RGD Reference Report - Transmembrane phosphoprotein Cbp regulates the activities of Src-family tyrosine kinases. - Rat Genome Database

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

Authors: Kawabuchi, M  Satomi, Y  Takao, T  Shimonishi, Y  Nada, S  Nagai, K  Tarakhovsky, A  Okada, M 
Citation: Kawabuchi M, etal., Nature 2000 Apr 27;404(6781):999-1003.
RGD ID: 632469
Pubmed: PMID:10801129   (View Abstract at PubMed)
DOI: DOI:10.1038/35010121   (Journal Full-text)

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-PTKs. 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 signalling. These findings reveal Cbp as a new component of the regulatory mechanism controlling the activity of membrane-associated Src-PTKs.



Objects referenced in this article
Gene Pag1 phosphoprotein membrane anchor with glycosphingolipid microdomains 1 Rattus norvegicus

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