Reduced cell motility and enhanced focal adhesion contact formation in cells from FAK-deficient mice

Nature. 1995 Oct 12;377(6549):539-44. doi: 10.1038/377539a0.


The intracellular protein tyrosine kinase FAK (focal adhesion kinase) was originally identified gy its high level of tyrosine phosphorylation in v-src-transformed cells. FAK is also highly phosphorylated during early development. In cultured cells it is localized to focal adhesion contacts and becomes phosphorylated and activated in response to integrin-mediated binding of cells to the extracellular matrix, suggesting an important role in cell adhesion and/or migration. We have generated FAK-deficient mice by gene targeting to examine the role of FAK during development. Mutant embryos displayed a general defect of mesoderm development, and cells from these embryos had reduced mobility in vitro. Surprisingly, the number of focal adhesions was increased in FAK-deficient cells, suggesting that FAK may be involved in the turnover of focal adhesion contacts during cell migration.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Base Sequence
  • Cell Adhesion / physiology*
  • Cell Adhesion Molecules / genetics
  • Cell Adhesion Molecules / physiology*
  • Cell Line
  • Cell Movement / physiology*
  • Cytoskeletal Proteins / metabolism
  • DNA Primers
  • Embryo, Mammalian / cytology
  • Embryo, Mammalian / enzymology*
  • Embryonic and Fetal Development
  • Focal Adhesion Kinase 1
  • Focal Adhesion Protein-Tyrosine Kinases
  • Gene Targeting
  • Mesoderm / cytology
  • Mice
  • Molecular Sequence Data
  • Phosphorylation
  • Protein-Tyrosine Kinases / genetics
  • Protein-Tyrosine Kinases / physiology*
  • Tyrosine / metabolism


  • Cell Adhesion Molecules
  • Cytoskeletal Proteins
  • DNA Primers
  • Tyrosine
  • Protein-Tyrosine Kinases
  • Focal Adhesion Kinase 1
  • Focal Adhesion Protein-Tyrosine Kinases
  • Ptk2 protein, mouse