[{"publication_status":"published","oa_version":"Published Version","page":"130-148.e17","day":"04","tmp":{"legal_code_url":"https://creativecommons.org/licenses/by-nc/4.0/legalcode","name":"Creative Commons Attribution-NonCommercial 4.0 International (CC BY-NC 4.0)","short":"CC BY-NC (4.0)","image":"/images/cc_by_nc.png"},"ec_funded":1,"abstract":[{"lang":"eng","text":"The plant-signaling molecule auxin triggers fast and slow cellular responses across land plants and algae. The nuclear auxin pathway mediates gene expression and controls growth and development in land plants, but this pathway is absent from algal sister groups. Several components of rapid responses have been identified in Arabidopsis, but it is unknown if these are part of a conserved mechanism. We recently identified a fast, proteome-wide phosphorylation response to auxin. Here, we show that this response occurs across 5 land plant and algal species and converges on a core group of shared targets. We found conserved rapid physiological responses to auxin in the same species and identified rapidly accelerated fibrosarcoma (RAF)-like protein kinases as central mediators of auxin-triggered phosphorylation across species. Genetic analysis connects this kinase to both auxin-triggered protein phosphorylation and rapid cellular response, thus identifying an ancient mechanism for fast auxin responses in the green lineage."}],"status":"public","date_updated":"2024-01-22T13:43:40Z","publication":"Cell","external_id":{"pmid":["38128538"]},"file":[{"file_size":13194060,"file_name":"2024_Cell_Kuhn.pdf","date_updated":"2024-01-22T13:41:41Z","success":1,"checksum":"06fd236a9ee0b46ccb05f44695bfc34b","file_id":"14874","date_created":"2024-01-22T13:41:41Z","creator":"dernst","relation":"main_file","content_type":"application/pdf","access_level":"open_access"}],"title":"RAF-like protein kinases mediate a deeply conserved, rapid auxin response","issue":"1","scopus_import":"1","has_accepted_license":"1","project":[{"grant_number":"742985","call_identifier":"H2020","_id":"261099A6-B435-11E9-9278-68D0E5697425","name":"Tracing Evolution of Auxin Transport and Polarity in Plants"},{"name":"RNA-directed DNA methylation in plant development","_id":"262EF96E-B435-11E9-9278-68D0E5697425","call_identifier":"FWF","grant_number":"P29988"}],"citation":{"ieee":"A. Kuhn <i>et al.</i>, “RAF-like protein kinases mediate a deeply conserved, rapid auxin response,” <i>Cell</i>, vol. 187, no. 1. Elsevier, p. 130–148.e17, 2024.","chicago":"Kuhn, Andre, Mark Roosjen, Sumanth Mutte, Shiv Mani Dubey, Vanessa Polet Carrillo Carrasco, Sjef Boeren, Aline Monzer, et al. “RAF-like Protein Kinases Mediate a Deeply Conserved, Rapid Auxin Response.” <i>Cell</i>. Elsevier, 2024. <a href=\"https://doi.org/10.1016/j.cell.2023.11.021\">https://doi.org/10.1016/j.cell.2023.11.021</a>.","ama":"Kuhn A, Roosjen M, Mutte S, et al. RAF-like protein kinases mediate a deeply conserved, rapid auxin response. <i>Cell</i>. 2024;187(1):130-148.e17. doi:<a href=\"https://doi.org/10.1016/j.cell.2023.11.021\">10.1016/j.cell.2023.11.021</a>","ista":"Kuhn A, Roosjen M, Mutte S, Dubey SM, Carrillo Carrasco VP, Boeren S, Monzer A, Koehorst J, Kohchi T, Nishihama R, Fendrych M, Sprakel J, Friml J, Weijers D. 2024. RAF-like protein kinases mediate a deeply conserved, rapid auxin response. Cell. 187(1), 130–148.e17.","apa":"Kuhn, A., Roosjen, M., Mutte, S., Dubey, S. M., Carrillo Carrasco, V. P., Boeren, S., … Weijers, D. (2024). RAF-like protein kinases mediate a deeply conserved, rapid auxin response. <i>Cell</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.cell.2023.11.021\">https://doi.org/10.1016/j.cell.2023.11.021</a>","short":"A. Kuhn, M. Roosjen, S. Mutte, S.M. Dubey, V.P. Carrillo Carrasco, S. Boeren, A. Monzer, J. Koehorst, T. Kohchi, R. Nishihama, M. Fendrych, J. Sprakel, J. Friml, D. Weijers, Cell 187 (2024) 130–148.e17.","mla":"Kuhn, Andre, et al. “RAF-like Protein Kinases Mediate a Deeply Conserved, Rapid Auxin Response.” <i>Cell</i>, vol. 187, no. 1, Elsevier, 2024, p. 130–148.e17, doi:<a href=\"https://doi.org/10.1016/j.cell.2023.11.021\">10.1016/j.cell.2023.11.021</a>."},"date_published":"2024-01-04T00:00:00Z","author":[{"full_name":"Kuhn, Andre","first_name":"Andre","last_name":"Kuhn"},{"first_name":"Mark","full_name":"Roosjen, Mark","last_name":"Roosjen"},{"last_name":"Mutte","first_name":"Sumanth","full_name":"Mutte, Sumanth"},{"full_name":"Dubey, Shiv Mani","first_name":"Shiv Mani","last_name":"Dubey"},{"last_name":"Carrillo Carrasco","first_name":"Vanessa Polet","full_name":"Carrillo Carrasco, Vanessa Polet"},{"last_name":"Boeren","first_name":"Sjef","full_name":"Boeren, Sjef"},{"last_name":"Monzer","id":"2DB5D88C-D7B3-11E9-B8FD-7907E6697425","full_name":"Monzer, Aline","first_name":"Aline"},{"last_name":"Koehorst","first_name":"Jasper","full_name":"Koehorst, Jasper"},{"first_name":"Takayuki","full_name":"Kohchi, Takayuki","last_name":"Kohchi"},{"full_name":"Nishihama, Ryuichi","first_name":"Ryuichi","last_name":"Nishihama"},{"orcid":"0000-0002-9767-8699","last_name":"Fendrych","id":"43905548-F248-11E8-B48F-1D18A9856A87","first_name":"Matyas","full_name":"Fendrych, Matyas"},{"first_name":"Joris","full_name":"Sprakel, Joris","last_name":"Sprakel"},{"id":"4159519E-F248-11E8-B48F-1D18A9856A87","last_name":"Friml","orcid":"0000-0002-8302-7596","first_name":"Jiří","full_name":"Friml, Jiří"},{"first_name":"Dolf","full_name":"Weijers, Dolf","last_name":"Weijers"}],"oa":1,"_id":"14826","type":"journal_article","language":[{"iso":"eng"}],"doi":"10.1016/j.cell.2023.11.021","publisher":"Elsevier","year":"2024","volume":187,"article_type":"original","month":"01","quality_controlled":"1","publication_identifier":{"eissn":["1097-4172"],"issn":["0092-8674"]},"article_processing_charge":"Yes (in subscription journal)","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","ddc":["580"],"file_date_updated":"2024-01-22T13:41:41Z","keyword":["General Biochemistry","Genetics and Molecular Biology"],"intvolume":"       187","date_created":"2024-01-17T12:45:40Z","pmid":1,"acknowledgement":"We are grateful to Asuka Shitaku and Eri Koide for generating and sharing the Marchantia PRAF-mCitrine line and Peng-Cheng Wang for sharing the Arabidopsis raf mutant. We are grateful to our team members for discussions and helpful advice. This work was supported by funding from the Netherlands Organization for Scientific Research (NWO): VICI grant 865.14.001 and ENW-KLEIN OCENW.KLEIN.027 grants to D.W.; VENI grant VI.VENI.212.003 to A.K.; the European Research Council AdG DIRNDL (contract number 833867) to D.W.; CoG CATCH to J.S.; StG CELLONGATE (contract 803048) to M.F.; and AdG ETAP (contract 742985) to J.F.; MEXT KAKENHI grant number JP19H05675 to T.K.; JSPS KAKENHI grant number JP20H03275 to R.N.; Takeda Science Foundation to R.N.; and the Austrian Science Fund (FWF, P29988) to J.F.","department":[{"_id":"JiFr"}]},{"oa":1,"_id":"12802","author":[{"first_name":"Lisa","full_name":"Knaus, Lisa","last_name":"Knaus","id":"3B2ABCF4-F248-11E8-B48F-1D18A9856A87"},{"last_name":"Basilico","id":"36035796-5ACA-11E9-A75E-7AF2E5697425","orcid":"0000-0003-1843-3173","full_name":"Basilico, Bernadette","first_name":"Bernadette"},{"last_name":"Malzl","full_name":"Malzl, Daniel","first_name":"Daniel"},{"full_name":"Gerykova Bujalkova, Maria","first_name":"Maria","last_name":"Gerykova Bujalkova"},{"first_name":"Mateja","full_name":"Smogavec, Mateja","last_name":"Smogavec"},{"first_name":"Lena A.","full_name":"Schwarz, Lena A.","last_name":"Schwarz"},{"full_name":"Gorkiewicz, Sarah","first_name":"Sarah","id":"f141a35d-15a9-11ec-9fb2-fef6becc7b6f","last_name":"Gorkiewicz"},{"full_name":"Amberg, Nicole","first_name":"Nicole","last_name":"Amberg","id":"4CD6AAC6-F248-11E8-B48F-1D18A9856A87","orcid":"0000-0002-3183-8207"},{"last_name":"Pauler","id":"48EA0138-F248-11E8-B48F-1D18A9856A87","orcid":"0000-0002-7462-0048","first_name":"Florian","full_name":"Pauler, Florian"},{"full_name":"Knittl-Frank, Christian","first_name":"Christian","last_name":"Knittl-Frank"},{"id":"7af593f1-d44a-11ed-bf94-a3646a6bb35e","last_name":"Tassinari","first_name":"Marianna","full_name":"Tassinari, Marianna"},{"first_name":"Nuno","full_name":"Maulide, Nuno","last_name":"Maulide"},{"last_name":"Rülicke","full_name":"Rülicke, Thomas","first_name":"Thomas"},{"last_name":"Menche","first_name":"Jörg","full_name":"Menche, Jörg"},{"id":"37B36620-F248-11E8-B48F-1D18A9856A87","last_name":"Hippenmeyer","orcid":"0000-0003-2279-1061","full_name":"Hippenmeyer, Simon","first_name":"Simon"},{"id":"3E57A680-F248-11E8-B48F-1D18A9856A87","last_name":"Novarino","orcid":"0000-0002-7673-7178","first_name":"Gaia","full_name":"Novarino, Gaia"}],"date_published":"2023-04-27T00:00:00Z","publisher":"Elsevier","year":"2023","language":[{"iso":"eng"}],"doi":"10.1016/j.cell.2023.02.037","type":"journal_article","quality_controlled":"1","publication_identifier":{"issn":["0092-8674"]},"month":"04","article_type":"original","volume":186,"isi":1,"acknowledgement":"We thank A. Freeman and V. Voronin for technical assistance, S. Deixler, A. Stichelberger, M. Schunn, and the Preclinical Facility for managing our animal colony. We thank L. Andersen and J. Sonntag, who were involved in generating the MADM lines. We thank the ISTA LSF Mass Spectrometry Core Facility for assistance with the proteomic analysis, as well as the ISTA electron microscopy and Imaging and Optics facility for technical support. Metabolomics LC-MS/MS analysis was performed by the Metabolomics Facility at Vienna BioCenter Core Facilities (VBCF). We acknowledge the support of the EMBL Metabolomics Core Facility (MCF) for lipidomics and intracellular metabolomics mass spectrometry data acquisition and analysis. RNA sequencing was performed by the Next Generation Sequencing Facility at VBCF. Schematics were generated using Biorender.com. This work was supported by the Austrian Science Fund (FWF, DK W1232-B24) and by the European Union’s Horizon 2020 research and innovation program (ERC) grant 725780 (LinPro) to S.H. and 715508 (REVERSEAUTISM) to G.N.","department":[{"_id":"SiHi"},{"_id":"GaNo"}],"date_created":"2023-04-05T08:15:40Z","keyword":["General Biochemistry","Genetics and Molecular Biology"],"intvolume":"       186","article_processing_charge":"Yes (via OA deal)","user_id":"4359f0d1-fa6c-11eb-b949-802e58b17ae8","ddc":["570"],"file_date_updated":"2023-05-02T09:26:21Z","ec_funded":1,"abstract":[{"lang":"eng","text":"Little is known about the critical metabolic changes that neural cells have to undergo during development and how temporary shifts in this program can influence brain circuitries and behavior. Inspired by the discovery that mutations in SLC7A5, a transporter of metabolically essential large neutral amino acids (LNAAs), lead to autism, we employed metabolomic profiling to study the metabolic states of the cerebral cortex across different developmental stages. We found that the forebrain undergoes significant metabolic remodeling throughout development, with certain groups of metabolites showing stage-specific changes, but what are the consequences of perturbing this metabolic program? By manipulating Slc7a5 expression in neural cells, we found that the metabolism of LNAAs and lipids are interconnected in the cortex. Deletion of Slc7a5 in neurons affects the postnatal metabolic state, leading to a shift in lipid metabolism. Additionally, it causes stage- and cell-type-specific alterations in neuronal activity patterns, resulting in a long-term circuit dysfunction."}],"publication_status":"published","oa_version":"Published Version","page":"1950-1967.e25","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)"},"day":"27","date_updated":"2024-02-07T08:03:32Z","acknowledged_ssus":[{"_id":"PreCl"},{"_id":"EM-Fac"},{"_id":"Bio"},{"_id":"LifeSc"}],"status":"public","external_id":{"isi":["000991468700001"]},"related_material":{"record":[{"relation":"dissertation_contains","status":"public","id":"13107"}],"link":[{"url":"https://ista.ac.at/en/news/feed-them-or-lose-them/","relation":"press_release","description":"News on ISTA Website"}]},"file":[{"file_size":15712841,"file_name":"2023_Cell_Knaus.pdf","date_updated":"2023-05-02T09:26:21Z","success":1,"date_created":"2023-05-02T09:26:21Z","file_id":"12889","checksum":"47e94fbe19e86505b429cb7a5b503ce6","creator":"dernst","relation":"main_file","content_type":"application/pdf","access_level":"open_access"}],"title":"Large neutral amino acid levels tune perinatal neuronal excitability and survival","publication":"Cell","project":[{"name":"Molecular Drug Targets","_id":"2548AE96-B435-11E9-9278-68D0E5697425","grant_number":"W1232-B24","call_identifier":"FWF"},{"_id":"260018B0-B435-11E9-9278-68D0E5697425","name":"Principles of Neural Stem Cell Lineage Progression in Cerebral Cortex Development","grant_number":"725780","call_identifier":"H2020"},{"name":"Probing the Reversibility of Autism Spectrum Disorders by Employing in vivo and in vitro Models","_id":"25444568-B435-11E9-9278-68D0E5697425","call_identifier":"H2020","grant_number":"715508"}],"citation":{"apa":"Knaus, L., Basilico, B., Malzl, D., Gerykova Bujalkova, M., Smogavec, M., Schwarz, L. A., … Novarino, G. (2023). Large neutral amino acid levels tune perinatal neuronal excitability and survival. <i>Cell</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.cell.2023.02.037\">https://doi.org/10.1016/j.cell.2023.02.037</a>","ista":"Knaus L, Basilico B, Malzl D, Gerykova Bujalkova M, Smogavec M, Schwarz LA, Gorkiewicz S, Amberg N, Pauler F, Knittl-Frank C, Tassinari M, Maulide N, Rülicke T, Menche J, Hippenmeyer S, Novarino G. 2023. Large neutral amino acid levels tune perinatal neuronal excitability and survival. Cell. 186(9), 1950–1967.e25.","short":"L. Knaus, B. Basilico, D. Malzl, M. Gerykova Bujalkova, M. Smogavec, L.A. Schwarz, S. Gorkiewicz, N. Amberg, F. Pauler, C. Knittl-Frank, M. Tassinari, N. Maulide, T. Rülicke, J. Menche, S. Hippenmeyer, G. Novarino, Cell 186 (2023) 1950–1967.e25.","mla":"Knaus, Lisa, et al. “Large Neutral Amino Acid Levels Tune Perinatal Neuronal Excitability and Survival.” <i>Cell</i>, vol. 186, no. 9, Elsevier, 2023, p. 1950–1967.e25, doi:<a href=\"https://doi.org/10.1016/j.cell.2023.02.037\">10.1016/j.cell.2023.02.037</a>.","ama":"Knaus L, Basilico B, Malzl D, et al. Large neutral amino acid levels tune perinatal neuronal excitability and survival. <i>Cell</i>. 2023;186(9):1950-1967.e25. doi:<a href=\"https://doi.org/10.1016/j.cell.2023.02.037\">10.1016/j.cell.2023.02.037</a>","chicago":"Knaus, Lisa, Bernadette Basilico, Daniel Malzl, Maria Gerykova Bujalkova, Mateja Smogavec, Lena A. Schwarz, Sarah Gorkiewicz, et al. “Large Neutral Amino Acid Levels Tune Perinatal Neuronal Excitability and Survival.” <i>Cell</i>. Elsevier, 2023. <a href=\"https://doi.org/10.1016/j.cell.2023.02.037\">https://doi.org/10.1016/j.cell.2023.02.037</a>.","ieee":"L. Knaus <i>et al.</i>, “Large neutral amino acid levels tune perinatal neuronal excitability and survival,” <i>Cell</i>, vol. 186, no. 9. Elsevier, p. 1950–1967.e25, 2023."},"has_accepted_license":"1","issue":"9","scopus_import":"1"},{"day":"22","publication_status":"published","page":"6313-6325.e18","oa_version":"Preprint","abstract":[{"lang":"eng","text":"How tissues acquire complex shapes is a fundamental question in biology and regenerative medicine. Zebrafish semicircular canals form from invaginations in the otic epithelium (buds) that extend and fuse to form the hubs of each canal. We find that conventional actomyosin-driven behaviors are not required. Instead, local secretion of hyaluronan, made by the enzymes uridine 5′-diphosphate dehydrogenase (ugdh) and hyaluronan synthase 3 (has3), drives canal morphogenesis. Charged hyaluronate polymers osmotically swell with water and generate isotropic extracellular pressure to deform the overlying epithelium into buds. The mechanical anisotropy needed to shape buds into tubes is conferred by a polarized distribution of actomyosin and E-cadherin-rich membrane tethers, which we term cytocinches. Most work on tissue morphogenesis ascribes actomyosin contractility as the driving force, while the extracellular matrix shapes tissues through differential stiffness. Our work inverts this expectation. Hyaluronate pressure shaped by anisotropic tissue stiffness may be a widespread mechanism for powering morphological change in organogenesis and tissue engineering."}],"status":"public","date_updated":"2023-08-17T06:28:25Z","publication":"Cell","title":"Extracellular hyaluronate pressure shaped by cellular tethers drives tissue morphogenesis","external_id":{"isi":["000735387500002"]},"main_file_link":[{"open_access":"1","url":"https://www.biorxiv.org/content/10.1101/2020.09.28.316042"}],"scopus_import":"1","issue":"26","citation":{"ama":"Munjal A, Hannezo EB, Tsai TYC, Mitchison TJ, Megason SG. Extracellular hyaluronate pressure shaped by cellular tethers drives tissue morphogenesis. <i>Cell</i>. 2021;184(26):6313-6325.e18. doi:<a href=\"https://doi.org/10.1016/j.cell.2021.11.025\">10.1016/j.cell.2021.11.025</a>","ista":"Munjal A, Hannezo EB, Tsai TYC, Mitchison TJ, Megason SG. 2021. Extracellular hyaluronate pressure shaped by cellular tethers drives tissue morphogenesis. Cell. 184(26), 6313–6325.e18.","apa":"Munjal, A., Hannezo, E. B., Tsai, T. Y. C., Mitchison, T. J., &#38; Megason, S. G. (2021). Extracellular hyaluronate pressure shaped by cellular tethers drives tissue morphogenesis. <i>Cell</i>. Elsevier ; Cell Press. <a href=\"https://doi.org/10.1016/j.cell.2021.11.025\">https://doi.org/10.1016/j.cell.2021.11.025</a>","short":"A. Munjal, E.B. Hannezo, T.Y.C. Tsai, T.J. Mitchison, S.G. Megason, Cell 184 (2021) 6313–6325.e18.","mla":"Munjal, Akankshi, et al. “Extracellular Hyaluronate Pressure Shaped by Cellular Tethers Drives Tissue Morphogenesis.” <i>Cell</i>, vol. 184, no. 26, Elsevier ; Cell Press, 2021, p. 6313–6325.e18, doi:<a href=\"https://doi.org/10.1016/j.cell.2021.11.025\">10.1016/j.cell.2021.11.025</a>.","ieee":"A. Munjal, E. B. Hannezo, T. Y. C. Tsai, T. J. Mitchison, and S. G. Megason, “Extracellular hyaluronate pressure shaped by cellular tethers drives tissue morphogenesis,” <i>Cell</i>, vol. 184, no. 26. Elsevier ; Cell Press, p. 6313–6325.e18, 2021.","chicago":"Munjal, Akankshi, Edouard B Hannezo, Tony Y.C. Tsai, Timothy J. Mitchison, and Sean G. Megason. “Extracellular Hyaluronate Pressure Shaped by Cellular Tethers Drives Tissue Morphogenesis.” <i>Cell</i>. Elsevier ; Cell Press, 2021. <a href=\"https://doi.org/10.1016/j.cell.2021.11.025\">https://doi.org/10.1016/j.cell.2021.11.025</a>."},"date_published":"2021-12-22T00:00:00Z","author":[{"first_name":"Akankshi","full_name":"Munjal, Akankshi","last_name":"Munjal"},{"orcid":"0000-0001-6005-1561","id":"3A9DB764-F248-11E8-B48F-1D18A9856A87","last_name":"Hannezo","first_name":"Edouard B","full_name":"Hannezo, Edouard B"},{"last_name":"Tsai","full_name":"Tsai, Tony Y.C.","first_name":"Tony Y.C."},{"last_name":"Mitchison","full_name":"Mitchison, Timothy J.","first_name":"Timothy J."},{"full_name":"Megason, Sean G.","first_name":"Sean G.","last_name":"Megason"}],"_id":"10573","oa":1,"type":"journal_article","doi":"10.1016/j.cell.2021.11.025","language":[{"iso":"eng"}],"year":"2021","publisher":"Elsevier ; Cell Press","isi":1,"volume":184,"article_type":"original","month":"12","publication_identifier":{"eissn":["1097-4172"],"issn":["0092-8674"]},"quality_controlled":"1","article_processing_charge":"No","user_id":"4359f0d1-fa6c-11eb-b949-802e58b17ae8","intvolume":"       184","date_created":"2021-12-26T23:01:26Z","department":[{"_id":"EdHa"}],"acknowledgement":"We thank Ian Swinburne, Sandy Nandagopal, and Toru Kawanishi for support, discussions, and reagents. We thank Vanessa Barone, Joseph Nasser, and members of the Megason lab for useful comments on the manuscript and general feedback. We are grateful to the Heisenberg and Knaut labs for transgenic fish. Diagrams on the right in the graphical abstract were created using BioRender. This work was supported by NIH R01DC015478 and NIH R01GM107733 to S.G.M. A.M. was supported by Human Frontiers Science Program LTF and NIH K99HD098918."},{"doi":"10.1016/j.cell.2020.07.021","language":[{"iso":"eng"}],"year":"2020","publisher":"Elsevier","type":"journal_article","author":[{"full_name":"Pfitzner, Anna-Katharina","first_name":"Anna-Katharina","last_name":"Pfitzner"},{"first_name":"Vincent","full_name":"Mercier, Vincent","last_name":"Mercier"},{"full_name":"Jiang, Xiuyun","first_name":"Xiuyun","last_name":"Jiang"},{"full_name":"Moser von Filseck, Joachim","first_name":"Joachim","last_name":"Moser von Filseck"},{"first_name":"Buzz","full_name":"Baum, Buzz","last_name":"Baum"},{"id":"bf63d406-f056-11eb-b41d-f263a6566d8b","last_name":"Šarić","orcid":"0000-0002-7854-2139","full_name":"Šarić, Anđela","first_name":"Anđela"},{"first_name":"Aurélien","full_name":"Roux, Aurélien","last_name":"Roux"}],"_id":"10348","oa":1,"date_published":"2020-08-18T00:00:00Z","date_created":"2021-11-26T08:02:27Z","acknowledgement":"The authors thank Nicolas Chiaruttini, Jean Gruenberg, and Lena Harker-Kirschneck for careful correction of this manuscript and helpful discussions. The authors want to thank the NCCR Chemical Biology for constant support during this project. A.R. acknowledges funding from the Swiss National Fund for Research (31003A_130520, 31003A_149975, and 31003A_173087) and the European Research Council Consolidator (311536). A.Š. acknowledges the European Research Council (802960). B.B. thanks the BBSRC (BB/K009001/1) and Wellcome Trust (203276/Z/16/Z) for support. J.M.v.F. acknowledges funding through an EMBO Long-Term Fellowship (ALTF 1065-2015), the European Commission FP7 (Marie Curie Actions, LTFCOFUND2013, and GA-2013-609409), and a Transitional Postdoc fellowship (2015/345) from the Swiss SystemsX.ch initiative, evaluated by the Swiss National Science Foundation and Swiss National Science Foundation Research (SNSF SINERGIA 160728/1 [leader, Sophie Martin]).","pmid":1,"article_processing_charge":"No","user_id":"8b945eb4-e2f2-11eb-945a-df72226e66a9","extern":"1","intvolume":"       182","keyword":["general biochemistry","genetics and molecular biology"],"month":"08","publication_identifier":{"issn":["0092-8674"]},"quality_controlled":"1","article_type":"original","volume":182,"date_updated":"2021-11-26T08:58:37Z","status":"public","day":"18","oa_version":"Published Version","publication_status":"published","page":"1140-1155.e18","abstract":[{"text":"The endosomal sorting complex required for transport-III (ESCRT-III) catalyzes membrane fission from within membrane necks, a process that is essential for many cellular functions, from cell division to lysosome degradation and autophagy. How it breaks membranes, though, remains unknown. Here, we characterize a sequential polymerization of ESCRT-III subunits that, driven by a recruitment cascade and by continuous subunit-turnover powered by the ATPase Vps4, induces membrane deformation and fission. During this process, the exchange of Vps24 for Did2 induces a tilt in the polymer-membrane interface, which triggers transition from flat spiral polymers to helical filament to drive the formation of membrane protrusions, and ends with the formation of a highly constricted Did2-Ist1 co-polymer that we show is competent to promote fission when bound on the inside of membrane necks. Overall, our results suggest a mechanism of stepwise changes in ESCRT-III filament structure and mechanical properties via exchange of the filament subunits to catalyze ESCRT-III activity.","lang":"eng"}],"citation":{"chicago":"Pfitzner, Anna-Katharina, Vincent Mercier, Xiuyun Jiang, Joachim Moser von Filseck, Buzz Baum, Anđela Šarić, and Aurélien Roux. “An ESCRT-III Polymerization Sequence Drives Membrane Deformation and Fission.” <i>Cell</i>. Elsevier, 2020. <a href=\"https://doi.org/10.1016/j.cell.2020.07.021\">https://doi.org/10.1016/j.cell.2020.07.021</a>.","ieee":"A.-K. Pfitzner <i>et al.</i>, “An ESCRT-III polymerization sequence drives membrane deformation and fission,” <i>Cell</i>, vol. 182, no. 5. Elsevier, p. 1140–1155.e18, 2020.","apa":"Pfitzner, A.-K., Mercier, V., Jiang, X., Moser von Filseck, J., Baum, B., Šarić, A., &#38; Roux, A. (2020). An ESCRT-III polymerization sequence drives membrane deformation and fission. <i>Cell</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.cell.2020.07.021\">https://doi.org/10.1016/j.cell.2020.07.021</a>","mla":"Pfitzner, Anna-Katharina, et al. “An ESCRT-III Polymerization Sequence Drives Membrane Deformation and Fission.” <i>Cell</i>, vol. 182, no. 5, Elsevier, 2020, p. 1140–1155.e18, doi:<a href=\"https://doi.org/10.1016/j.cell.2020.07.021\">10.1016/j.cell.2020.07.021</a>.","ista":"Pfitzner A-K, Mercier V, Jiang X, Moser von Filseck J, Baum B, Šarić A, Roux A. 2020. An ESCRT-III polymerization sequence drives membrane deformation and fission. Cell. 182(5), 1140–1155.e18.","short":"A.-K. Pfitzner, V. Mercier, X. Jiang, J. Moser von Filseck, B. Baum, A. Šarić, A. Roux, Cell 182 (2020) 1140–1155.e18.","ama":"Pfitzner A-K, Mercier V, Jiang X, et al. An ESCRT-III polymerization sequence drives membrane deformation and fission. <i>Cell</i>. 2020;182(5):1140-1155.e18. doi:<a href=\"https://doi.org/10.1016/j.cell.2020.07.021\">10.1016/j.cell.2020.07.021</a>"},"scopus_import":"1","issue":"5","main_file_link":[{"url":"https://www.sciencedirect.com/science/article/pii/S0092867420309296","open_access":"1"}],"publication":"Cell","title":"An ESCRT-III polymerization sequence drives membrane deformation and fission","external_id":{"pmid":["32814015"]}},{"citation":{"ieee":"A. Kopf and M. K. Sixt, “The neural crest pitches in to remove apoptotic debris,” <i>Cell</i>, vol. 179, no. 1. Elsevier, pp. 51–53, 2019.","chicago":"Kopf, Aglaja, and Michael K Sixt. “The Neural Crest Pitches in to Remove Apoptotic Debris.” <i>Cell</i>. Elsevier, 2019. <a href=\"https://doi.org/10.1016/j.cell.2019.08.047\">https://doi.org/10.1016/j.cell.2019.08.047</a>.","ama":"Kopf A, Sixt MK. The neural crest pitches in to remove apoptotic debris. <i>Cell</i>. 2019;179(1):51-53. doi:<a href=\"https://doi.org/10.1016/j.cell.2019.08.047\">10.1016/j.cell.2019.08.047</a>","apa":"Kopf, A., &#38; Sixt, M. K. (2019). The neural crest pitches in to remove apoptotic debris. <i>Cell</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.cell.2019.08.047\">https://doi.org/10.1016/j.cell.2019.08.047</a>","ista":"Kopf A, Sixt MK. 2019. The neural crest pitches in to remove apoptotic debris. Cell. 179(1), 51–53.","short":"A. Kopf, M.K. Sixt, Cell 179 (2019) 51–53.","mla":"Kopf, Aglaja, and Michael K. Sixt. “The Neural Crest Pitches in to Remove Apoptotic Debris.” <i>Cell</i>, vol. 179, no. 1, Elsevier, 2019, pp. 51–53, doi:<a href=\"https://doi.org/10.1016/j.cell.2019.08.047\">10.1016/j.cell.2019.08.047</a>."},"issue":"1","scopus_import":"1","publication":"Cell","external_id":{"isi":["000486618500011"],"pmid":["31539498"]},"related_material":{"record":[{"status":"public","id":"6891","relation":"dissertation_contains"}]},"title":"The neural crest pitches in to remove apoptotic debris","date_updated":"2024-03-25T23:30:22Z","status":"public","oa_version":"None","publication_status":"published","page":"51-53","day":"19","date_created":"2019-09-15T22:00:46Z","pmid":1,"department":[{"_id":"MiSi"}],"article_processing_charge":"No","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","intvolume":"       179","month":"09","quality_controlled":"1","publication_identifier":{"issn":["0092-8674"],"eissn":["1097-4172"]},"isi":1,"article_type":"original","volume":179,"language":[{"iso":"eng"}],"doi":"10.1016/j.cell.2019.08.047","publisher":"Elsevier","year":"2019","type":"journal_article","author":[{"id":"31DAC7B6-F248-11E8-B48F-1D18A9856A87","last_name":"Kopf","orcid":"0000-0002-2187-6656","first_name":"Aglaja","full_name":"Kopf, Aglaja"},{"orcid":"0000-0002-6620-9179","last_name":"Sixt","id":"41E9FBEA-F248-11E8-B48F-1D18A9856A87","full_name":"Sixt, Michael K","first_name":"Michael K"}],"_id":"6877","date_published":"2019-09-19T00:00:00Z"},{"isi":1,"volume":179,"article_type":"original","month":"10","publication_identifier":{"eissn":["1097-4172"],"issn":["0092-8674"]},"quality_controlled":"1","file_date_updated":"2020-10-21T07:09:45Z","user_id":"4359f0d1-fa6c-11eb-b949-802e58b17ae8","article_processing_charge":"No","ddc":["570"],"intvolume":"       179","date_created":"2019-11-12T12:51:06Z","department":[{"_id":"CaHe"},{"_id":"BjHo"}],"pmid":1,"date_published":"2019-10-31T00:00:00Z","author":[{"first_name":"Cornelia","full_name":"Schwayer, Cornelia","orcid":"0000-0001-5130-2226","last_name":"Schwayer","id":"3436488C-F248-11E8-B48F-1D18A9856A87"},{"last_name":"Shamipour","id":"40B34FE2-F248-11E8-B48F-1D18A9856A87","full_name":"Shamipour, Shayan","first_name":"Shayan"},{"last_name":"Pranjic-Ferscha","id":"4362B3C2-F248-11E8-B48F-1D18A9856A87","first_name":"Kornelija","full_name":"Pranjic-Ferscha, Kornelija"},{"id":"30A536BA-F248-11E8-B48F-1D18A9856A87","last_name":"Schauer","orcid":"0000-0001-7659-9142","first_name":"Alexandra","full_name":"Schauer, Alexandra"},{"last_name":"Balda","first_name":"M","full_name":"Balda, M"},{"first_name":"M","full_name":"Tada, M","last_name":"Tada"},{"full_name":"Matter, K","first_name":"K","last_name":"Matter"},{"first_name":"Carl-Philipp J","full_name":"Heisenberg, Carl-Philipp J","orcid":"0000-0002-0912-4566","id":"39427864-F248-11E8-B48F-1D18A9856A87","last_name":"Heisenberg"}],"_id":"7001","oa":1,"type":"journal_article","doi":"10.1016/j.cell.2019.10.006","language":[{"iso":"eng"}],"year":"2019","publisher":"Cell Press","publication":"Cell","title":"Mechanosensation of tight junctions depends on ZO-1 phase separation and flow","file":[{"creator":"dernst","relation":"main_file","content_type":"application/pdf","access_level":"open_access","file_size":8805878,"file_name":"2019_Cell_Schwayer_accepted.pdf","date_updated":"2020-10-21T07:09:45Z","success":1,"checksum":"33dac4bb77ee630e2666e936b4d57980","file_id":"8684","date_created":"2020-10-21T07:09:45Z"}],"external_id":{"isi":["000493898000012"],"pmid":["31675500"]},"related_material":{"record":[{"relation":"dissertation_contains","status":"public","id":"7186"},{"relation":"dissertation_contains","status":"public","id":"8350"}],"link":[{"url":"https://ist.ac.at/en/news/biochemistry-meets-mechanics-the-sensitive-nature-of-cell-cell-contact-formation-in-embryo-development/","relation":"press_release","description":"News auf IST Website"}]},"scopus_import":"1","issue":"4","has_accepted_license":"1","citation":{"ieee":"C. Schwayer <i>et al.</i>, “Mechanosensation of tight junctions depends on ZO-1 phase separation and flow,” <i>Cell</i>, vol. 179, no. 4. Cell Press, p. 937–952.e18, 2019.","chicago":"Schwayer, Cornelia, Shayan Shamipour, Kornelija Pranjic-Ferscha, Alexandra Schauer, M Balda, M Tada, K Matter, and Carl-Philipp J Heisenberg. “Mechanosensation of Tight Junctions Depends on ZO-1 Phase Separation and Flow.” <i>Cell</i>. Cell Press, 2019. <a href=\"https://doi.org/10.1016/j.cell.2019.10.006\">https://doi.org/10.1016/j.cell.2019.10.006</a>.","ama":"Schwayer C, Shamipour S, Pranjic-Ferscha K, et al. Mechanosensation of tight junctions depends on ZO-1 phase separation and flow. <i>Cell</i>. 2019;179(4):937-952.e18. doi:<a href=\"https://doi.org/10.1016/j.cell.2019.10.006\">10.1016/j.cell.2019.10.006</a>","short":"C. Schwayer, S. Shamipour, K. Pranjic-Ferscha, A. Schauer, M. Balda, M. Tada, K. Matter, C.-P.J. Heisenberg, Cell 179 (2019) 937–952.e18.","mla":"Schwayer, Cornelia, et al. “Mechanosensation of Tight Junctions Depends on ZO-1 Phase Separation and Flow.” <i>Cell</i>, vol. 179, no. 4, Cell Press, 2019, p. 937–952.e18, doi:<a href=\"https://doi.org/10.1016/j.cell.2019.10.006\">10.1016/j.cell.2019.10.006</a>.","apa":"Schwayer, C., Shamipour, S., Pranjic-Ferscha, K., Schauer, A., Balda, M., Tada, M., … Heisenberg, C.-P. J. (2019). Mechanosensation of tight junctions depends on ZO-1 phase separation and flow. <i>Cell</i>. Cell Press. <a href=\"https://doi.org/10.1016/j.cell.2019.10.006\">https://doi.org/10.1016/j.cell.2019.10.006</a>","ista":"Schwayer C, Shamipour S, Pranjic-Ferscha K, Schauer A, Balda M, Tada M, Matter K, Heisenberg C-PJ. 2019. Mechanosensation of tight junctions depends on ZO-1 phase separation and flow. Cell. 179(4), 937–952.e18."},"project":[{"grant_number":"742573","call_identifier":"H2020","_id":"260F1432-B435-11E9-9278-68D0E5697425","name":"Interaction and feedback between cell mechanics and fate specification in vertebrate gastrulation"}],"day":"31","publication_status":"published","oa_version":"Submitted Version","page":"937-952.e18","ec_funded":1,"status":"public","acknowledged_ssus":[{"_id":"PreCl"},{"_id":"Bio"}],"date_updated":"2024-03-25T23:30:21Z"},{"status":"public","type":"journal_article","doi":"10.1016/j.cell.2018.10.039","language":[{"iso":"eng"}],"year":"2018","date_updated":"2021-01-12T08:19:15Z","publisher":"Elsevier","day":"15","page":"1365-1379.e25","date_published":"2018-11-15T00:00:00Z","oa_version":"None","publication_status":"published","abstract":[{"text":"The exchange of metabolites between the mitochondrial matrix and the cytosol depends on β-barrel channels in the outer membrane and α-helical carrier proteins in the inner membrane. The essential translocase of the inner membrane (TIM) chaperones escort these proteins through the intermembrane space, but the structural and mechanistic details remain elusive. We have used an integrated structural biology approach to reveal the functional principle of TIM chaperones. Multiple clamp-like binding sites hold the mitochondrial membrane proteins in a translocation-competent elongated form, thus mimicking characteristics of co-translational membrane insertion. The bound preprotein undergoes conformational dynamics within the chaperone binding clefts, pointing to a multitude of dynamic local binding events. Mutations in these binding sites cause cell death or growth defects associated with impairment of carrier and β-barrel protein biogenesis. Our work reveals how a single mitochondrial “transfer-chaperone” system is able to guide α-helical and β-barrel membrane proteins in a “nascent chain-like” conformation through a ribosome-free compartment.","lang":"eng"}],"author":[{"last_name":"Weinhäupl","first_name":"Katharina","full_name":"Weinhäupl, Katharina"},{"full_name":"Lindau, Caroline","first_name":"Caroline","last_name":"Lindau"},{"last_name":"Hessel","first_name":"Audrey","full_name":"Hessel, Audrey"},{"last_name":"Wang","full_name":"Wang, Yong","first_name":"Yong"},{"last_name":"Schütze","first_name":"Conny","full_name":"Schütze, Conny"},{"last_name":"Jores","first_name":"Tobias","full_name":"Jores, Tobias"},{"last_name":"Melchionda","full_name":"Melchionda, Laura","first_name":"Laura"},{"last_name":"Schönfisch","first_name":"Birgit","full_name":"Schönfisch, Birgit"},{"last_name":"Kalbacher","full_name":"Kalbacher, Hubert","first_name":"Hubert"},{"first_name":"Beate","full_name":"Bersch, Beate","last_name":"Bersch"},{"last_name":"Rapaport","full_name":"Rapaport, Doron","first_name":"Doron"},{"last_name":"Brennich","full_name":"Brennich, Martha","first_name":"Martha"},{"full_name":"Lindorff-Larsen, Kresten","first_name":"Kresten","last_name":"Lindorff-Larsen"},{"full_name":"Wiedemann, Nils","first_name":"Nils","last_name":"Wiedemann"},{"full_name":"Schanda, Paul","first_name":"Paul","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","last_name":"Schanda","orcid":"0000-0002-9350-7606"}],"_id":"8436","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","article_processing_charge":"No","extern":"1","issue":"5","intvolume":"       175","keyword":["General Biochemistry","Genetics and Molecular Biology"],"date_created":"2020-09-18T10:04:39Z","citation":{"ama":"Weinhäupl K, Lindau C, Hessel A, et al. Structural basis of membrane protein chaperoning through the mitochondrial intermembrane space. <i>Cell</i>. 2018;175(5):1365-1379.e25. doi:<a href=\"https://doi.org/10.1016/j.cell.2018.10.039\">10.1016/j.cell.2018.10.039</a>","apa":"Weinhäupl, K., Lindau, C., Hessel, A., Wang, Y., Schütze, C., Jores, T., … Schanda, P. (2018). Structural basis of membrane protein chaperoning through the mitochondrial intermembrane space. <i>Cell</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.cell.2018.10.039\">https://doi.org/10.1016/j.cell.2018.10.039</a>","ista":"Weinhäupl K, Lindau C, Hessel A, Wang Y, Schütze C, Jores T, Melchionda L, Schönfisch B, Kalbacher H, Bersch B, Rapaport D, Brennich M, Lindorff-Larsen K, Wiedemann N, Schanda P. 2018. Structural basis of membrane protein chaperoning through the mitochondrial intermembrane space. Cell. 175(5), 1365–1379.e25.","mla":"Weinhäupl, Katharina, et al. “Structural Basis of Membrane Protein Chaperoning through the Mitochondrial Intermembrane Space.” <i>Cell</i>, vol. 175, no. 5, Elsevier, 2018, p. 1365–1379.e25, doi:<a href=\"https://doi.org/10.1016/j.cell.2018.10.039\">10.1016/j.cell.2018.10.039</a>.","short":"K. Weinhäupl, C. Lindau, A. Hessel, Y. Wang, C. Schütze, T. Jores, L. Melchionda, B. Schönfisch, H. Kalbacher, B. Bersch, D. Rapaport, M. Brennich, K. Lindorff-Larsen, N. Wiedemann, P. Schanda, Cell 175 (2018) 1365–1379.e25.","ieee":"K. Weinhäupl <i>et al.</i>, “Structural basis of membrane protein chaperoning through the mitochondrial intermembrane space,” <i>Cell</i>, vol. 175, no. 5. Elsevier, p. 1365–1379.e25, 2018.","chicago":"Weinhäupl, Katharina, Caroline Lindau, Audrey Hessel, Yong Wang, Conny Schütze, Tobias Jores, Laura Melchionda, et al. “Structural Basis of Membrane Protein Chaperoning through the Mitochondrial Intermembrane Space.” <i>Cell</i>. Elsevier, 2018. <a href=\"https://doi.org/10.1016/j.cell.2018.10.039\">https://doi.org/10.1016/j.cell.2018.10.039</a>."},"publication":"Cell","title":"Structural basis of membrane protein chaperoning through the mitochondrial intermembrane space","article_type":"original","volume":175,"month":"11","publication_identifier":{"issn":["0092-8674"]},"quality_controlled":"1"},{"_id":"11073","oa":1,"author":[{"full_name":"Hatch, Emily M.","first_name":"Emily M.","last_name":"Hatch"},{"id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","last_name":"HETZER","orcid":"0000-0002-2111-992X","full_name":"HETZER, Martin W","first_name":"Martin W"}],"date_published":"2015-06-18T00:00:00Z","year":"2015","publisher":"Elsevier","doi":"10.1016/j.cell.2015.06.005","language":[{"iso":"eng"}],"type":"journal_article","publication_identifier":{"issn":["0092-8674"]},"quality_controlled":"1","month":"06","article_type":"original","volume":161,"pmid":1,"date_created":"2022-04-07T07:48:49Z","intvolume":"       161","keyword":["General Biochemistry","Genetics and Molecular Biology"],"article_processing_charge":"No","extern":"1","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","abstract":[{"lang":"eng","text":"Human cancer cells bear complex chromosome rearrangements that can be potential drivers of cancer development. However, the molecular mechanisms underlying these rearrangements have been unclear. Zhang et al. use a new technique combining live-cell imaging and single-cell sequencing to demonstrate that chromosomes mis-segregated to micronuclei frequently undergo chromothripsis-like rearrangements in the subsequent cell cycle."}],"day":"18","oa_version":"Published Version","publication_status":"published","page":"1502-1504","date_updated":"2022-07-18T08:34:33Z","status":"public","main_file_link":[{"url":"https://doi.org/10.1016/j.cell.2015.06.005","open_access":"1"}],"title":"Linking micronuclei to chromosome fragmentation","external_id":{"pmid":["26091034"]},"publication":"Cell","citation":{"ieee":"E. M. Hatch and M. Hetzer, “Linking micronuclei to chromosome fragmentation,” <i>Cell</i>, vol. 161, no. 7. Elsevier, pp. 1502–1504, 2015.","chicago":"Hatch, Emily M., and Martin Hetzer. “Linking Micronuclei to Chromosome Fragmentation.” <i>Cell</i>. Elsevier, 2015. <a href=\"https://doi.org/10.1016/j.cell.2015.06.005\">https://doi.org/10.1016/j.cell.2015.06.005</a>.","ama":"Hatch EM, Hetzer M. Linking micronuclei to chromosome fragmentation. <i>Cell</i>. 2015;161(7):1502-1504. doi:<a href=\"https://doi.org/10.1016/j.cell.2015.06.005\">10.1016/j.cell.2015.06.005</a>","apa":"Hatch, E. M., &#38; Hetzer, M. (2015). Linking micronuclei to chromosome fragmentation. <i>Cell</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.cell.2015.06.005\">https://doi.org/10.1016/j.cell.2015.06.005</a>","mla":"Hatch, Emily M., and Martin Hetzer. “Linking Micronuclei to Chromosome Fragmentation.” <i>Cell</i>, vol. 161, no. 7, Elsevier, 2015, pp. 1502–04, doi:<a href=\"https://doi.org/10.1016/j.cell.2015.06.005\">10.1016/j.cell.2015.06.005</a>.","ista":"Hatch EM, Hetzer M. 2015. Linking micronuclei to chromosome fragmentation. Cell. 161(7), 1502–1504.","short":"E.M. Hatch, M. Hetzer, Cell 161 (2015) 1502–1504."},"scopus_import":"1","issue":"7"},{"publication":"Cell","title":"Nuclear pores set the speed limit for mitosis","external_id":{"pmid":["24581486"]},"main_file_link":[{"url":"https://doi.org/10.1016/j.cell.2014.02.004","open_access":"1"}],"scopus_import":"1","issue":"5","citation":{"ista":"Buchwalter A, Hetzer M. 2014. Nuclear pores set the speed limit for mitosis. Cell. 156(5), 868–869.","short":"A. Buchwalter, M. Hetzer, Cell 156 (2014) 868–869.","mla":"Buchwalter, Abigail, and Martin Hetzer. “Nuclear Pores Set the Speed Limit for Mitosis.” <i>Cell</i>, vol. 156, no. 5, Elsevier, 2014, pp. 868–69, doi:<a href=\"https://doi.org/10.1016/j.cell.2014.02.004\">10.1016/j.cell.2014.02.004</a>.","apa":"Buchwalter, A., &#38; Hetzer, M. (2014). Nuclear pores set the speed limit for mitosis. <i>Cell</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.cell.2014.02.004\">https://doi.org/10.1016/j.cell.2014.02.004</a>","ama":"Buchwalter A, Hetzer M. Nuclear pores set the speed limit for mitosis. <i>Cell</i>. 2014;156(5):868-869. doi:<a href=\"https://doi.org/10.1016/j.cell.2014.02.004\">10.1016/j.cell.2014.02.004</a>","chicago":"Buchwalter, Abigail, and Martin Hetzer. “Nuclear Pores Set the Speed Limit for Mitosis.” <i>Cell</i>. Elsevier, 2014. <a href=\"https://doi.org/10.1016/j.cell.2014.02.004\">https://doi.org/10.1016/j.cell.2014.02.004</a>.","ieee":"A. Buchwalter and M. Hetzer, “Nuclear pores set the speed limit for mitosis,” <i>Cell</i>, vol. 156, no. 5. Elsevier, pp. 868–869, 2014."},"day":"27","publication_status":"published","oa_version":"Published Version","page":"868-869","abstract":[{"lang":"eng","text":"The spindle assembly checkpoint prevents separation of sister chromatids until each kinetochore is attached to the mitotic spindle. Rodriguez-Bravo et al. report that the nuclear pore complex scaffolds spindle assembly checkpoint signaling in interphase, providing a store of inhibitory signals that limits the speed of the subsequent mitosis."}],"status":"public","date_updated":"2022-07-18T08:44:33Z","article_type":"original","volume":156,"month":"02","publication_identifier":{"issn":["0092-8674"]},"quality_controlled":"1","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","article_processing_charge":"No","extern":"1","intvolume":"       156","keyword":["General Biochemistry","Genetics and Molecular Biology"],"date_created":"2022-04-07T07:50:04Z","pmid":1,"date_published":"2014-02-27T00:00:00Z","author":[{"last_name":"Buchwalter","first_name":"Abigail","full_name":"Buchwalter, Abigail"},{"full_name":"HETZER, Martin W","first_name":"Martin W","last_name":"HETZER","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","orcid":"0000-0002-2111-992X"}],"_id":"11080","oa":1,"type":"journal_article","doi":"10.1016/j.cell.2014.02.004","language":[{"iso":"eng"}],"year":"2014","publisher":"Elsevier"},{"date_published":"2014-01-16T00:00:00Z","_id":"6122","oa":1,"author":[{"full_name":"Linneweber, Gerit A.","first_name":"Gerit A.","last_name":"Linneweber"},{"full_name":"Jacobson, Jake","first_name":"Jake","last_name":"Jacobson"},{"full_name":"Busch, Karl Emanuel","first_name":"Karl Emanuel","last_name":"Busch"},{"first_name":"Bruno","full_name":"Hudry, Bruno","last_name":"Hudry"},{"full_name":"Christov, Christo P.","first_name":"Christo P.","last_name":"Christov"},{"first_name":"Dirk","full_name":"Dormann, Dirk","last_name":"Dormann"},{"first_name":"Michaela","full_name":"Yuan, Michaela","last_name":"Yuan"},{"full_name":"Otani, Tomoki","first_name":"Tomoki","last_name":"Otani"},{"full_name":"Knust, Elisabeth","first_name":"Elisabeth","last_name":"Knust"},{"full_name":"de Bono, Mario","first_name":"Mario","last_name":"de Bono","id":"4E3FF80E-F248-11E8-B48F-1D18A9856A87","orcid":"0000-0001-8347-0443"},{"last_name":"Miguel-Aliaga","first_name":"Irene","full_name":"Miguel-Aliaga, Irene"}],"type":"journal_article","year":"2014","publisher":"Elsevier","doi":"10.1016/j.cell.2013.12.008","language":[{"iso":"eng"}],"volume":156,"publication_identifier":{"issn":["0092-8674"]},"quality_controlled":"1","month":"01","intvolume":"       156","file_date_updated":"2020-07-14T12:47:20Z","extern":"1","ddc":["570"],"user_id":"3E5EF7F0-F248-11E8-B48F-1D18A9856A87","pmid":1,"date_created":"2019-03-19T14:35:30Z","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)"},"day":"16","oa_version":"Published Version","page":"69-83","publication_status":"published","status":"public","date_updated":"2021-01-12T08:06:13Z","title":"Neuronal control of metabolism through nutrient-dependent modulation of tracheal branching","file":[{"creator":"kschuh","relation":"main_file","content_type":"application/pdf","access_level":"open_access","file_size":5020084,"file_name":"2014_Elsevier_Linneweber.pdf","date_updated":"2020-07-14T12:47:20Z","checksum":"ad6ef68f37fb711d9abcd97fc06ad316","date_created":"2019-03-19T14:40:38Z","file_id":"6123"}],"external_id":{"pmid":["24439370"]},"publication":"Cell","has_accepted_license":"1","issue":"1-2","citation":{"apa":"Linneweber, G. A., Jacobson, J., Busch, K. E., Hudry, B., Christov, C. P., Dormann, D., … Miguel-Aliaga, I. (2014). Neuronal control of metabolism through nutrient-dependent modulation of tracheal branching. <i>Cell</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.cell.2013.12.008\">https://doi.org/10.1016/j.cell.2013.12.008</a>","ista":"Linneweber GA, Jacobson J, Busch KE, Hudry B, Christov CP, Dormann D, Yuan M, Otani T, Knust E, de Bono M, Miguel-Aliaga I. 2014. Neuronal control of metabolism through nutrient-dependent modulation of tracheal branching. Cell. 156(1–2), 69–83.","mla":"Linneweber, Gerit A., et al. “Neuronal Control of Metabolism through Nutrient-Dependent Modulation of Tracheal Branching.” <i>Cell</i>, vol. 156, no. 1–2, Elsevier, 2014, pp. 69–83, doi:<a href=\"https://doi.org/10.1016/j.cell.2013.12.008\">10.1016/j.cell.2013.12.008</a>.","short":"G.A. Linneweber, J. Jacobson, K.E. Busch, B. Hudry, C.P. Christov, D. Dormann, M. Yuan, T. Otani, E. Knust, M. de Bono, I. Miguel-Aliaga, Cell 156 (2014) 69–83.","ama":"Linneweber GA, Jacobson J, Busch KE, et al. Neuronal control of metabolism through nutrient-dependent modulation of tracheal branching. <i>Cell</i>. 2014;156(1-2):69-83. doi:<a href=\"https://doi.org/10.1016/j.cell.2013.12.008\">10.1016/j.cell.2013.12.008</a>","chicago":"Linneweber, Gerit A., Jake Jacobson, Karl Emanuel Busch, Bruno Hudry, Christo P. Christov, Dirk Dormann, Michaela Yuan, et al. “Neuronal Control of Metabolism through Nutrient-Dependent Modulation of Tracheal Branching.” <i>Cell</i>. Elsevier, 2014. <a href=\"https://doi.org/10.1016/j.cell.2013.12.008\">https://doi.org/10.1016/j.cell.2013.12.008</a>.","ieee":"G. A. Linneweber <i>et al.</i>, “Neuronal control of metabolism through nutrient-dependent modulation of tracheal branching,” <i>Cell</i>, vol. 156, no. 1–2. Elsevier, pp. 69–83, 2014."}},{"date_created":"2021-06-04T12:00:16Z","pmid":1,"department":[{"_id":"DaZi"}],"extern":"1","article_processing_charge":"No","user_id":"8b945eb4-e2f2-11eb-945a-df72226e66a9","intvolume":"       156","month":"03","quality_controlled":"1","publication_identifier":{"issn":["0092-8674"],"eissn":["1097-4172"]},"volume":156,"article_type":"original","language":[{"iso":"eng"}],"doi":"10.1016/j.cell.2014.01.029","publisher":"Elsevier","year":"2014","type":"journal_article","author":[{"last_name":"Huff","full_name":"Huff, Jason T.","first_name":"Jason T."},{"first_name":"Daniel","full_name":"Zilberman, Daniel","orcid":"0000-0002-0123-8649","last_name":"Zilberman","id":"6973db13-dd5f-11ea-814e-b3e5455e9ed1"}],"oa":1,"_id":"9458","date_published":"2014-03-13T00:00:00Z","citation":{"ieee":"J. T. Huff and D. Zilberman, “Dnmt1-independent CG methylation contributes to nucleosome positioning in diverse eukaryotes,” <i>Cell</i>, vol. 156, no. 6. Elsevier, pp. 1286–1297, 2014.","chicago":"Huff, Jason T., and Daniel Zilberman. “Dnmt1-Independent CG Methylation Contributes to Nucleosome Positioning in Diverse Eukaryotes.” <i>Cell</i>. Elsevier, 2014. <a href=\"https://doi.org/10.1016/j.cell.2014.01.029\">https://doi.org/10.1016/j.cell.2014.01.029</a>.","ama":"Huff JT, Zilberman D. Dnmt1-independent CG methylation contributes to nucleosome positioning in diverse eukaryotes. <i>Cell</i>. 2014;156(6):1286-1297. doi:<a href=\"https://doi.org/10.1016/j.cell.2014.01.029\">10.1016/j.cell.2014.01.029</a>","ista":"Huff JT, Zilberman D. 2014. Dnmt1-independent CG methylation contributes to nucleosome positioning in diverse eukaryotes. Cell. 156(6), 1286–1297.","apa":"Huff, J. T., &#38; Zilberman, D. (2014). Dnmt1-independent CG methylation contributes to nucleosome positioning in diverse eukaryotes. <i>Cell</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.cell.2014.01.029\">https://doi.org/10.1016/j.cell.2014.01.029</a>","mla":"Huff, Jason T., and Daniel Zilberman. “Dnmt1-Independent CG Methylation Contributes to Nucleosome Positioning in Diverse Eukaryotes.” <i>Cell</i>, vol. 156, no. 6, Elsevier, 2014, pp. 1286–97, doi:<a href=\"https://doi.org/10.1016/j.cell.2014.01.029\">10.1016/j.cell.2014.01.029</a>.","short":"J.T. Huff, D. Zilberman, Cell 156 (2014) 1286–1297."},"issue":"6","scopus_import":"1","main_file_link":[{"open_access":"1","url":"https://doi.org/10.1016/j.cell.2014.01.029"}],"publication":"Cell","external_id":{"pmid":["24630728"]},"title":"Dnmt1-independent CG methylation contributes to nucleosome positioning in diverse eukaryotes","date_updated":"2021-12-14T08:22:36Z","status":"public","oa_version":"Published Version","page":"1286-1297","publication_status":"published","day":"13","abstract":[{"lang":"eng","text":"Dnmt1 epigenetically propagates symmetrical CG methylation in many eukaryotes. Their genomes are typically depleted of CG dinucleotides because of imperfect repair of deaminated methylcytosines. Here, we extensively survey diverse species lacking Dnmt1 and show that, surprisingly, symmetrical CG methylation is nonetheless frequently present and catalyzed by a different DNA methyltransferase family, Dnmt5. Numerous Dnmt5-containing organisms that diverged more than a billion years ago exhibit clustered methylation, specifically in nucleosome linkers. Clustered methylation occurs at unprecedented densities and directly disfavors nucleosomes, contributing to nucleosome positioning between clusters. Dense methylation is enabled by a regime of genomic sequence evolution that enriches CG dinucleotides and drives the highest CG frequencies known. Species with linker methylation have small, transcriptionally active nuclei that approach the physical limits of chromatin compaction. These features constitute a previously unappreciated genome architecture, in which dense methylation influences nucleosome positions, likely facilitating nuclear processes under extreme spatial constraints."}]},{"type":"journal_article","language":[{"iso":"eng"}],"doi":"10.1016/j.cell.2013.06.007","publisher":"Elsevier","year":"2013","date_published":"2013-07-03T00:00:00Z","author":[{"full_name":"Hatch, Emily M.","first_name":"Emily M.","last_name":"Hatch"},{"first_name":"Andrew H.","full_name":"Fischer, Andrew H.","last_name":"Fischer"},{"last_name":"Deerinck","full_name":"Deerinck, Thomas J.","first_name":"Thomas J."},{"id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","last_name":"HETZER","orcid":"0000-0002-2111-992X","first_name":"Martin W","full_name":"HETZER, Martin W"}],"oa":1,"_id":"11085","extern":"1","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","article_processing_charge":"No","keyword":["General Biochemistry","Genetics and Molecular Biology"],"intvolume":"       154","date_created":"2022-04-07T07:50:51Z","pmid":1,"volume":154,"article_type":"original","month":"07","quality_controlled":"1","publication_identifier":{"issn":["0092-8674"]},"status":"public","date_updated":"2022-07-18T08:45:47Z","page":"47-60","publication_status":"published","oa_version":"Published Version","day":"03","abstract":[{"lang":"eng","text":"During mitotic exit, missegregated chromosomes can recruit their own nuclear envelope (NE) to form micronuclei (MN). MN have reduced functioning compared to primary nuclei in the same cell, although the two compartments appear to be structurally comparable. Here we show that over 60% of MN undergo an irreversible loss of compartmentalization during interphase due to NE collapse. This disruption of the MN, which is induced by defects in nuclear lamina assembly, drastically reduces nuclear functions and can trigger massive DNA damage. MN disruption is associated with chromatin compaction and invasion of endoplasmic reticulum (ER) tubules into the chromatin. We identified disrupted MN in both major subtypes of human non-small-cell lung cancer, suggesting that disrupted MN could be a useful objective biomarker for genomic instability in solid tumors. Our study shows that NE collapse is a key event underlying MN dysfunction and establishes a link between aberrant NE organization and aneuploidy."}],"issue":"1","scopus_import":"1","citation":{"ama":"Hatch EM, Fischer AH, Deerinck TJ, Hetzer M. Catastrophic nuclear envelope collapse in cancer cell micronuclei. <i>Cell</i>. 2013;154(1):47-60. doi:<a href=\"https://doi.org/10.1016/j.cell.2013.06.007\">10.1016/j.cell.2013.06.007</a>","short":"E.M. Hatch, A.H. Fischer, T.J. Deerinck, M. Hetzer, Cell 154 (2013) 47–60.","apa":"Hatch, E. M., Fischer, A. H., Deerinck, T. J., &#38; Hetzer, M. (2013). Catastrophic nuclear envelope collapse in cancer cell micronuclei. <i>Cell</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.cell.2013.06.007\">https://doi.org/10.1016/j.cell.2013.06.007</a>","mla":"Hatch, Emily M., et al. “Catastrophic Nuclear Envelope Collapse in Cancer Cell Micronuclei.” <i>Cell</i>, vol. 154, no. 1, Elsevier, 2013, pp. 47–60, doi:<a href=\"https://doi.org/10.1016/j.cell.2013.06.007\">10.1016/j.cell.2013.06.007</a>.","ista":"Hatch EM, Fischer AH, Deerinck TJ, Hetzer M. 2013. Catastrophic nuclear envelope collapse in cancer cell micronuclei. Cell. 154(1), 47–60.","ieee":"E. M. Hatch, A. H. Fischer, T. J. Deerinck, and M. Hetzer, “Catastrophic nuclear envelope collapse in cancer cell micronuclei,” <i>Cell</i>, vol. 154, no. 1. Elsevier, pp. 47–60, 2013.","chicago":"Hatch, Emily M., Andrew H. Fischer, Thomas J. Deerinck, and Martin Hetzer. “Catastrophic Nuclear Envelope Collapse in Cancer Cell Micronuclei.” <i>Cell</i>. Elsevier, 2013. <a href=\"https://doi.org/10.1016/j.cell.2013.06.007\">https://doi.org/10.1016/j.cell.2013.06.007</a>."},"publication":"Cell","external_id":{"pmid":["23827674"]},"title":"Catastrophic nuclear envelope collapse in cancer cell micronuclei","main_file_link":[{"open_access":"1","url":"https://doi.org/10.1016/j.cell.2013.06.007"}]},{"status":"public","date_updated":"2022-07-18T08:50:47Z","publication_status":"published","oa_version":"Published Version","page":"971-982","day":"29","abstract":[{"lang":"eng","text":"Intracellular proteins with long lifespans have recently been linked to age-dependent defects, ranging from decreased fertility to the functional decline of neurons. Why long-lived proteins exist in metabolically active cellular environments and how they are maintained over time remains poorly understood. Here, we provide a system-wide identification of proteins with exceptional lifespans in the rat brain. These proteins are inefficiently replenished despite being translated robustly throughout adulthood. Using nucleoporins as a paradigm for long-term protein persistence, we found that nuclear pore complexes (NPCs) are maintained over a cell’s life through slow but finite exchange of even its most stable subcomplexes. This maintenance is limited, however, as some nucleoporin levels decrease during aging, providing a rationale for the previously observed age-dependent deterioration of NPC function. Our identification of a long-lived proteome reveals cellular components that are at increased risk for damage accumulation, linking long-term protein persistence to the cellular aging process."}],"issue":"5","scopus_import":"1","citation":{"ieee":"B. H. Toyama <i>et al.</i>, “Identification of long-lived proteins reveals exceptional stability of essential cellular structures,” <i>Cell</i>, vol. 154, no. 5. Elsevier, pp. 971–982, 2013.","chicago":"Toyama, Brandon H., Jeffrey N. Savas, Sung Kyu Park, Michael S. Harris, Nicholas T. Ingolia, John R. Yates, and Martin Hetzer. “Identification of Long-Lived Proteins Reveals Exceptional Stability of Essential Cellular Structures.” <i>Cell</i>. Elsevier, 2013. <a href=\"https://doi.org/10.1016/j.cell.2013.07.037\">https://doi.org/10.1016/j.cell.2013.07.037</a>.","ama":"Toyama BH, Savas JN, Park SK, et al. Identification of long-lived proteins reveals exceptional stability of essential cellular structures. <i>Cell</i>. 2013;154(5):971-982. doi:<a href=\"https://doi.org/10.1016/j.cell.2013.07.037\">10.1016/j.cell.2013.07.037</a>","ista":"Toyama BH, Savas JN, Park SK, Harris MS, Ingolia NT, Yates JR, Hetzer M. 2013. Identification of long-lived proteins reveals exceptional stability of essential cellular structures. Cell. 154(5), 971–982.","apa":"Toyama, B. H., Savas, J. N., Park, S. K., Harris, M. S., Ingolia, N. T., Yates, J. R., &#38; Hetzer, M. (2013). Identification of long-lived proteins reveals exceptional stability of essential cellular structures. <i>Cell</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.cell.2013.07.037\">https://doi.org/10.1016/j.cell.2013.07.037</a>","short":"B.H. Toyama, J.N. Savas, S.K. Park, M.S. Harris, N.T. Ingolia, J.R. Yates, M. Hetzer, Cell 154 (2013) 971–982.","mla":"Toyama, Brandon H., et al. “Identification of Long-Lived Proteins Reveals Exceptional Stability of Essential Cellular Structures.” <i>Cell</i>, vol. 154, no. 5, Elsevier, 2013, pp. 971–82, doi:<a href=\"https://doi.org/10.1016/j.cell.2013.07.037\">10.1016/j.cell.2013.07.037</a>."},"publication":"Cell","external_id":{"pmid":["23993091"]},"title":"Identification of long-lived proteins reveals exceptional stability of essential cellular structures","main_file_link":[{"open_access":"1","url":"https://doi.org/10.1016/j.cell.2013.07.037"}],"type":"journal_article","language":[{"iso":"eng"}],"doi":"10.1016/j.cell.2013.07.037","publisher":"Elsevier","year":"2013","date_published":"2013-08-29T00:00:00Z","author":[{"first_name":"Brandon H.","full_name":"Toyama, Brandon H.","last_name":"Toyama"},{"last_name":"Savas","full_name":"Savas, Jeffrey N.","first_name":"Jeffrey N."},{"full_name":"Park, Sung Kyu","first_name":"Sung Kyu","last_name":"Park"},{"first_name":"Michael S.","full_name":"Harris, Michael S.","last_name":"Harris"},{"full_name":"Ingolia, Nicholas T.","first_name":"Nicholas T.","last_name":"Ingolia"},{"full_name":"Yates, John R.","first_name":"John R.","last_name":"Yates"},{"first_name":"Martin W","full_name":"HETZER, Martin W","orcid":"0000-0002-2111-992X","last_name":"HETZER","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed"}],"oa":1,"_id":"11087","article_processing_charge":"No","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","extern":"1","keyword":["General Biochemistry","Genetics and Molecular Biology"],"intvolume":"       154","date_created":"2022-04-07T07:51:08Z","pmid":1,"article_type":"original","volume":154,"month":"08","quality_controlled":"1","publication_identifier":{"issn":["0092-8674"]}},{"_id":"9459","oa":1,"author":[{"last_name":"Zemach","full_name":"Zemach, Assaf","first_name":"Assaf"},{"full_name":"Kim, M. Yvonne","first_name":"M. Yvonne","last_name":"Kim"},{"last_name":"Hsieh","full_name":"Hsieh, Ping-Hung","first_name":"Ping-Hung"},{"last_name":"Coleman-Derr","first_name":"Devin","full_name":"Coleman-Derr, Devin"},{"last_name":"Eshed-Williams","full_name":"Eshed-Williams, Leor","first_name":"Leor"},{"last_name":"Thao","first_name":"Ka","full_name":"Thao, Ka"},{"last_name":"Harmer","first_name":"Stacey L.","full_name":"Harmer, Stacey L."},{"first_name":"Daniel","full_name":"Zilberman, Daniel","last_name":"Zilberman","id":"6973db13-dd5f-11ea-814e-b3e5455e9ed1","orcid":"0000-0002-0123-8649"}],"date_published":"2013-03-28T00:00:00Z","year":"2013","publisher":"Elsevier","doi":"10.1016/j.cell.2013.02.033","language":[{"iso":"eng"}],"type":"journal_article","publication_identifier":{"issn":["0092-8674"],"eissn":["1097-4172"]},"quality_controlled":"1","month":"03","article_type":"original","volume":153,"department":[{"_id":"DaZi"}],"pmid":1,"date_created":"2021-06-04T12:23:28Z","intvolume":"       153","extern":"1","article_processing_charge":"No","user_id":"8b945eb4-e2f2-11eb-945a-df72226e66a9","abstract":[{"lang":"eng","text":"Nucleosome remodelers of the DDM1/Lsh family are required for DNA methylation of transposable elements, but the reason for this is unknown. How DDM1 interacts with other methylation pathways, such as small-RNA-directed DNA methylation (RdDM), which is thought to mediate plant asymmetric methylation through DRM enzymes, is also unclear. Here, we show that most asymmetric methylation is facilitated by DDM1 and mediated by the methyltransferase CMT2 separately from RdDM. We find that heterochromatic sequences preferentially require DDM1 for DNA methylation and that this preference depends on linker histone H1. RdDM is instead inhibited by heterochromatin and absolutely requires the nucleosome remodeler DRD1. Together, DDM1 and RdDM mediate nearly all transposon methylation and collaborate to repress transposition and regulate the methylation and expression of genes. Our results indicate that DDM1 provides DNA methyltransferases access to H1-containing heterochromatin to allow stable silencing of transposable elements in cooperation with the RdDM pathway."}],"day":"28","oa_version":"Published Version","page":"193-205","publication_status":"published","date_updated":"2021-12-14T08:25:35Z","status":"public","main_file_link":[{"url":"https://doi.org/10.1016/j.cell.2013.02.033","open_access":"1"}],"title":"The Arabidopsis nucleosome remodeler DDM1 allows DNA methyltransferases to access H1-containing heterochromatin","external_id":{"pmid":["23540698"]},"publication":"Cell","citation":{"chicago":"Zemach, Assaf, M. Yvonne Kim, Ping-Hung Hsieh, Devin Coleman-Derr, Leor Eshed-Williams, Ka Thao, Stacey L. Harmer, and Daniel Zilberman. “The Arabidopsis Nucleosome Remodeler DDM1 Allows DNA Methyltransferases to Access H1-Containing Heterochromatin.” <i>Cell</i>. Elsevier, 2013. <a href=\"https://doi.org/10.1016/j.cell.2013.02.033\">https://doi.org/10.1016/j.cell.2013.02.033</a>.","ieee":"A. Zemach <i>et al.</i>, “The Arabidopsis nucleosome remodeler DDM1 allows DNA methyltransferases to access H1-containing heterochromatin,” <i>Cell</i>, vol. 153, no. 1. Elsevier, pp. 193–205, 2013.","mla":"Zemach, Assaf, et al. “The Arabidopsis Nucleosome Remodeler DDM1 Allows DNA Methyltransferases to Access H1-Containing Heterochromatin.” <i>Cell</i>, vol. 153, no. 1, Elsevier, 2013, pp. 193–205, doi:<a href=\"https://doi.org/10.1016/j.cell.2013.02.033\">10.1016/j.cell.2013.02.033</a>.","apa":"Zemach, A., Kim, M. Y., Hsieh, P.-H., Coleman-Derr, D., Eshed-Williams, L., Thao, K., … Zilberman, D. (2013). The Arabidopsis nucleosome remodeler DDM1 allows DNA methyltransferases to access H1-containing heterochromatin. <i>Cell</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.cell.2013.02.033\">https://doi.org/10.1016/j.cell.2013.02.033</a>","short":"A. Zemach, M.Y. Kim, P.-H. Hsieh, D. Coleman-Derr, L. Eshed-Williams, K. Thao, S.L. Harmer, D. Zilberman, Cell 153 (2013) 193–205.","ista":"Zemach A, Kim MY, Hsieh P-H, Coleman-Derr D, Eshed-Williams L, Thao K, Harmer SL, Zilberman D. 2013. The Arabidopsis nucleosome remodeler DDM1 allows DNA methyltransferases to access H1-containing heterochromatin. Cell. 153(1), 193–205.","ama":"Zemach A, Kim MY, Hsieh P-H, et al. The Arabidopsis nucleosome remodeler DDM1 allows DNA methyltransferases to access H1-containing heterochromatin. <i>Cell</i>. 2013;153(1):193-205. doi:<a href=\"https://doi.org/10.1016/j.cell.2013.02.033\">10.1016/j.cell.2013.02.033</a>"},"scopus_import":"1","issue":"1"},{"date_published":"2012-05-11T00:00:00Z","author":[{"last_name":"Hatch","first_name":"Emily M.","full_name":"Hatch, Emily M."},{"first_name":"Martin W","full_name":"HETZER, Martin W","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","last_name":"HETZER","orcid":"0000-0002-2111-992X"}],"_id":"11090","oa":1,"type":"journal_article","doi":"10.1016/j.cell.2012.04.018","language":[{"iso":"eng"}],"year":"2012","publisher":"Elsevier","volume":149,"article_type":"letter_note","month":"05","publication_identifier":{"issn":["0092-8674"]},"quality_controlled":"1","extern":"1","article_processing_charge":"No","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","intvolume":"       149","keyword":["General Biochemistry","Genetics and Molecular Biology"],"date_created":"2022-04-07T07:51:45Z","pmid":1,"day":"11","page":"733-735","publication_status":"published","oa_version":"Published Version","abstract":[{"lang":"eng","text":"Nuclear export of mRNAs is thought to occur exclusively through nuclear pore complexes. In this issue of Cell, Speese et al. identify an alternate pathway for mRNA export in muscle cells where ribonucleoprotein complexes involved in forming neuromuscular junctions transit the nuclear envelope by fusing with and budding through the nuclear membrane."}],"status":"public","date_updated":"2022-07-18T08:58:48Z","publication":"Cell","title":"RNP export by nuclear envelope budding","external_id":{"pmid":["22579277"]},"main_file_link":[{"open_access":"1","url":"https://doi.org/10.1016/j.cell.2012.04.018"}],"scopus_import":"1","issue":"4","citation":{"ieee":"E. M. Hatch and M. Hetzer, “RNP export by nuclear envelope budding,” <i>Cell</i>, vol. 149, no. 4. Elsevier, pp. 733–735, 2012.","chicago":"Hatch, Emily M., and Martin Hetzer. “RNP Export by Nuclear Envelope Budding.” <i>Cell</i>. Elsevier, 2012. <a href=\"https://doi.org/10.1016/j.cell.2012.04.018\">https://doi.org/10.1016/j.cell.2012.04.018</a>.","ama":"Hatch EM, Hetzer M. RNP export by nuclear envelope budding. <i>Cell</i>. 2012;149(4):733-735. doi:<a href=\"https://doi.org/10.1016/j.cell.2012.04.018\">10.1016/j.cell.2012.04.018</a>","apa":"Hatch, E. M., &#38; Hetzer, M. (2012). RNP export by nuclear envelope budding. <i>Cell</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.cell.2012.04.018\">https://doi.org/10.1016/j.cell.2012.04.018</a>","ista":"Hatch EM, Hetzer M. 2012. RNP export by nuclear envelope budding. Cell. 149(4), 733–735.","mla":"Hatch, Emily M., and Martin Hetzer. “RNP Export by Nuclear Envelope Budding.” <i>Cell</i>, vol. 149, no. 4, Elsevier, 2012, pp. 733–35, doi:<a href=\"https://doi.org/10.1016/j.cell.2012.04.018\">10.1016/j.cell.2012.04.018</a>.","short":"E.M. Hatch, M. Hetzer, Cell 149 (2012) 733–735."}},{"type":"journal_article","publisher":"Elsevier","year":"2010","language":[{"iso":"eng"}],"doi":"10.1016/j.cell.2010.04.036","date_published":"2010-06-11T00:00:00Z","oa":1,"_id":"11101","author":[{"full_name":"Doucet, Christine M.","first_name":"Christine M.","last_name":"Doucet"},{"full_name":"Talamas, Jessica A.","first_name":"Jessica A.","last_name":"Talamas"},{"full_name":"HETZER, Martin W","first_name":"Martin W","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","last_name":"HETZER","orcid":"0000-0002-2111-992X"}],"keyword":["General Biochemistry","Genetics and Molecular Biology"],"intvolume":"       141","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","extern":"1","article_processing_charge":"No","pmid":1,"date_created":"2022-04-07T07:53:29Z","volume":141,"article_type":"original","quality_controlled":"1","publication_identifier":{"issn":["0092-8674"]},"month":"06","status":"public","date_updated":"2022-07-18T08:54:52Z","abstract":[{"text":"In metazoa, nuclear pore complexes (NPCs) assemble from disassembled precursors into a reforming nuclear envelope (NE) at the end of mitosis and into growing intact NEs during interphase. Here, we show via RNAi-mediated knockdown that ELYS, a nucleoporin critical for the recruitment of the essential Nup107/160 complex to chromatin, is required for NPC assembly at the end of mitosis but not during interphase. Conversely, the transmembrane nucleoporin POM121 is critical for the incorporation of the Nup107/160 complex into new assembly sites specifically during interphase. Strikingly, recruitment of the Nup107/160 complex to an intact NE involves a membrane curvature-sensing domain of its constituent Nup133, which is not required for postmitotic NPC formation. Our results suggest that in organisms with open mitosis, NPCs assemble via two distinct mechanisms to accommodate cell cycle-dependent differences in NE topology.","lang":"eng"}],"page":"1030-1041","oa_version":"Published Version","publication_status":"published","day":"11","issue":"6","scopus_import":"1","citation":{"chicago":"Doucet, Christine M., Jessica A. Talamas, and Martin Hetzer. “Cell Cycle-Dependent Differences in Nuclear Pore Complex Assembly in Metazoa.” <i>Cell</i>. Elsevier, 2010. <a href=\"https://doi.org/10.1016/j.cell.2010.04.036\">https://doi.org/10.1016/j.cell.2010.04.036</a>.","ieee":"C. M. Doucet, J. A. Talamas, and M. Hetzer, “Cell cycle-dependent differences in nuclear pore complex assembly in metazoa,” <i>Cell</i>, vol. 141, no. 6. Elsevier, pp. 1030–1041, 2010.","apa":"Doucet, C. M., Talamas, J. A., &#38; Hetzer, M. (2010). Cell cycle-dependent differences in nuclear pore complex assembly in metazoa. <i>Cell</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.cell.2010.04.036\">https://doi.org/10.1016/j.cell.2010.04.036</a>","ista":"Doucet CM, Talamas JA, Hetzer M. 2010. Cell cycle-dependent differences in nuclear pore complex assembly in metazoa. Cell. 141(6), 1030–1041.","mla":"Doucet, Christine M., et al. “Cell Cycle-Dependent Differences in Nuclear Pore Complex Assembly in Metazoa.” <i>Cell</i>, vol. 141, no. 6, Elsevier, 2010, pp. 1030–41, doi:<a href=\"https://doi.org/10.1016/j.cell.2010.04.036\">10.1016/j.cell.2010.04.036</a>.","short":"C.M. Doucet, J.A. Talamas, M. Hetzer, Cell 141 (2010) 1030–1041.","ama":"Doucet CM, Talamas JA, Hetzer M. Cell cycle-dependent differences in nuclear pore complex assembly in metazoa. <i>Cell</i>. 2010;141(6):1030-1041. doi:<a href=\"https://doi.org/10.1016/j.cell.2010.04.036\">10.1016/j.cell.2010.04.036</a>"},"external_id":{"pmid":["20550937"]},"title":"Cell cycle-dependent differences in nuclear pore complex assembly in metazoa","publication":"Cell","main_file_link":[{"open_access":"1","url":"https://doi.org/10.1016/j.cell.2010.04.036"}]},{"year":"2010","publisher":"Elsevier","doi":"10.1016/j.cell.2009.12.054","language":[{"iso":"eng"}],"type":"journal_article","_id":"11102","oa":1,"author":[{"last_name":"Capelson","first_name":"Maya","full_name":"Capelson, Maya"},{"full_name":"Liang, Yun","first_name":"Yun","last_name":"Liang"},{"last_name":"Schulte","first_name":"Roberta","full_name":"Schulte, Roberta"},{"last_name":"Mair","full_name":"Mair, William","first_name":"William"},{"first_name":"Ulrich","full_name":"Wagner, Ulrich","last_name":"Wagner"},{"last_name":"HETZER","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","orcid":"0000-0002-2111-992X","first_name":"Martin W","full_name":"HETZER, Martin W"}],"date_published":"2010-02-05T00:00:00Z","pmid":1,"date_created":"2022-04-07T07:53:36Z","intvolume":"       140","keyword":["General Biochemistry","Genetics and Molecular Biology"],"extern":"1","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","article_processing_charge":"No","publication_identifier":{"issn":["0092-8674"]},"quality_controlled":"1","month":"02","volume":140,"article_type":"original","date_updated":"2022-07-18T08:55:03Z","status":"public","abstract":[{"text":"Nuclear pore complexes have recently been shown to play roles in gene activation; however their potential involvement in metazoan transcription remains unclear. Here we show that the nucleoporins Sec13, Nup98, and Nup88, as well as a group of FG-repeat nucleoporins, bind to the Drosophila genome at functionally distinct loci that often do not represent nuclear envelope contact sites. Whereas Nup88 localizes to silent loci, Sec13, Nup98, and a subset of FG-repeat nucleoporins bind to developmentally regulated genes undergoing transcription induction. Strikingly, RNAi-mediated knockdown of intranuclear Sec13 and Nup98 specifically inhibits transcription of their target genes and prevents efficient reactivation of transcription after heat shock, suggesting an essential role of NPC components in regulating complex gene expression programs of multicellular organisms.","lang":"eng"}],"day":"05","oa_version":"Published Version","page":"372-383","publication_status":"published","citation":{"short":"M. Capelson, Y. Liang, R. Schulte, W. Mair, U. Wagner, M. Hetzer, Cell 140 (2010) 372–383.","mla":"Capelson, Maya, et al. “Chromatin-Bound Nuclear Pore Components Regulate Gene Expression in Higher Eukaryotes.” <i>Cell</i>, vol. 140, no. 3, Elsevier, 2010, pp. 372–83, doi:<a href=\"https://doi.org/10.1016/j.cell.2009.12.054\">10.1016/j.cell.2009.12.054</a>.","apa":"Capelson, M., Liang, Y., Schulte, R., Mair, W., Wagner, U., &#38; Hetzer, M. (2010). Chromatin-bound nuclear pore components regulate gene expression in higher eukaryotes. <i>Cell</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.cell.2009.12.054\">https://doi.org/10.1016/j.cell.2009.12.054</a>","ista":"Capelson M, Liang Y, Schulte R, Mair W, Wagner U, Hetzer M. 2010. Chromatin-bound nuclear pore components regulate gene expression in higher eukaryotes. Cell. 140(3), 372–383.","ama":"Capelson M, Liang Y, Schulte R, Mair W, Wagner U, Hetzer M. Chromatin-bound nuclear pore components regulate gene expression in higher eukaryotes. <i>Cell</i>. 2010;140(3):372-383. doi:<a href=\"https://doi.org/10.1016/j.cell.2009.12.054\">10.1016/j.cell.2009.12.054</a>","chicago":"Capelson, Maya, Yun Liang, Roberta Schulte, William Mair, Ulrich Wagner, and Martin Hetzer. “Chromatin-Bound Nuclear Pore Components Regulate Gene Expression in Higher Eukaryotes.” <i>Cell</i>. Elsevier, 2010. <a href=\"https://doi.org/10.1016/j.cell.2009.12.054\">https://doi.org/10.1016/j.cell.2009.12.054</a>.","ieee":"M. Capelson, Y. Liang, R. Schulte, W. Mair, U. Wagner, and M. Hetzer, “Chromatin-bound nuclear pore components regulate gene expression in higher eukaryotes,” <i>Cell</i>, vol. 140, no. 3. Elsevier, pp. 372–383, 2010."},"scopus_import":"1","issue":"3","main_file_link":[{"url":"https://doi.org/10.1016/j.cell.2009.12.054","open_access":"1"}],"title":"Chromatin-bound nuclear pore components regulate gene expression in higher eukaryotes","external_id":{"pmid":["20144761"]},"publication":"Cell"},{"month":"09","quality_controlled":"1","publication_identifier":{"issn":["0092-8674"]},"publication":"Cell","volume":142,"article_type":"original","title":"‘Fore brain: A hint of the ancestral cortex","date_created":"2020-04-30T10:36:52Z","citation":{"ama":"Sweeney LB, Luo L. ‘Fore brain: A hint of the ancestral cortex. <i>Cell</i>. 2010;142(5):679-681. doi:<a href=\"https://doi.org/10.1016/j.cell.2010.08.024\">10.1016/j.cell.2010.08.024</a>","apa":"Sweeney, L. B., &#38; Luo, L. (2010). ‘Fore brain: A hint of the ancestral cortex. <i>Cell</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.cell.2010.08.024\">https://doi.org/10.1016/j.cell.2010.08.024</a>","ista":"Sweeney LB, Luo L. 2010. ‘Fore brain: A hint of the ancestral cortex. Cell. 142(5), 679–681.","short":"L.B. Sweeney, L. Luo, Cell 142 (2010) 679–681.","mla":"Sweeney, Lora B., and Liqun Luo. “‘Fore Brain: A Hint of the Ancestral Cortex.” <i>Cell</i>, vol. 142, no. 5, Elsevier, 2010, pp. 679–81, doi:<a href=\"https://doi.org/10.1016/j.cell.2010.08.024\">10.1016/j.cell.2010.08.024</a>.","ieee":"L. B. Sweeney and L. Luo, “‘Fore brain: A hint of the ancestral cortex,” <i>Cell</i>, vol. 142, no. 5. Elsevier, pp. 679–681, 2010.","chicago":"Sweeney, Lora B., and Liqun Luo. “‘Fore Brain: A Hint of the Ancestral Cortex.” <i>Cell</i>. Elsevier, 2010. <a href=\"https://doi.org/10.1016/j.cell.2010.08.024\">https://doi.org/10.1016/j.cell.2010.08.024</a>."},"article_processing_charge":"No","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","extern":"1","issue":"5","intvolume":"       142","author":[{"orcid":"0000-0001-9242-5601","id":"56BE8254-C4F0-11E9-8E45-0B23E6697425","last_name":"Sweeney","full_name":"Sweeney, Lora Beatrice Jaeger","first_name":"Lora Beatrice Jaeger"},{"full_name":"Luo, Liqun","first_name":"Liqun","last_name":"Luo"}],"_id":"7703","page":"679-681","date_published":"2010-09-03T00:00:00Z","oa_version":"None","publication_status":"published","day":"03","abstract":[{"lang":"eng","text":"By combining gene expression profiling with image registration, Tomer et al. (2010) find that the mushroom body of the segmented worm Platynereis dumerilii shares many features with the mammalian cerebral cortex. The authors propose that the mushroom body and cortex evolved from the same structure in the common ancestor of vertebrates and invertebrates."}],"language":[{"iso":"eng"}],"doi":"10.1016/j.cell.2010.08.024","publisher":"Elsevier","date_updated":"2024-01-31T10:14:59Z","year":"2010","status":"public","type":"journal_article"},{"quality_controlled":"1","publication_identifier":{"issn":["0092-8674"]},"month":"01","article_type":"original","volume":136,"pmid":1,"date_created":"2022-04-07T07:54:52Z","keyword":["General Biochemistry","Genetics and Molecular Biology"],"intvolume":"       136","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","article_processing_charge":"No","extern":"1","oa":1,"_id":"11108","author":[{"full_name":"D'Angelo, Maximiliano A.","first_name":"Maximiliano A.","last_name":"D'Angelo"},{"last_name":"Raices","first_name":"Marcela","full_name":"Raices, Marcela"},{"last_name":"Panowski","full_name":"Panowski, Siler H.","first_name":"Siler H."},{"id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","last_name":"HETZER","orcid":"0000-0002-2111-992X","full_name":"HETZER, Martin W","first_name":"Martin W"}],"date_published":"2009-01-23T00:00:00Z","publisher":"Elsevier","year":"2009","language":[{"iso":"eng"}],"doi":"10.1016/j.cell.2008.11.037","type":"journal_article","main_file_link":[{"url":"https://doi.org/10.1016/j.cell.2008.11.037","open_access":"1"}],"external_id":{"pmid":["19167330"]},"title":"Age-dependent deterioration of nuclear pore complexes causes a loss of nuclear integrity in postmitotic cells","publication":"Cell","citation":{"chicago":"D’Angelo, Maximiliano A., Marcela Raices, Siler H. Panowski, and Martin Hetzer. “Age-Dependent Deterioration of Nuclear Pore Complexes Causes a Loss of Nuclear Integrity in Postmitotic Cells.” <i>Cell</i>. Elsevier, 2009. <a href=\"https://doi.org/10.1016/j.cell.2008.11.037\">https://doi.org/10.1016/j.cell.2008.11.037</a>.","ieee":"M. A. D’Angelo, M. Raices, S. H. Panowski, and M. Hetzer, “Age-dependent deterioration of nuclear pore complexes causes a loss of nuclear integrity in postmitotic cells,” <i>Cell</i>, vol. 136, no. 2. Elsevier, pp. 284–295, 2009.","apa":"D’Angelo, M. A., Raices, M., Panowski, S. H., &#38; Hetzer, M. (2009). Age-dependent deterioration of nuclear pore complexes causes a loss of nuclear integrity in postmitotic cells. <i>Cell</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.cell.2008.11.037\">https://doi.org/10.1016/j.cell.2008.11.037</a>","mla":"D’Angelo, Maximiliano A., et al. “Age-Dependent Deterioration of Nuclear Pore Complexes Causes a Loss of Nuclear Integrity in Postmitotic Cells.” <i>Cell</i>, vol. 136, no. 2, Elsevier, 2009, pp. 284–95, doi:<a href=\"https://doi.org/10.1016/j.cell.2008.11.037\">10.1016/j.cell.2008.11.037</a>.","short":"M.A. D’Angelo, M. Raices, S.H. Panowski, M. Hetzer, Cell 136 (2009) 284–295.","ista":"D’Angelo MA, Raices M, Panowski SH, Hetzer M. 2009. Age-dependent deterioration of nuclear pore complexes causes a loss of nuclear integrity in postmitotic cells. Cell. 136(2), 284–295.","ama":"D’Angelo MA, Raices M, Panowski SH, Hetzer M. Age-dependent deterioration of nuclear pore complexes causes a loss of nuclear integrity in postmitotic cells. <i>Cell</i>. 2009;136(2):284-295. doi:<a href=\"https://doi.org/10.1016/j.cell.2008.11.037\">10.1016/j.cell.2008.11.037</a>"},"issue":"2","scopus_import":"1","abstract":[{"text":"In dividing cells, nuclear pore complexes (NPCs) disassemble during mitosis and reassemble into the newly forming nuclei. However, the fate of nuclear pores in postmitotic cells is unknown. Here, we show that NPCs, unlike other nuclear structures, do not turn over in differentiated cells. While a subset of NPC components, like Nup153 and Nup50, are continuously exchanged, scaffold nucleoporins, like the Nup107/160 complex, are extremely long-lived and remain incorporated in the nuclear membrane during the entire cellular life span. Besides the lack of nucleoporin expression and NPC turnover, we discovered an age-related deterioration of NPCs, leading to an increase in nuclear permeability and the leaking of cytoplasmic proteins into the nucleus. Our finding that nuclear “leakiness” is dramatically accelerated during aging and that a subset of nucleoporins is oxidatively damaged in old cells suggests that the accumulation of damage at the NPC might be a crucial aging event.","lang":"eng"}],"publication_status":"published","page":"284-295","oa_version":"Published Version","day":"23","date_updated":"2022-07-18T08:55:29Z","status":"public"},{"title":"Graded expression of semaphorin-1a cell-autonomously directs dendritic targeting of olfactory projection neurons","volume":128,"article_type":"original","publication":"Cell","publication_identifier":{"issn":["0092-8674"]},"quality_controlled":"1","month":"01","intvolume":"       128","issue":"2","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","article_processing_charge":"No","extern":"1","citation":{"apa":"Komiyama, T., Sweeney, L. B., Schuldiner, O., Garcia, K. C., &#38; Luo, L. (2007). Graded expression of semaphorin-1a cell-autonomously directs dendritic targeting of olfactory projection neurons. <i>Cell</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.cell.2006.12.028\">https://doi.org/10.1016/j.cell.2006.12.028</a>","short":"T. Komiyama, L.B. Sweeney, O. Schuldiner, K.C. Garcia, L. Luo, Cell 128 (2007) 399–410.","ista":"Komiyama T, Sweeney LB, Schuldiner O, Garcia KC, Luo L. 2007. Graded expression of semaphorin-1a cell-autonomously directs dendritic targeting of olfactory projection neurons. Cell. 128(2), 399–410.","mla":"Komiyama, Takaki, et al. “Graded Expression of Semaphorin-1a Cell-Autonomously Directs Dendritic Targeting of Olfactory Projection Neurons.” <i>Cell</i>, vol. 128, no. 2, Elsevier, 2007, pp. 399–410, doi:<a href=\"https://doi.org/10.1016/j.cell.2006.12.028\">10.1016/j.cell.2006.12.028</a>.","ama":"Komiyama T, Sweeney LB, Schuldiner O, Garcia KC, Luo L. Graded expression of semaphorin-1a cell-autonomously directs dendritic targeting of olfactory projection neurons. <i>Cell</i>. 2007;128(2):399-410. doi:<a href=\"https://doi.org/10.1016/j.cell.2006.12.028\">10.1016/j.cell.2006.12.028</a>","chicago":"Komiyama, Takaki, Lora B. Sweeney, Oren Schuldiner, K. Christopher Garcia, and Liqun Luo. “Graded Expression of Semaphorin-1a Cell-Autonomously Directs Dendritic Targeting of Olfactory Projection Neurons.” <i>Cell</i>. Elsevier, 2007. <a href=\"https://doi.org/10.1016/j.cell.2006.12.028\">https://doi.org/10.1016/j.cell.2006.12.028</a>.","ieee":"T. Komiyama, L. B. Sweeney, O. Schuldiner, K. C. Garcia, and L. Luo, “Graded expression of semaphorin-1a cell-autonomously directs dendritic targeting of olfactory projection neurons,” <i>Cell</i>, vol. 128, no. 2. Elsevier, pp. 399–410, 2007."},"date_created":"2020-04-30T10:37:08Z","abstract":[{"text":"Gradients of axon guidance molecules instruct the formation of continuous neural maps, such as the retinotopic map in the vertebrate visual system. Here we show that molecular gradients can also instruct the formation of a discrete neural map. In the fly olfactory system, axons of 50 classes of olfactory receptor neurons (ORNs) and dendrites of 50 classes of projection neurons (PNs) form one-to-one connections at discrete units called glomeruli. We provide expression, loss- and gain-of-function data to demonstrate that the levels of transmembrane Semaphorin-1a (Sema-1a), acting cell-autonomously as a receptor or part of a receptor complex, direct the dendritic targeting of PNs along the dorsolateral to ventromedial axis of the antennal lobe. Sema-1a also regulates PN axon targeting in higher olfactory centers. Thus, graded expression of Sema-1a contributes to connection specificity from ORNs to PNs and then to higher brain centers, ensuring proper representation of olfactory information in the brain.","lang":"eng"}],"day":"26","date_published":"2007-01-26T00:00:00Z","page":"399-410","publication_status":"published","oa_version":"None","_id":"7704","author":[{"full_name":"Komiyama, Takaki","first_name":"Takaki","last_name":"Komiyama"},{"orcid":"0000-0001-9242-5601","last_name":"Sweeney","id":"56BE8254-C4F0-11E9-8E45-0B23E6697425","first_name":"Lora Beatrice Jaeger","full_name":"Sweeney, Lora Beatrice Jaeger"},{"full_name":"Schuldiner, Oren","first_name":"Oren","last_name":"Schuldiner"},{"last_name":"Garcia","first_name":"K. Christopher","full_name":"Garcia, K. Christopher"},{"last_name":"Luo","first_name":"Liqun","full_name":"Luo, Liqun"}],"type":"journal_article","status":"public","year":"2007","publisher":"Elsevier","date_updated":"2024-01-31T10:14:48Z","doi":"10.1016/j.cell.2006.12.028","language":[{"iso":"eng"}]}]