SRC

SRC

The Src family of protein tyrosine kinases (SFKs; EC 2.7.10.2) plays key roles in regulating signal transduction by a diverse set of cell surface receptors in the context of multiple cellular environments. The nine members of the Src family include Src, Lck, Hck, Fyn, Blk, Lyn, Fgr, Yes, and Yrk, and all share a very similar domain structure with a high degree of homology in the SH1 (catalytic), linker, SH2 (p-Tyr binding), SH3 (protein-protein interaction) and SH4 (membrane association) domains. In the auto-inhibited, tail-phosphorylated (Tyr527) state, the SH3 and SH2 domains turn inward and make intramolecular interactions that lock the catalytic domain in an inactive conformation. Several lines of evidence indicate that loss of Tyr527 phosphorylation by protein tyrosine phosphatases (PTPs) leads to activation of Src catalytic activity.

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More About SRC

The Src family of protein tyrosine kinases (SFKs; EC 2.7.10.2) plays key roles in regulating signal transduction by a diverse set of cell surface receptors in the context of multiple cellular environments. The nine members of the Src family include Src, Lck, Hck, Fyn, Blk, Lyn, Fgr, Yes, and Yrk, and all share a very similar domain structure with a high degree of homology in the SH1 (catalytic), linker, SH2 (p-Tyr binding), SH3 (protein-protein interaction) and SH4 (membrane association) domains. In the auto-inhibited, tail-phosphorylated (Tyr527) state, the SH3 and SH2 domains turn inward and make intramolecular interactions that lock the catalytic domain in an inactive conformation. Several lines of evidence indicate that loss of Tyr527 phosphorylation by protein tyrosine phosphatases (PTPs) leads to activation of Src catalytic activity[1],[2].

SRC-family members listed: SRC, Lck, Lyn

[1] S.M. Thomas, J.S. Brugge. Cellular functions regulated by Src family kinases. Annu. Rev. Cell Dev. Biol. 1997, 13, 513-609.
[2] M.P. Playford, M.D. Schaller. The interplay between Src and integrins in normal and tumor biology. Oncogene 2004, 23, 7928-7946. 

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