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Vol. 18, Issue 1, 253-264, January 2007
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PIX
,||
Departments of *Anesthesiology and Critical Care Medicine, Biomedical Engineering, Cell Biology, and ||Pediatrics, Johns Hopkins University School of Medicine, Baltimore, MD 21287; and School of Biological Sciences, Seoul National University, Seoul 151-742, South Korea
Submitted March 17, 2006;
Revised October 25, 2006;
Accepted October 27, 2006
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 after 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 
PIX and thereby increased its binding to Rac1. In addition, 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 PIX.
The online version of this contains supplemental material at MBC Online (http://www.molbiolcell.org). This article was published online ahead of print in MBC in Press (http://www.molbiolcell.org/cgi/doi/10.1091/mbc.E06-03-0207) on November 8, 2006.
Address correspondence to: Lewis Romer (Lromer{at}jhmi.edu)
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