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Both emerin and lamin C depend on lamin A for localization at the nuclear envelope

¹ Department of Biological Sciences, The University of Durham, South Road, Durham, DH1 3LE, UK
² Department of Biology and Biochemistry, The University of Brunel, Middlesex, UB8 3PH, UK
³ Department of Molecular Cell Biology and Genetics, University Maastricht, PO Box 616, Maastricht, 6200 MD, The Netherlands
⁴ Ernst-Moritz-Arndt-University, Institute of Human Genetics, Fleischmannstrasse 42-44, 17487 Greifswald, Germany
⁵ MRIC, North East Wales Institute, Plas Coch, Mold Road, Wrexham, LL11 2AW, Wales
⁶ Department of Biological Sciences, The University of Dundee, Dundee, DD1 4HN, Scotland
^* Author for correspondence (e-mail: c.j.hutchison{at}durham.ac.uk )

Accepted April 14, 2001

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.

Key words: Lamins, Emerin, Nuclear envelope, Nuclear lamina, Emery-Dreifuss muscular dystrophy