Syndecan-4 associates with α-actinin

被引:82
作者
Greene, DK
Tumova, S
Couchman, JR
Woods, A
机构
[1] Univ Alabama Birmingham, Dept Cell Biol, Birmingham, AL 35294 USA
[2] Univ Helsinki, Dept Biosci, FIN-00014 Helsinki, Finland
[3] Univ London Imperial Coll Sci Technol & Med, Div Biomed Sci, Div Cell & Mol Biol, London SW7 2AZ, England
关键词
D O I
10.1074/jbc.M207123200
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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.
引用
收藏
页码:7617 / 7623
页数:7
相关论文
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