Please use this identifier to cite or link to this item:
http://bura.brunel.ac.uk/handle/2438/2939
Full metadata record
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Vaughan, A | - |
dc.contributor.author | Alvarez-Reyes, M | - |
dc.contributor.author | Bridger, JM | - |
dc.contributor.author | Broers, JL | - |
dc.contributor.author | Raemakers, FC | - |
dc.contributor.author | Wehnert, M | - |
dc.contributor.author | Morris, GE | - |
dc.contributor.author | Whitfield, WGF | - |
dc.contributor.author | Hutchison, CJ | - |
dc.coverage.spatial | 14 | en |
dc.date.accessioned | 2008-12-23T14:35:24Z | - |
dc.date.available | 2008-12-23T14:35:24Z | - |
dc.date.issued | 2001 | - |
dc.identifier.citation | Journal of Cell Science. 114, 2577-2590 | en |
dc.identifier.issn | 0021-9533 | - |
dc.identifier.uri | http://bura.brunel.ac.uk/handle/2438/2939 | - |
dc.description.abstract | 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 GFPlamin 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. | en |
dc.format.extent | 872188 bytes | - |
dc.format.mimetype | application/pdf | - |
dc.language.iso | en | - |
dc.publisher | Company of Biologists | en |
dc.subject | Lamins, Emerin, Nuclear envelope, Nuclear lamina, Emery-Dreifuss muscular dystrophy | en |
dc.title | Both emerin and lamin C depend on lamin A for localization at the nuclear envelope | en |
dc.type | Research Paper | en |
Appears in Collections: | Community Health and Public Health Dept of Health Sciences Research Papers |
Items in BURA are protected by copyright, with all rights reserved, unless otherwise indicated.