Paxillin association in vitro with integrin cytoplasmic domain peptides

FEBS Letters

Healy, Judith M.²  Sabe, Hisataka³  Sekiguchi, Kiyotoshi¹  Yamaguchi, Ryuji³  Tanaka, Toshiki² 

[1] Research Institute, Osaka Medical Center for Maternal and Child Health, 840 Murodo-cho, Izumi, Osaka 590-02, Japan;Biomolecular Engineering Research Institute, 6-2-3 Furuedai, Suita, Osaka 565, Japan;Institute for Virus Research, Kyoto University, Shogoin, Sankyoku, Kyoto 606, Japan

关键词: Integrin;    Paxillin;    Cell adhesion;   

DOI  :  10.1016/S0014-5793(96)01280-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Short cytoplasmic domains of integrin heterodimers are crucial for transduction of signals generated by adhesion of cells to the extracellular matrix. Here, we describe the use of peptides mimicking the intracellular tails of integrin α ₅ β ₁ to assay in vitro associations with cytoskeletal proteins. Our results suggest that the focal adhesion protein, paxillin, may interact directly with the intracellular region of the integrin β ₁ subunit. Paxillin is known to form stable complexes with several signaling molecules, including focal adhesion kinase. Physical interaction between paxillin and the β ₁ cytoplasmic domain suggests a model in which paxillin may function as a key intermediary in integrinmediated signal transduction.

【 授权许可】

Unknown