Science. 1990 Jun 22;248(4962):1537-9.

Binding of transforming protein, P47gag-crk, to a broad range of phosphotyrosine-containing proteins.

Matsuda M, Mayer BJ, Fukui Y, Hanafusa H.

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Rockefeller University, New York, NY 10021.

Abstract

Although the oncogene product of CT10 virus, P47gag-crk, does not itself phosphorylate proteins at tyrosine residues, it elevates phosphotyrosine in transformed cells. The P47gag-crk oncoprotein contains SH2 and SH3 domains, which are conserved in several proteins involved in signal transduction, including nonreceptor tyrosine kinases. P47gag-crk bound in vitro to phosphotyrosine-containing proteins from crk-transformed cells and from cells transformed by oncogenic tyrosine kinases. The association between P47gag-crk and p60v-src, a phosphotyrosine-containing protein, was abolished by dephosphorylation of p60v-src. This suggests that the SH2 and SH3 regions function to regulate protein interactions in a phosphotyrosine-dependent manner.

PMID:: 1694307; [PubMed - indexed for MEDLINE]

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