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. 1992 Mar 15;89(6):2190–2194. doi: 10.1073/pnas.89.6.2190

Molecular cloning and expression of chicken C-terminal Src kinase: lack of stable association with c-Src protein.

H Sabe 1, B Knudsen 1, M Okada 1, S Nada 1, H Nakagawa 1, H Hanafusa 1
PMCID: PMC48622  PMID: 1372437

Abstract

Cloning and sequencing of chicken C-terminal Src kinase (CSK), a tyrosine kinase that phosphorylates the regulatory C-terminal tyrosine residue present on cytoplasmic tyrosine kinases of the Src family, demonstrated a high degree of interspecies conservation as well as src homology 2 and 3 domains N-terminal to the kinase domain. The lack of autophosphorylation sites distinguishes CSK from other tyrosine kinases. CSK is unique and does not belong to a gene family, suggesting that it may phosphorylate other members of the Src family of tyrosine kinases in addition to c-Src. Since complex formation between c-Src and CSK seemed a likely regulatory step in the control of c-Src kinase activity, such an association was investigated by immunoprecipitation and Western blotting as well as intracellular localization studies. Although some portions of CSK were found in a membrane fraction, no complex formation between CSK and c-Src was observed, suggesting that the src homology 2 domain of CSK does not play a role in the direct interaction of c-Src.

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