IMR Press / FBL / Volume 7 / Issue 4 / DOI: 10.2741/panetti

Frontiers in Bioscience-Landmark (FBL) is published by IMR Press from Volume 26 Issue 5 (2021). Previous articles were published by another publisher on a subscription basis, and they are hosted by IMR Press on imrpress.com as a courtesy and upon agreement with Frontiers in Bioscience.

Open Access Article
Tyrosine phosphorylation of paxillin, FAK, and p130CAS: effects on cell spreading and migration
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1 Department of Microbiology and Immunology and Thrombosis Research Center, Temple University School of Medicine, Philadelphia, PA 19140, USA
Academic Editor:Alexander Tsygankov
Front. Biosci. (Landmark Ed) 2002, 7(4), 143–150; https://doi.org/10.2741/panetti
Published: 1 January 2002
(This article belongs to the Special Issue Tyrosine protein phosphorylation in cell signaling)
Abstract

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.

Keywords
Tyrosine phosphorylation
Focal contacts
Paxillin
FAK
p130CAS
Cell migration
Cell spreading
Review
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