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MBC in Press, published online ahead of print November 8, 2006
Mol. Biol. Cell 10.1091/mbc.E06-03-0207

A more recent version of this article appeared on January 1, 2007
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Submitted on March 17, 2006
Revised on October 25, 2006
Accepted on October 27, 2006

FAK Potentiates Rac1 Activation and Localization to Matrix Adhesion Sites: A Role for {beta}PIX

Fumin Chang,* Christopher A. Lemmon,*{dagger} Dongeun Park,{ddagger} and Lewis H. Romer*{sect}||

Departments of *Anesthesiology and Critical Care Medicine, {dagger}Biomedical Engineering, {sect}Cell Biology, and ||Pediatrics, Johns Hopkins University School of Medicine, Baltimore, MD 21287; {ddagger}School of Biological Sciences, Seoul National University, Seoul 151-742, South Korea

Monitoring Editor: Carole Parent

FAK, a cytoplasmic protein tyrosine kinase, is activated and localized to focal adhesions upon cell attachment to extracellular matrix. FAK null cells spread poorly and exhibit altered focal adhesion turnover. Rac1 is a member of the Rho-family GTPases that promotes membrane ruffling, leading edge extension, and cell spreading. We investigated the activation and subcellular location of Rac1 in FAK null and FAK reexpressing fibroblasts. FAK reexpressers had a more robust pattern of Rac1 activation following cell adhesion to fibronectin than the FAK null cells. Translocation of Rac1 to focal adhesions was observed in FAK reexpressers, but seldom in FAK null cells. Experiments with constitutively active L61Rac1 and dominant negative N17Rac1 indicated that the activation state of Rac1 regulated its localization to focal adhesions. We demonstrated that FAK tyrosine-phosphorylated {beta}PIX, and thereby increased its binding to Rac1. In addition, {beta}PIX facilitated the targeting of activated Rac1 to focal adhesions and the efficiency of cell spreading. These data indicate that FAK has a role in the activation and focal adhesion translocation of Rac1 through the tyrosine phosphorylation of {beta}PIX.

Address correspondence to: Lewis H. Romer (Lromer{at}jhmi.edu)




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