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J. Biol. Chem., Vol. 282, Issue 9, 6308-6315, March 2, 2007

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Lamina-associated Polypeptide 2- Forms Homo-trimers via Its C Terminus, and Oligomerization Is Unaffected by a Disease-causing Mutation^*

Luc Snyers, Sylvia Vlcek, Thomas Dechat¹, Darko Skegro^¶, Barbara Korbei, Andreas Gajewski, Olga Mayans^¶2, Christian Schöfer, and Roland Foisner²³

From the Center for Anatomy and Cell Biology, Medical University of Vienna, Schwarzspanierstrasse 17, A-1090 Vienna, Austria, the Max F. Perutz Laboratories, Medical University of Vienna, Dr. Bohr-Gasse 9, A-1030 Vienna, Austria, and the ^¶Division of Structural Biology, Biozentrum, University of Basel, Klingelbergstrasse 70, 4056 Basel, Switzerland

The nucleoplasmic protein, Lamina-associated polypeptide (LAP) 2, is one of six alternatively spliced products of the LAP2gene, which share a common N-terminal region. In contrast to the other isoforms, which also share most of their C termini, LAP2 has a large unique C-terminal region that contains binding sites for chromatin, A-type lamins, and retinoblastoma protein. By immunoprecipitation analyses of LAP2 complexes from cells expressing differently tagged LAP2 proteins and fragments, we demonstrate that LAP2 forms higher order structures containing multiple LAP2 molecules in vivo and that complex formation is mediated by the C terminus. Solid phase binding assays using recombinant and in vitro translated LAP2 fragments showed direct interactions of LAP2 C termini. Cross-linking of LAP2 complexes and multiangle light scattering of purified LAP2 revealed the existence of stable homo-trimers in vivo and in vitro. Finally, we show that, in contrast to the LAP2-lamin A interaction, its self-association is not affected by a disease-linked single point mutation in the LAP2 C terminus.

Received for publication, June 16, 2006 , and in revised form, January 5, 2007.

^* This study was supported in part by Austrian Science Research Fund Grant FWF P17871 [GenBank] (to R. F.), Austrian National Bank Grant 9840 (to C. S.), and from the Swiss National Foundation Grant 3100A0-100852 (to O. M.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

¹ Present address: Dept. of Cell and Molecular Biology, Feinberg School of Medicine, Northwestern University, Chicago, IL.

² Supported by the EURO-Laminopathies research project of the European Commission (Contract LSHM-CT-2005-018690).

³ To whom correspondence should be addressed. Tel.: 43-1-4277-61680; Fax: 43-1-4277-9616; E-mail: roland.foisner{at}meduniwien.ac.at.

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