Tyrosine phosphorylation of paxillin, FAK, and p130CAS: Effects on cell spreading and migration

被引：120

作者：

Panetti, TS ^{[1
]}

机构：

[1] Temple Univ, Sch Med, Microbiol & Immunol & Thrombosis Res Ctr, Philadelphia, PA 19140 USA

来源：

FRONTIERS IN BIOSCIENCE-LANDMARK | 2002年 / 7卷

关键词：

tyrosine phosphorylation; focal contacts; paxillin; FAK; p130CAS; cell migration; cell spreading; review;

D O I：

10.2741/panetti

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：

Integrins are transmembrane receptors that mediate cell attachment to the substrate. At the cytoplasmic surface of the integrin, cytoskeletal proteins cluster into focal adhesions. The focal adhesions contain multiple proteins that provide a structural and signaling complex inside the cell. This review focuses on three of the cytoskeletal components of the focal adhesion, paxillin, FAK, and p130CAS, that are phosphorylated and play a regulatory role in cell spreading and cell migration. A brief discussion is included of tyrosine phosphorylation of the integrin in relation to localization and phosphorylation of these cytoskeletal proteins. The phosphorylation of integrins and cytoskeletal proteins regulates localization and downstream signaling with profound effects on cell movement.

引用

页码：D143 / D150

页数：8

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