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Science 22 June 1990:
Vol. 248. no. 4962, pp. 1537 - 1539
DOI: 10.1126/science.1694307

Articles

Science, Vol 248, Issue 4962, 1537-1539
Copyright © 1990 by American Association for the Advancement of Science


articles

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

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

Rockefeller University, New York, NY 10021.

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.


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