Direct interaction of focal adhesion kinase (FAK) with Met is required for FAK to promote hepatocyte growth factor-induced cell invasion

Shu Yi Chen, Hong Chen Chen

Research output: Contribution to journalArticlepeer-review

124 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)5155-5167
Number of pages13
JournalMolecular and Cellular Biology
Volume26
Issue number13
DOIs
Publication statusPublished - 2006 Jul

All Science Journal Classification (ASJC) codes

  • Molecular Biology
  • Cell Biology

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