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Molecular Cloning and Expression of Chicken C-Terminal Src Kinase: Lack of Stable Association with c-Src Protein

Hisataka Sabe, Beatrice Knudsen, Masato Okada, Shigeyuki Nada, Hachiro Nakagawa and Hidesaburo Hanafusa
Proceedings of the National Academy of Sciences of the United States of America
Vol. 89, No. 6 (Mar. 15, 1992), pp. 2190-2194
Stable URL: http://www.jstor.org/stable/2358669
Page Count: 5
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Since scans are not currently available to screen readers, please contact JSTOR User Support for access. We'll provide a PDF copy for your screen reader.
Molecular Cloning and Expression of Chicken C-Terminal Src Kinase: Lack of Stable Association with c-Src Protein
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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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