Src Kinases

Src kinases consist of eight non-receptor tyrosine kinases (Src, Fyn, Yes, Lck, Lyn, Hck, Fgr and Blk) that interact with the intracellular domains of growth factor/cytokine receptors, GPCRs and integrins. Members of the Src kinase family have 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.

c-Src, Fyn and Yes are ubiquitously expressed, although high levels of c-Src are found in platelets, neural tissue and osteoclasts. For c-Src, autophosphorylation of Tyr⁴¹⁸ and dephosphorylation of Tyr⁵³⁰ is required to switch the kinase from the inactive 'closed' formation to the active 'open' formation. c-Src can be inactivated by two kinases, c-Src kinase (CSK) and CSK homologous kinase (CHK), both of which phosphorylate Tyr⁵³⁰ of c-Src. The activity of the Src kinase family can also be regulated by phosphatases (e.g. SHP1), by binding to adaptor proteins (e.g. Cbp) and by proteasomal degradation. Src kinases are key upstream mediators of both the PI 3-K and MAPK signaling pathways, and have been shown to have important roles in cell proliferation, migration and survival.

External sources of pharmacological information for Src Kinases :

• BJP Guide

Src Kinase Gene Data