Transmembrane phosphoprotein Cbp regulates the activities of Src-family tyrosine kinases

Masahiro Kawabuchi, Yoshinori Satomi, Toshifumi Takao, Yasutsugu Shimonishi, Shigeyuki Nada, Katsuya Nagai, Alexander Tarakhovsky () and Masato Okada ()
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Masahiro Kawabuchi: Divisions of Protein Metabolism
Yoshinori Satomi: Organic Chemistry, Institute for Protein Research, Osaka University
Toshifumi Takao: Organic Chemistry, Institute for Protein Research, Osaka University
Yasutsugu Shimonishi: Organic Chemistry, Institute for Protein Research, Osaka University
Shigeyuki Nada: Institute of Scientific and Industrial Research Osaka University
Katsuya Nagai: Divisions of Protein Metabolism
Alexander Tarakhovsky: Laboratory for Lymphocyte Signalling, Institute for Genetics, University of Cologne
Masato Okada: Divisions of Protein Metabolism

Nature, 2000, vol. 404, issue 6781, 999-1003

Abstract: Abstract The Src family of protein tyrosine kinases (Src-PTKs) is important in the regulation of growth and differentiation of eukaryotic cells. The activity of Src-PTKs in cells of different types is negatively controlled by Csk, which specifically phosphorylates a conserved regulatory tyrosine residue at the carboxy-terminal tail of the Src-PTKs1,2,3. Csk is mainly cytoplasmic and Src-PTKs are predominantly membrane-associated. This raises a question about the mechanism of interaction between these enzymes. Here we present Cbp—a transmembrane phosphoprotein that is ubiquitously expressed and binds specifically to the SH2 domain of Csk. Cbp is involved in the membrane localization of Csk and in the Csk-mediated inhibition of c-Src. In the plasma membrane Cbp is exclusively localized in the GM1 ganglioside-enriched detergent-insoluble membrane domain, which is important in receptor-mediated signalling4,5,6,7,8. These findings reveal Cbp as a new component of the regulatory mechanism controlling the activity of membrane-associated Src-PTKs.

Date: 2000
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DOI: 10.1038/35010121

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