1csk

Structural highlights

Function

[CSK_HUMAN] 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.^{[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. ↑ Bergman M, Mustelin T, Oetken C, Partanen J, Flint NA, Amrein KE, Autero M, Burn P, Alitalo K. The human p50csk tyrosine kinase phosphorylates p56lck at Tyr-505 and down regulates its catalytic activity. EMBO J. 1992 Aug;11(8):2919-24. PMID:1639064
2. ↑ Sun G, Budde RJ. Expression, purification, and initial characterization of human Yes protein tyrosine kinase from a bacterial expression system. Arch Biochem Biophys. 1997 Sep 1;345(1):135-42. PMID:9281320 doi:10.1006/abbi.1997.0236
3. ↑ Borchert TV, Mathieu M, Zeelen JP, Courtneidge SA, Wierenga RK. The crystal structure of human CskSH3: structural diversity near the RT-Src and n-Src loop. FEBS Lett. 1994 Mar 14;341(1):79-85. PMID:7511113