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Molecular and Cellular Biology, July 2006, p. 5155-5167, Vol. 26, No. 13
0270-7306/06/$08.00+0     doi:10.1128/MCB.02186-05
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Direct Interaction of Focal Adhesion Kinase (FAK) with Met Is Required for FAK To Promote Hepatocyte Growth Factor-Induced Cell Invasion{dagger}

Shu-Yi Chen and Hong-Chen Chen*

Department of Life Science and Graduate Institute of Biomedical Sciences, National Chung Hsing University, Taichung 40227, Taiwan

Received 11 November 2005/ Returned for modification 30 December 2005/ Accepted 20 April 2006

Focal adhesion kinase (FAK) has been implicated to be a point of convergence of integrin and growth factor signaling pathways. Here we report that FAK directly interacts with the hepatocyte growth factor receptor c-Met. Phosphorylation of c-Met at Tyr-1349 and, to a lesser extent, Tyr-1356 is required for its interaction with the band 4.1 and ezrin/radixin/moesin homology domain (FERM domain) of FAK. The F2 subdomain of the FAK FERM domain alone is sufficient for Met binding, in which a patch of basic residues (216KAKTLRK222) are critical for the interaction. Met-FAK interaction leads to FAK activation and subsequent contribution to hepatocyte growth factor-induced cell motility and cell invasion. Our results provide evidence that constitutive Met-FAK interaction may be a critical determinant for tumor cells to acquire invasive potential.

* Corresponding author. Mailing address: Department of Life Science and Graduate Institute of Biomedical Sciences, National Chung Hsing University, 250 Kuo-Kuang Road, Taichung 40227, Taiwan. Phone: 886-4-22854922. Fax: 886-4-22853469. E-mail: hcchen{at}nchu.edu.tw.

{dagger} Supplemental material for this article may be found at http://mcb.asm.org/.

Molecular and Cellular Biology, July 2006, p. 5155-5167, Vol. 26, No. 13
0270-7306/06/$08.00+0     doi:10.1128/MCB.02186-05
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



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