-9525"]},"language":[{"iso":"eng"}],"quality_controlled":"1","intvolume":"       194","month":"07","pmid":1,"article_processing_charge":"No","keyword":["Cell Biology"],"title":"POM121 and Sun1 play a role in early steps of interphase NPC assembly","oa_version":"Published Version","issue":"1","_id":"11094","year":"2011","oa":1,"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","author":[{"full_name":"Talamas, Jessica A.","first_name":"Jessica A.","last_name":"Talamas"},{"last_name":"HETZER","orcid":"0000-0002-2111-992X","first_name":"Martin W","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","full_name":"HETZER, Martin W"}],"publication_status":"published","article_type":"original","status":"public","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."}],"scopus_import":"1","date_published":"2011-07-04T00:00:00Z"},{"extern":"1","main_file_link":[{"url":"https://doi.org/10.1083/jcb.200901106","open_access":"1"}],"publication":"Journal of Cell Biology","page":"183-191","day":"20","publisher":"Rockefeller University Press","doi":"10.1083/jcb.200901106","related_material":{"link":[{"url":"https://doi.org/10.1083/jcb.20090110620090903c","relation":"erratum"}]},"type":"journal_article","citation":{"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.","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>.","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>","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>.","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>"},"volume":186,"date_created":"2022-04-07T07:54:18Z","date_updated":"2024-10-14T11:28:48Z","external_id":{"pmid":["19620630"]},"intvolume":"       186","language":[{"iso":"eng"}],"quality_controlled":"1","publication_identifier":{"issn":["0021-9525"],"eissn":["1540-8140"]},"pmid":1,"month":"07","article_processing_charge":"No","title":"Recruitment of functionally distinct membrane proteins to chromatin mediates nuclear envelope formation in vivo","keyword":["Cell Biology"],"year":"2009","issue":"2","_id":"11106","oa_version":"Published Version","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","oa":1,"article_type":"original","publication_status":"published","author":[{"last_name":"Anderson","first_name":"Daniel J.","full_name":"Anderson, Daniel J."},{"first_name":"Jesse D.","full_name":"Vargas, Jesse D.","last_name":"Vargas"},{"full_name":"Hsiao, Joshua P.","first_name":"Joshua P.","last_name":"Hsiao"},{"last_name":"HETZER","orcid":"0000-0002-2111-992X","first_name":"Martin W","full_name":"HETZER, Martin W","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed"}],"abstract":[{"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.","lang":"eng"}],"date_published":"2009-07-20T00:00:00Z","scopus_import":"1","status":"public"},{"title":"ER membrane–bending proteins are necessary for de novo nuclear pore formation","keyword":["Cell Biology"],"oa_version":"Published Version","year":"2009","_id":"11107","issue":"5","month":"03","pmid":1,"article_processing_charge":"No","status":"public","date_published":"2009-03-09T00:00:00Z","scopus_import":"1","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"}],"oa":1,"user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","author":[{"last_name":"Dawson","full_name":"Dawson, T. Renee","first_name":"T. Renee"},{"last_name":"Lazarus","first_name":"Michelle D.","full_name":"Lazarus, Michelle D."},{"id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","full_name":"HETZER, Martin W","first_name":"Martin W","last_name":"HETZER","orcid":"0000-0002-2111-992X"},{"full_name":"Wente, Susan R.","first_name":"Susan R.","last_name":"Wente"}],"article_type":"original","publication_status":"published","type":"journal_article","page":"659-675","doi":"10.1083/jcb.200806174","day":"09","publisher":"Rockefeller University Press","volume":184,"citation":{"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.","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>","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>.","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.","short":"T.R. Dawson, M.D. Lazarus, M. Hetzer, S.R. Wente, Journal of Cell Biology 184 (2009) 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>.","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>"},"extern":"1","main_file_link":[{"open_access":"1","url":"https://doi.org/10.1083/jcb.200806174"}],"publication":"Journal of Cell Biology","external_id":{"pmid":["19273614"]},"date_updated":"2022-07-18T08:55:05Z","publication_identifier":{"issn":["0021-9525"],"eissn":["1540-8140"]},"intvolume":"       184","language":[{"iso":"eng"}],"quality_controlled":"1","date_created":"2022-04-07T07:54:44Z"},{"external_id":{"pmid":["18779370"]},"date_updated":"2024-10-14T11:29:29Z","publication_identifier":{"issn":["0021-9525"],"eissn":["1540-8140"]},"intvolume":"       182","quality_controlled":"1","language":[{"iso":"eng"}],"date_created":"2022-04-07T07:55:23Z","type":"journal_article","page":"911-924","day":"08","publisher":"Rockefeller University Press","doi":"10.1083/jcb.200805140","volume":182,"citation":{"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>","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>.","short":"D.J. Anderson, M. Hetzer, Journal of Cell Biology 182 (2008) 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.","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>.","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>","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."},"extern":"1","publication":"Journal of Cell Biology","status":"public","date_published":"2008-09-08T00:00:00Z","scopus_import":"1","abstract":[{"lang":"eng","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."}],"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","author":[{"last_name":"Anderson","first_name":"Daniel J.","full_name":"Anderson, Daniel J."},{"orcid":"0000-0002-2111-992X","last_name":"HETZER","first_name":"Martin W","full_name":"HETZER, Martin W","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed"}],"article_type":"original","publication_status":"published","title":"Reshaping of the endoplasmic reticulum limits the rate for nuclear envelope formation","keyword":["Cell Biology"],"oa_version":"None","year":"2008","issue":"5","_id":"11111","month":"09","pmid":1,"article_processing_charge":"No"},{"author":[{"orcid":"0000-0002-2111-992X","last_name":"HETZER","full_name":"HETZER, Martin W","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","first_name":"Martin W"},{"last_name":"Mattaj","full_name":"Mattaj, Iain W.","first_name":"Iain W."}],"article_type":"original","publication_status":"published","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","status":"public","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."}],"date_published":"2000-01-24T00:00:00Z","scopus_import":"1","article_processing_charge":"No","month":"01","pmid":1,"oa_version":"None","_id":"11126","issue":"2","year":"2000","keyword":["Cell Biology"],"title":"An Atp-dependent, Ran-independent mechanism for nuclear import of the U1a and U2b′′ spliceosome proteins","date_created":"2022-04-07T07:57:49Z","publication_identifier":{"issn":["0021-9525"],"eissn":["1540-8140"]},"quality_controlled":"1","language":[{"iso":"eng"}],"intvolume":"       148","external_id":{"pmid":["10648562"]},"date_updated":"2022-07-18T08:58:29Z","publication":"Journal of Cell Biology","extern":"1","volume":148,"citation":{"ama":"Hetzer M, Mattaj IW. An Atp-dependent, Ran-independent mechanism for nuclear import of the U1a and U2b′′ spliceosome proteins. <i>Journal of Cell Biology</i>. 2000;148(2):293-304. doi:<a href=\"https://doi.org/10.1083/jcb.148.2.293\">10.1083/jcb.148.2.293</a>","chicago":"Hetzer, Martin, and Iain W. Mattaj. “An Atp-Dependent, Ran-Independent Mechanism for Nuclear Import of the U1a and U2b′′ Spliceosome Proteins.” <i>Journal of Cell Biology</i>. Rockefeller University Press, 2000. <a href=\"https://doi.org/10.1083/jcb.148.2.293\">https://doi.org/10.1083/jcb.148.2.293</a>.","short":"M. Hetzer, I.W. Mattaj, Journal of Cell Biology 148 (2000) 293–304.","apa":"Hetzer, M., &#38; Mattaj, I. W. (2000). An Atp-dependent, Ran-independent mechanism for nuclear import of the U1a and U2b′′ spliceosome proteins. <i>Journal of Cell Biology</i>. Rockefeller University Press. <a href=\"https://doi.org/10.1083/jcb.148.2.293\">https://doi.org/10.1083/jcb.148.2.293</a>","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.” <i>Journal of Cell Biology</i>, vol. 148, no. 2, Rockefeller University Press, 2000, pp. 293–304, doi:<a href=\"https://doi.org/10.1083/jcb.148.2.293\">10.1083/jcb.148.2.293</a>.","ieee":"M. Hetzer and I. W. Mattaj, “An Atp-dependent, Ran-independent mechanism for nuclear import of the U1a and U2b′′ spliceosome proteins,” <i>Journal of Cell Biology</i>, vol. 148, no. 2. Rockefeller University Press, pp. 293–304, 2000."},"type":"journal_article","publisher":"Rockefeller University Press","doi":"10.1083/jcb.148.2.293","day":"24","page":"293-304"}]