[{"language":[{"iso":"eng"}],"article_processing_charge":"No","abstract":[{"lang":"eng","text":"The inner nuclear membrane (INM) is a subdomain of the endoplasmic reticulum (ER) that is gated by the nuclear pore complex. It is unknown whether proteins of the INM and ER are degraded through shared or distinct pathways in mammalian cells. We applied dynamic proteomics to profile protein half-lives and report that INM and ER residents turn over at similar rates, indicating that the INM’s unique topology is not a barrier to turnover. Using a microscopy approach, we observed that the proteasome can degrade INM proteins in situ. However, we also uncovered evidence for selective, vesicular transport-mediated turnover of a single INM protein, emerin, that is potentiated by ER stress. Emerin is rapidly cleared from the INM by a mechanism that requires emerin’s LEM domain to mediate vesicular trafficking to lysosomes. This work demonstrates that the INM can be dynamically remodeled in response to environmental inputs."}],"publisher":"eLife Sciences Publications","publication":"eLife","date_published":"2019-10-10T00:00:00Z","volume":8,"intvolume":"         8","oa_version":"Published Version","ddc":["570"],"article_type":"original","year":"2019","quality_controlled":"1","doi":"10.7554/elife.49796","has_accepted_license":"1","publication_identifier":{"issn":["2050-084X"]},"title":"Selective clearance of the inner nuclear membrane protein emerin by vesicular transport during ER stress","citation":{"short":"A. Buchwalter, R. Schulte, H. Tsai, J. Capitanio, M. Hetzer, ELife 8 (2019).","ista":"Buchwalter A, Schulte R, Tsai H, Capitanio J, Hetzer M. 2019. Selective clearance of the inner nuclear membrane protein emerin by vesicular transport during ER stress. eLife. 8, e49796.","mla":"Buchwalter, Abigail, et al. “Selective Clearance of the Inner Nuclear Membrane Protein Emerin by Vesicular Transport during ER Stress.” <i>ELife</i>, vol. 8, e49796, eLife Sciences Publications, 2019, doi:<a href=\"https://doi.org/10.7554/elife.49796\">10.7554/elife.49796</a>.","ieee":"A. Buchwalter, R. Schulte, H. Tsai, J. Capitanio, and M. Hetzer, “Selective clearance of the inner nuclear membrane protein emerin by vesicular transport during ER stress,” <i>eLife</i>, vol. 8. eLife Sciences Publications, 2019.","apa":"Buchwalter, A., Schulte, R., Tsai, H., Capitanio, J., &#38; Hetzer, M. (2019). Selective clearance of the inner nuclear membrane protein emerin by vesicular transport during ER stress. <i>ELife</i>. eLife Sciences Publications. <a href=\"https://doi.org/10.7554/elife.49796\">https://doi.org/10.7554/elife.49796</a>","chicago":"Buchwalter, Abigail, Roberta Schulte, Hsiao Tsai, Juliana Capitanio, and Martin Hetzer. “Selective Clearance of the Inner Nuclear Membrane Protein Emerin by Vesicular Transport during ER Stress.” <i>ELife</i>. eLife Sciences Publications, 2019. <a href=\"https://doi.org/10.7554/elife.49796\">https://doi.org/10.7554/elife.49796</a>.","ama":"Buchwalter A, Schulte R, Tsai H, Capitanio J, Hetzer M. Selective clearance of the inner nuclear membrane protein emerin by vesicular transport during ER stress. <i>eLife</i>. 2019;8. doi:<a href=\"https://doi.org/10.7554/elife.49796\">10.7554/elife.49796</a>"},"oa":1,"date_updated":"2024-10-14T12:08:36Z","file_date_updated":"2022-04-08T08:18:01Z","scopus_import":"1","_id":"11060","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","day":"10","article_number":"e49796","related_material":{"record":[{"relation":"research_data","status":"public","id":"13079"}]},"publication_status":"published","author":[{"first_name":"Abigail","last_name":"Buchwalter","full_name":"Buchwalter, Abigail"},{"full_name":"Schulte, Roberta","first_name":"Roberta","last_name":"Schulte"},{"last_name":"Tsai","first_name":"Hsiao","full_name":"Tsai, Hsiao"},{"full_name":"Capitanio, Juliana","last_name":"Capitanio","first_name":"Juliana"},{"id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","last_name":"HETZER","first_name":"Martin W","orcid":"0000-0002-2111-992X","full_name":"HETZER, Martin W"}],"pmid":1,"extern":"1","external_id":{"pmid":["31599721"]},"date_created":"2022-04-07T07:45:02Z","tmp":{"short":"CC BY (4.0)","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","image":"/images/cc_by.png"},"status":"public","keyword":["General Immunology and Microbiology","General Biochemistry","Genetics and Molecular Biology","General Medicine","General Neuroscience"],"file":[{"checksum":"1e8672a1e9c3dc0a2d3d0dad89673616","file_id":"11138","success":1,"content_type":"application/pdf","file_size":6984654,"creator":"dernst","relation":"main_file","access_level":"open_access","date_created":"2022-04-08T08:18:01Z","date_updated":"2022-04-08T08:18:01Z","file_name":"2019_eLife_Buchwalter.pdf"}],"month":"10","type":"journal_article"},{"article_type":"original","ddc":["580"],"oa_version":"Published Version","year":"2019","has_accepted_license":"1","doi":"10.7554/elife.42530","quality_controlled":"1","publication_identifier":{"issn":["2050-084X"]},"article_processing_charge":"No","language":[{"iso":"eng"}],"publisher":"eLife Sciences Publications","abstract":[{"lang":"eng","text":"Transposable elements (TEs), the movement of which can damage the genome, are epigenetically silenced in eukaryotes. Intriguingly, TEs are activated in the sperm companion cell – vegetative cell (VC) – of the flowering plant Arabidopsis thaliana. However, the extent and mechanism of this activation are unknown. Here we show that about 100 heterochromatic TEs are activated in VCs, mostly by DEMETER-catalyzed DNA demethylation. We further demonstrate that DEMETER access to some of these TEs is permitted by the natural depletion of linker histone H1 in VCs. Ectopically expressed H1 suppresses TEs in VCs by reducing DNA demethylation and via a methylation-independent mechanism. We demonstrate that H1 is required for heterochromatin condensation in plant cells and show that H1 overexpression creates heterochromatic foci in the VC progenitor cell. Taken together, our results demonstrate that the natural depletion of H1 during male gametogenesis facilitates DEMETER-directed DNA demethylation, heterochromatin relaxation, and TE activation."}],"intvolume":"         8","volume":8,"date_published":"2019-05-28T00:00:00Z","publication":"eLife","author":[{"full_name":"He, Shengbo","last_name":"He","first_name":"Shengbo"},{"first_name":"Martin","last_name":"Vickers","full_name":"Vickers, Martin"},{"first_name":"Jingyi","last_name":"Zhang","full_name":"Zhang, Jingyi"},{"id":"e0164712-22ee-11ed-b12a-d80fcdf35958","first_name":"Xiaoqi","orcid":"0000-0002-4008-1234","last_name":"Feng","full_name":"Feng, Xiaoqi"}],"publication_status":"published","date_created":"2023-01-16T09:17:21Z","external_id":{"unknown":["31135340"]},"extern":"1","department":[{"_id":"XiFe"}],"keyword":["General Immunology and Microbiology","General Biochemistry","Genetics and Molecular Biology","General Medicine","General Neuroscience"],"status":"public","tmp":{"short":"CC BY (4.0)","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","image":"/images/cc_by.png"},"type":"journal_article","month":"05","file":[{"creator":"alisjak","file_id":"12525","checksum":"ea6b89c20d59e5eb3646916fe5d568ad","success":1,"file_size":2493837,"content_type":"application/pdf","access_level":"open_access","relation":"main_file","file_name":"2019_elife_He.pdf","date_created":"2023-02-07T09:42:46Z","date_updated":"2023-02-07T09:42:46Z"}],"title":"Natural depletion of histone H1 in sex cells causes DNA demethylation, heterochromatin decondensation and transposon activation","date_updated":"2025-01-14T14:31:41Z","oa":1,"citation":{"short":"S. He, M. Vickers, J. Zhang, X. Feng, ELife 8 (2019).","ista":"He S, Vickers M, Zhang J, Feng X. 2019. Natural depletion of histone H1 in sex cells causes DNA demethylation, heterochromatin decondensation and transposon activation. eLife. 8, 42530.","ieee":"S. He, M. Vickers, J. Zhang, and X. Feng, “Natural depletion of histone H1 in sex cells causes DNA demethylation, heterochromatin decondensation and transposon activation,” <i>eLife</i>, vol. 8. eLife Sciences Publications, 2019.","mla":"He, Shengbo, et al. “Natural Depletion of Histone H1 in Sex Cells Causes DNA Demethylation, Heterochromatin Decondensation and Transposon Activation.” <i>ELife</i>, vol. 8, 42530, eLife Sciences Publications, 2019, doi:<a href=\"https://doi.org/10.7554/elife.42530\">10.7554/elife.42530</a>.","apa":"He, S., Vickers, M., Zhang, J., &#38; Feng, X. (2019). Natural depletion of histone H1 in sex cells causes DNA demethylation, heterochromatin decondensation and transposon activation. <i>ELife</i>. eLife Sciences Publications. <a href=\"https://doi.org/10.7554/elife.42530\">https://doi.org/10.7554/elife.42530</a>","chicago":"He, Shengbo, Martin Vickers, Jingyi Zhang, and Xiaoqi Feng. “Natural Depletion of Histone H1 in Sex Cells Causes DNA Demethylation, Heterochromatin Decondensation and Transposon Activation.” <i>ELife</i>. eLife Sciences Publications, 2019. <a href=\"https://doi.org/10.7554/elife.42530\">https://doi.org/10.7554/elife.42530</a>.","ama":"He S, Vickers M, Zhang J, Feng X. Natural depletion of histone H1 in sex cells causes DNA demethylation, heterochromatin decondensation and transposon activation. <i>eLife</i>. 2019;8. doi:<a href=\"https://doi.org/10.7554/elife.42530\">10.7554/elife.42530</a>"},"_id":"12192","file_date_updated":"2023-02-07T09:42:46Z","scopus_import":"1","article_number":"42530","day":"28","acknowledgement":"We thank David Twell for the pDONR-P4-P1R-pLAT52 and pDONR-P2R-P3-mRFP vectors, the John Innes Centre Bioimaging Facility (Elaine Barclay and Grant Calder) for their assistance with microscopy, and the Norwich BioScience Institute Partnership Computing infrastructure for Science Group for High Performance Computing resources. This work was funded by a Biotechnology and Biological Sciences Research Council (BBSRC) David Phillips Fellowship (BB/L025043/1; SH, JZ and XF), a European Research Council Starting Grant ('SexMeth' 804981; XF) and a Grant to Exceptional Researchers by the Gatsby Charitable Foundation (SH and XF).","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87"},{"quality_controlled":"1","doi":"10.7554/elife.26163","publication_identifier":{"issn":["2050-084X"]},"oa_version":"Published Version","article_type":"original","year":"2017","publication":"eLife","date_published":"2017-08-01T00:00:00Z","volume":6,"intvolume":"         6","language":[{"iso":"eng"}],"article_processing_charge":"Yes","abstract":[{"text":"Biofilm formation is critical for the infection cycle of Vibrio cholerae. Vibrio exopolysaccharides (VPS) and the matrix proteins RbmA, Bap1 and RbmC are required for the development of biofilm architecture. We demonstrate that RbmA binds VPS directly and uses a binary structural switch within its first fibronectin type III (FnIII-1) domain to control RbmA structural dynamics and the formation of VPS-dependent higher-order structures. The structural switch in FnIII-1 regulates interactions in trans with the FnIII-2 domain, leading to open (monomeric) or closed (dimeric) interfaces. The ability of RbmA to switch between open and closed states is important for V. cholerae biofilm formation, as RbmA variants with switches that are locked in either of the two states lead to biofilms with altered architecture and structural integrity.","lang":"eng"}],"main_file_link":[{"url":"https://doi.org/10.7554/eLife.26163","open_access":"1"}],"publisher":"eLife Sciences Publications","status":"public","keyword":["General Immunology and Microbiology","General Biochemistry","Genetics and Molecular Biology","General Medicine","General Neuroscience"],"type":"journal_article","month":"08","publication_status":"published","pmid":1,"author":[{"full_name":"Fong, Jiunn CN","first_name":"Jiunn CN","last_name":"Fong"},{"full_name":"Rogers, Andrew","first_name":"Andrew","last_name":"Rogers"},{"full_name":"Michael, Alicia Kathleen","id":"6437c950-2a03-11ee-914d-d6476dd7b75c","first_name":"Alicia Kathleen","last_name":"Michael"},{"full_name":"Parsley, Nicole C","first_name":"Nicole C","last_name":"Parsley"},{"full_name":"Cornell, William-Cole","last_name":"Cornell","first_name":"William-Cole"},{"first_name":"Yu-Cheng","last_name":"Lin","full_name":"Lin, Yu-Cheng"},{"last_name":"Singh","first_name":"Praveen K","full_name":"Singh, Praveen K"},{"full_name":"Hartmann, Raimo","last_name":"Hartmann","first_name":"Raimo"},{"full_name":"Drescher, Knut","first_name":"Knut","last_name":"Drescher"},{"full_name":"Vinogradov, Evgeny","first_name":"Evgeny","last_name":"Vinogradov"},{"full_name":"Dietrich, Lars EP","last_name":"Dietrich","first_name":"Lars EP"},{"full_name":"Partch, Carrie L","last_name":"Partch","first_name":"Carrie L"},{"first_name":"Fitnat H","last_name":"Yildiz","full_name":"Yildiz, Fitnat H"}],"extern":"1","external_id":{"pmid":["28762945"]},"date_created":"2024-03-21T07:55:36Z","scopus_import":"1","_id":"15154","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","day":"01","article_number":"26163","title":"Structural dynamics of RbmA governs plasticity of Vibrio cholerae biofilms","citation":{"mla":"Fong, Jiunn CN, et al. “Structural Dynamics of RbmA Governs Plasticity of Vibrio Cholerae Biofilms.” <i>ELife</i>, vol. 6, 26163, eLife Sciences Publications, 2017, doi:<a href=\"https://doi.org/10.7554/elife.26163\">10.7554/elife.26163</a>.","ieee":"J. C. Fong <i>et al.</i>, “Structural dynamics of RbmA governs plasticity of Vibrio cholerae biofilms,” <i>eLife</i>, vol. 6. eLife Sciences Publications, 2017.","ista":"Fong JC, Rogers A, Michael AK, Parsley NC, Cornell W-C, Lin Y-C, Singh PK, Hartmann R, Drescher K, Vinogradov E, Dietrich LE, Partch CL, Yildiz FH. 2017. Structural dynamics of RbmA governs plasticity of Vibrio cholerae biofilms. eLife. 6, 26163.","short":"J.C. Fong, A. Rogers, A.K. Michael, N.C. Parsley, W.-C. Cornell, Y.-C. Lin, P.K. Singh, R. Hartmann, K. Drescher, E. Vinogradov, L.E. Dietrich, C.L. Partch, F.H. Yildiz, ELife 6 (2017).","chicago":"Fong, Jiunn CN, Andrew Rogers, Alicia K. Michael, Nicole C Parsley, William-Cole Cornell, Yu-Cheng Lin, Praveen K Singh, et al. “Structural Dynamics of RbmA Governs Plasticity of Vibrio Cholerae Biofilms.” <i>ELife</i>. eLife Sciences Publications, 2017. <a href=\"https://doi.org/10.7554/elife.26163\">https://doi.org/10.7554/elife.26163</a>.","ama":"Fong JC, Rogers A, Michael AK, et al. Structural dynamics of RbmA governs plasticity of Vibrio cholerae biofilms. <i>eLife</i>. 2017;6. doi:<a href=\"https://doi.org/10.7554/elife.26163\">10.7554/elife.26163</a>","apa":"Fong, J. C., Rogers, A., Michael, A. K., Parsley, N. C., Cornell, W.-C., Lin, Y.-C., … Yildiz, F. H. (2017). Structural dynamics of RbmA governs plasticity of Vibrio cholerae biofilms. <i>ELife</i>. eLife Sciences Publications. <a href=\"https://doi.org/10.7554/elife.26163\">https://doi.org/10.7554/elife.26163</a>"},"oa":1,"date_updated":"2024-03-25T12:22:54Z"},{"date_published":"2017-11-09T00:00:00Z","publication":"eLife","volume":6,"intvolume":"         6","language":[{"iso":"eng"}],"article_processing_charge":"No","abstract":[{"lang":"eng","text":"Eukaryotic cells are densely packed with macromolecular complexes and intertwining organelles, continually transported and reshaped. Intriguingly, organelles avoid clashing and entangling with each other in such limited space. Mitochondria form extensive networks constantly remodeled by fission and fusion. Here, we show that mitochondrial fission is triggered by mechanical forces. Mechano-stimulation of mitochondria – via encounter with motile intracellular pathogens, via external pressure applied by an atomic force microscope, or via cell migration across uneven microsurfaces – results in the recruitment of the mitochondrial fission machinery, and subsequent division. We propose that MFF, owing to affinity for narrow mitochondria, acts as a membrane-bound force sensor to recruit the fission machinery to mechanically strained sites. Thus, mitochondria adapt to the environment by sensing and responding to biomechanical cues. Our findings that mechanical triggers can be coupled to biochemical responses in membrane dynamics may explain how organelles orderly cohabit in the crowded cytoplasm."}],"publisher":"eLife Sciences Publications","main_file_link":[{"open_access":"1","url":"https://elifesciences.org/articles/30292"}],"quality_controlled":"1","doi":"10.7554/elife.30292","has_accepted_license":"1","publication_identifier":{"issn":["2050-084X"]},"ddc":["572"],"oa_version":"Published Version","article_type":"original","year":"2017","file_date_updated":"2021-11-29T09:07:41Z","scopus_import":"1","_id":"10370","user_id":"8b945eb4-e2f2-11eb-945a-df72226e66a9","article_number":"e30292","day":"09","title":"Mechanical force induces mitochondrial fission","citation":{"mla":"Helle, Sebastian Carsten Johannes, et al. “Mechanical Force Induces Mitochondrial Fission.” <i>ELife</i>, vol. 6, e30292, eLife Sciences Publications, 2017, doi:<a href=\"https://doi.org/10.7554/elife.30292\">10.7554/elife.30292</a>.","ieee":"S. C. J. Helle <i>et al.</i>, “Mechanical force induces mitochondrial fission,” <i>eLife</i>, vol. 6. eLife Sciences Publications, 2017.","short":"S.C.J. Helle, Q. Feng, M.J. Aebersold, L. Hirt, R.R. Grüter, A. Vahid, A. Sirianni, S. Mostowy, J.G. Snedeker, A. Šarić, T. Idema, T. Zambelli, B. Kornmann, ELife 6 (2017).","ista":"Helle SCJ, Feng Q, Aebersold MJ, Hirt L, Grüter RR, Vahid A, Sirianni A, Mostowy S, Snedeker JG, Šarić A, Idema T, Zambelli T, Kornmann B. 2017. Mechanical force induces mitochondrial fission. eLife. 6, e30292.","chicago":"Helle, Sebastian Carsten Johannes, Qian Feng, Mathias J Aebersold, Luca Hirt, Raphael R Grüter, Afshin Vahid, Andrea Sirianni, et al. “Mechanical Force Induces Mitochondrial Fission.” <i>ELife</i>. eLife Sciences Publications, 2017. <a href=\"https://doi.org/10.7554/elife.30292\">https://doi.org/10.7554/elife.30292</a>.","ama":"Helle SCJ, Feng Q, Aebersold MJ, et al. Mechanical force induces mitochondrial fission. <i>eLife</i>. 2017;6. doi:<a href=\"https://doi.org/10.7554/elife.30292\">10.7554/elife.30292</a>","apa":"Helle, S. C. J., Feng, Q., Aebersold, M. J., Hirt, L., Grüter, R. R., Vahid, A., … Kornmann, B. (2017). Mechanical force induces mitochondrial fission. <i>ELife</i>. eLife Sciences Publications. <a href=\"https://doi.org/10.7554/elife.30292\">https://doi.org/10.7554/elife.30292</a>"},"oa":1,"date_updated":"2021-11-29T09:28:14Z","tmp":{"short":"CC BY (4.0)","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","image":"/images/cc_by.png"},"status":"public","keyword":["general immunology and microbiology","general biochemistry","genetics and molecular biology","general medicine","general neuroscience"],"file":[{"creator":"cchlebak","file_id":"10372","checksum":"c35f42dcfb007f6d6c761a27e24c26d3","success":1,"file_size":6120157,"content_type":"application/pdf","access_level":"open_access","relation":"main_file","file_name":"2017_eLife_Helle.pdf","date_updated":"2021-11-29T09:07:41Z","date_created":"2021-11-29T09:07:41Z"}],"month":"11","type":"journal_article","publication_status":"published","author":[{"full_name":"Helle, Sebastian Carsten Johannes","first_name":"Sebastian Carsten Johannes","last_name":"Helle"},{"last_name":"Feng","first_name":"Qian","full_name":"Feng, Qian"},{"full_name":"Aebersold, Mathias J","first_name":"Mathias J","last_name":"Aebersold"},{"last_name":"Hirt","first_name":"Luca","full_name":"Hirt, Luca"},{"last_name":"Grüter","first_name":"Raphael R","full_name":"Grüter, Raphael R"},{"full_name":"Vahid, Afshin","first_name":"Afshin","last_name":"Vahid"},{"first_name":"Andrea","last_name":"Sirianni","full_name":"Sirianni, Andrea"},{"last_name":"Mostowy","first_name":"Serge","full_name":"Mostowy, Serge"},{"full_name":"Snedeker, Jess G","last_name":"Snedeker","first_name":"Jess G"},{"full_name":"Šarić, Anđela","id":"bf63d406-f056-11eb-b41d-f263a6566d8b","last_name":"Šarić","orcid":"0000-0002-7854-2139","first_name":"Anđela"},{"full_name":"Idema, Timon","last_name":"Idema","first_name":"Timon"},{"first_name":"Tomaso","last_name":"Zambelli","full_name":"Zambelli, Tomaso"},{"last_name":"Kornmann","first_name":"Benoît","full_name":"Kornmann, Benoît"}],"pmid":1,"extern":"1","date_created":"2021-11-29T08:51:38Z","external_id":{"pmid":["29119945"]}}]