Reference work entry
The activity of the Src family tyrosine kinases (SFKs), known as representative proto-oncogene products, is negatively regulated by the phosphorylation at their C-terminal regulatory tyrosine (Brown and Cooper 1996; Cooper et al. 1986). The protein tyrosine kinase Csk was identified as a specific kinase that directs the negative regulatory sites of SFKs (Nada et al. 1991; Okada and Nakagawa 1988). Analysis of Csk-deficient mice and cells provided evidence that Csk functions as an indispensable negative regulator of SFKs (Nada et al. 1991, 1993). The molecular basis of Csk-SFK interaction is recently verified by the crystal structure of Csk/c-Src complex (Levinson et al. 2008). Csk is expressed ubiquitously, but is highly concentrated in developing nervous system and the immune system (Okada et al. 1991). Csk is highly conserved in animal kingdom from the unicellular choanoflagellate to human in parallel with SFKs...
- D’Arco M, Giniatullin R, Leone V, Carloni P, Birsa N, Nair A, Nistri A, Fabbretti E. The C-terminal Src inhibitory kinase (Csk)-mediated tyrosine phosphorylation is a novel molecular mechanism to limit P2X3 receptor function in mouse sensory neurons. J Biol Chem. 2009;284:21393–401.PubMedPubMedCentralCrossRefGoogle Scholar
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