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Title: Both emerin and lamin C depend on lamin A for localization at the nuclear envelope
Authors: Vaughan, A
Alvarez-Reyes, M
Bridger, JM
Broers, JL
Raemakers, FC
Wehnert, M
Morris, GE
Whitfield, WGF
Hutchison, CJ
Keywords: Lamins, Emerin, Nuclear envelope, Nuclear lamina, Emery-Dreifuss muscular dystrophy
Issue Date: 2001
Publisher: Company of Biologists
Citation: Journal of Cell Science. 114, 2577-2590
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.
ISSN: 0021-9533
Appears in Collections:Community Health and Public Health
Dept of Clinical Sciences Research Papers

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