Stimulation of cell migration by overexpression of focal adhesion kinase and its association with Src and Fyn

J Cell Sci. 1996 Jul;109 ( Pt 7):1787-94. doi: 10.1242/jcs.109.7.1787.


Cellular interactions with the extracellular matrix proteins play important roles in a variety of biological processes. Recent studies suggest that integrin-mediated cell-matrix interaction can transduce biochemical signals across the plasma membrane to regulate cellular functions such as proliferation, differentiation and migration. These studies have implicated a critical role of focal adhesion kinase (FAK) in integrin-mediated signal transduction pathways. We report here that overexpression of FAK in CHO cells increased their migration on fibronectin. A mutation of the major autophosphorylation site Y397 in FAK abolished its ability to stimulate cell migration, while phosphorylation of Y397 in a kinase-defective FAK by endogenous FAK led to increased migration. We also find that the wild-type and the kinase-defective FAK were associated with Src and Fyn in CHO cells whereas the F397 mutant was not. These results directly demonstrate a functional role for FAK in integrin signaling leading to cell migration. They also provide evidence for the functional significance of FAK/Src complex formation in vivo.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • CHO Cells
  • Cell Adhesion Molecules / biosynthesis
  • Cell Adhesion Molecules / genetics*
  • Cell Movement / genetics*
  • Cricetinae
  • Fibronectins
  • Focal Adhesion Protein-Tyrosine Kinases
  • Gene Expression Regulation
  • Genes, src*
  • Mutation
  • Protein-Tyrosine Kinases / biosynthesis
  • Protein-Tyrosine Kinases / genetics*
  • Proto-Oncogene Proteins / genetics*
  • Proto-Oncogene Proteins c-fyn


  • Cell Adhesion Molecules
  • Fibronectins
  • Proto-Oncogene Proteins
  • Protein-Tyrosine Kinases
  • Focal Adhesion Protein-Tyrosine Kinases
  • Proto-Oncogene Proteins c-fyn