1k9a

Structural highlights

Function

[CSK_RAT] Non-receptor tyrosine-protein kinase that plays an important role in the regulation of cell growth, differentiation, migration and immune response. Phosphorylates tyrosine residues located in the C-terminal tails of Src-family kinases (SFKs) including LCK, SRC, HCK, FYN, LYN or YES1. Upon tail phosphorylation, Src-family members engage in intramolecular interactions between the phosphotyrosine tail and the SH2 domain that result in an inactive conformation. To inhibit SFKs, CSK is recruited to the plasma membrane via binding to transmembrane proteins or adapter proteins located near the plasma membrane. Suppresses signaling by various surface receptors, including T-cell receptor (TCR) and B-cell receptor (BCR) by phosphorylating and maintaining inactive several positive effectors such as FYN or LCK (By similarity).^{[1] [2]}

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

• Tyrosine kinase

References

1. ↑ Okada M, Nada S, Yamanashi Y, Yamamoto T, Nakagawa H. CSK: a protein-tyrosine kinase involved in regulation of src family kinases. J Biol Chem. 1991 Dec 25;266(36):24249-52. PMID:1722201
2. ↑ Ruzzene M, James P, Brunati AM, Donella-Deana A, Pinna LA. Regulation of c-Fgr protein kinase by c-Src kinase (CSK) and by polycationic effectors. J Biol Chem. 1994 Jun 3;269(22):15885-91. PMID:7515063
3. ↑ Ogawa A, Takayama Y, Sakai H, Chong KT, Takeuchi S, Nakagawa A, Nada S, Okada M, Tsukihara T. Structure of the carboxyl-terminal Src kinase, Csk. J Biol Chem. 2002 Apr 26;277(17):14351-4. Epub 2002 Mar 7. PMID:11884384 doi:10.1074/jbc.C200086200