Induced focal adhesion kinase (FAK) expression in FAK-null cells enhances cell spreading and migration requiring both auto- and activation loop phosphorylation sites and inhibits adhesion-dependent tyrosine phosphorylation of Pyk2
Owen, J.D.; Ruest, P.J.; Fry, D.W.; Hanks, S.K.
Molecular and Cellular Biology 19(7): 4806-4818
1999
ISSN/ISBN: 0270-7306 PMID: 10373530 DOI: 10.1128/mcb.19.7.4806
Accession: 010829452
Focal adhesion kinase (FAK) is a nonreceptor protein tyrosine kinase involved in integrin-mediated control of cell behavior. Following cell adhesion to components of the extracellular matrix, FAK becomes phosphorylated at multiple sites, including tyrosines 397, 576, and 577. Tyr-397 is an autophosphorylation site that promotes interaction with c-Src or Fyn.
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