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

DOI PDF 被引用文献3件
  • Leslie A. Cary
    Cornell University Cancer Biology Laboratories, Department of Pathology, College of Veterinary Medicine , , Ithaca, NY 14853, USA
  • James F. Chang
    Cornell University Cancer Biology Laboratories, Department of Pathology, College of Veterinary Medicine , , Ithaca, NY 14853, USA
  • Jun-Lin Guan
    Cornell University Cancer Biology Laboratories, Department of Pathology, College of Veterinary Medicine , , Ithaca, NY 14853, USA

書誌事項

公開日
1996-07-01
権利情報
  • http://www.biologists.com/user-licence-1-1/
DOI
  • 10.1242/jcs.109.7.1787
公開者
The Company of Biologists

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<jats:title>ABSTRACT</jats:title> <jats:p>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.</jats:p>

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