C-terminal Src kinase (Csk) is a ubiquitously expressed tyrosine kinase that phosphorylates c-Src at Tyr-530, down-regulating Src kinase activity. In vitro, Csk can also phosphorylate other members of the Src family, such as Lck, c-Fgr, Fyn, and Lyn, at their conserved C-terminal tyrosine residue. The structure of Csk resembles c-Src and includes an SH3, SH2, and a catalytic domain. However, Csk lacks the catalytic domain autophosphorylation site, the C-terminal regulatory tyrosine and the N-terminal myristoylation signal of c-Src. Csk is involved in the regulation of integrin signaling during cell attachment and interacts with FAK and paxillin in podosomes. Csk gene knockout leads to neural tube defects and embryonic lethality in mice. In Csk-deficient mouse embryonic fibroblasts, actin stress fiber formation via G-protein signaling is completely abolished, suggesting that Csk may also play a critical role in linking G-protein signals to actin cytoskeletal reorganization.
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*For more information, see UniProt Accession P41240
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*All molecular weights (MW) are confirmed by comparison to Bio-Rad Rainbow Markers and to western blot mobilities of known proteins with similar MW.
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