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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
Syndecan-4 Associates with -Actinin*
Daniel K.
Greene ,
Sarka
Tumova§,
John R.
Couchman¶, and
Anne
Woods
From the 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 -actinin interacts with syndecan-4
in a -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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