Focal Adhesion Kinase (FAK) is a cytoplasmic tyrosine kinase that colocalizes with integrins in focal adhesions. This cellular localization is directed by a 125 amino acid sequence at the C-terminus called "Focal Adhesion Targeting" sequence (FAT). The binding of extracellular matrix ligands to integrins triggers autophosphorylation at Tyr-397, and activation of FAK through phosphorylation of Tyr residues (Tyr-576 and Tyr-577) in the kinase domain activation loop. For example, cell adhesion to a fibronectin substratum involves concurrent activation of Src and phosphorylation of the FAK activation loop. In addition, phosphorylation of other Tyr residues (Tyr-925 and Tyr-861) creates binding sites for SH2 domains of intracellular signaling molecules such as Src, PI3 kinase, and Grb2. FAK's ability to bind numerous structural and signaling proteins via a variety of interactions is important for FAK activation level and for FAK interaction with a variety of substrates localized to sites of cell adhesion. Thus, FAK activity is regulated by a complex set of phosphorylation sites, and this phospho-regulation could be important for cell motility, cell growth, cytoskeletal organization and adhesion-dependent cell survival.
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