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Originally published In Press as doi:10.1074/jbc.M207123200 on December 18, 2002

J. Biol. Chem., Vol. 278, Issue 9, 7617-7623, February 28, 2003
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Syndecan-4 Associates with alpha -Actinin*

Daniel K. GreeneDagger , Sarka Tumova§, John R. Couchman, and Anne WoodsDagger ||

From the Dagger  Department of Cell Biology, University of Alabama, Birmingham, Alabama 35294-0006, § Department of Bioscience, University of Helsinki, Helsinki FIN-00014, Finland, and  Cell and Molecular Biology Division, Division of Biomedical Sciences, Imperial College, London SW7 2AZ, United Kingdom

Cell adhesion to the extracellular matrix influences many cellular functions. The integrin family of matrix receptors plays major roles in the formation of adhesions, but other proteins modulate integrin signaling. Syndecan-4, a transmembrane proteoglycan, cooperatively signals with integrins during the formation of focal adhesions. To date, a direct link between syndecan-4 and the cytoskeleton has remained elusive. We now demonstrate by Triton X-100 extraction immunoprecipitation and in vitro binding assays that the focal adhesion component alpha -actinin interacts with syndecan-4 in a beta -integrin-independent manner.

* This study was supported by National Institutes of Health Grant GM50194 (to A. W.) and by Sankyo, Co., Ltd.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

|| To whom correspondence should be addressed: Dept. of Cell Biology, THT 946, University of Alabama, 1530 3rd Ave. S., Birmingham, AL 35294-0006. Tel.: 205-934-1548; Fax: 205-934-7029; E-mail: anwoods@uab.edu.

Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
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