Phosphorylation of FAK by Src kinases

Stable Identifier
Reaction [transition]
Mus musculus
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Phosphorylation of FAK by Src kinases

Phosphorylation of Tyr397 in FAK triggers the phosphorylation of other tyrosine residues (Tyr407, Tyr576, Tyr577, Tyr861 and Tyr925) in a Src-dependent manner. The initial phosphorylation of FAK at Tyr397 is thought to create a high-affinity binding site for SH2 domains, enabling formation of a signalling complex between FAK and members of the Src-family kinases. Tyr-576 and Tyr-577 are located in the central catalytic domain and their phosphorylation is required for the maximum kinase activity of FAK. The tyrosine phosphorylation of these residues is likely to be mediated by Src (or other members of the src family).

Literature References
PubMed ID Title Journal Year
7529876 Tyrosine phosphorylation of focal adhesion kinase at sites in the catalytic domain regulates kinase activity: a role for Src family kinases

Calalb, MB, Polte, TR, Hanks, SK

Mol Cell Biol 1995
12387730 Site-specific phosphorylation of platelet focal adhesion kinase by low-density lipoprotein

Relou, IA, Bax, LA, van Rijn, HJ, Akkerman, JW

Biochem J 2003
Catalyst Activity

protein tyrosine kinase activity of Src [cytosol]

Orthologous Events
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