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A more recent version of this article appeared on July 1, 2003
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Submitted on August 16, 2002
Revised on February 12, 2003
Accepted on February 13, 2003
-PIX complex and promotes Rac-dependent relocalization of Paxillin to focal contacts
1 Molecular Oncology Group, McGill University Health Centre,
Department of Biochemistry, McGill University, Montreal, Quebec, Canada
2 Molecular Oncology Group, McGill University Health Centre,
Department of Medicine, McGill University, Montreal, Quebec, Canada
3 Department of Cell and Developmental Biology,
SUNY Upstate Medical University, Syracuse, NY, USA
4 Molecular Oncology Group, McGill University Health Centre,
Departments of Biochemistry, Medicine and Oncology, McGill University, Montreal, Quebec, Canada
* Corresponding author. E-mail address: morag{at}molonc.mcgill.ca.
We have previously demonstrated that the CrkII and CrkL adapter proteins are required for the spreading of epithelial colonies and the breakdown of adherens junctions in response to hepatocyte growth factor (HGF). When overexpressed, CrkII and CrkL promote lamellipodia formation, cell spreading and the loss of epithelial adherens junctions in the absence of HGF. The exact mechanism by which Crk proteins elicit these changes is unclear. We show that the overexpression of CrkII or CrkL, but not SH2 or amino-terminal SH3 domain mutant Crk proteins, promotes the relocalization of Paxillin to focal contacts throughout the cell and within lamellipodia in a Rac-dependent manner. In stable cell lines overexpressing CrkII, enhanced lamellipodia formation and cell spreading correlate with an increased association of CrkII with Paxillin, GIT2 (an ARF-GAP) and 
-PIX (a Rac1 exchange factor). Mutants of Paxillin that fail to associate with Crk or GIT2, or do not target to focal adhesions inhibit Crk-dependent cell spreading and lamellipodia formation. We conclude from these studies that the association of Crk with Paxillin is important for the spreading of epithelial colonies, by influencing the recruitment of Paxillin to focal complexes and promoting the enhanced assembly of Paxillin/GIT2/-PIX complexes.
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