{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,15]],"date-time":"2026-10-15T18:39:25Z","timestamp":1792089565841,"version":"4.4.0"},"reference-count":55,"publisher":"The Company of Biologists","issue":"14","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2001,7,15]]},"abstract":"<jats:p>Physical interactions between lamins and emerin were investigated by co-immunoprecipitation of in vitro translated proteins. Emerin interacted with in vitro translated lamins A, B1 and C in co-immunprecipitation reactions. Competition reactions revealed a clear preference for interactions between emerin and lamin C. Structural associations between lamins and emerin were investigated in four human cell lines displaying abnormal expression and\/or localisation of lamins A and C. In each cell line absence of lamins A and C from the nuclear envelope (NE) was correlated with mis-localisation of endogenous and exogenous emerin to the ER. In two cell lines that did not express lamin A but did express lamin C, lamin C as well as emerin was mis-localised. When GFP-lamin A was expressed in SW13 cells (which normally express only very low levels of endogenous lamin A and mis-localise endogenous emerin and lamin C), all three proteins became associated with the NE. When GFP-lamin C was expressed in SW13 cells neither the endogenous nor the exogenous lamin C was localised to the NE and emerin remained in the ER. Finally, lamins A and C were selectively eliminated from the NE of HeLa cells using a dominant negative mutant of lamin B1. Elimination of these lamins from the lamina led to the accumulation of emerin as aggregates within the ER. Our data suggest that lamin A is essential for anchorage of emerin to the inner nuclear membrane and of lamin C to the lamina.<\/jats:p>","DOI":"10.1242\/jcs.114.14.2577","type":"journal-article","created":{"date-parts":[[2021,4,25]],"date-time":"2021-04-25T23:27:39Z","timestamp":1619393259000},"page":"2577-2590","source":"Crossref","is-referenced-by-count":213,"title":["Both emerin and lamin C depend on lamin A for localization at the nuclear envelope"],"prefix":"10.1242","volume":"114","author":[{"given":"O. Anthony","family":"Vaughan","sequence":"first","affiliation":[{"name":"Department of Biological Sciences, The University of Durham, South Road, Durham, DH1 3LE, UK"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mauricio","family":"Alvarez-Reyes","sequence":"additional","affiliation":[{"name":"Department of Biological Sciences, The University of Durham, South Road, Durham, DH1 3LE, UK"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Joanna M.","family":"Bridger","sequence":"additional","affiliation":[{"name":"Department of Biology and Biochemistry, The University of Brunel, Middlesex, UB8 3PH, UK"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jos L. V.","family":"Broers","sequence":"additional","affiliation":[{"name":"Department of Molecular Cell Biology and Genetics, University Maastricht, PO Box 616, Maastricht, 6200 MD, The Netherlands"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Frans C. S.","family":"Ramaekers","sequence":"additional","affiliation":[{"name":"Department of Molecular Cell Biology and Genetics, University Maastricht, PO Box 616, Maastricht, 6200 MD, The Netherlands"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Manfred","family":"Wehnert","sequence":"additional","affiliation":[{"name":"Ernst-Moritz-Arndt-University, Institute of Human Genetics, Fleischmannstrasse 42-44, 17487 Greifswald, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Glen E.","family":"Morris","sequence":"additional","affiliation":[{"name":"MRIC, North East Wales Institute, Plas Coch, Mold Road, Wrexham, LL11 2AW, Wales"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"William G. 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