Publication Date:
1990-06-22
Description:
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.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Matsuda, M -- Mayer, B J -- Fukui, Y -- Hanafusa, H -- AI 07233/AI/NIAID NIH HHS/ -- CA44356/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1990 Jun 22;248(4962):1537-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Rockefeller University, New York, NY 10021.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1694307" target="_blank"〉PubMed〈/a〉
Keywords:
Animals
;
Cell Line, Transformed
;
Cell Transformation, Viral
;
Oncogene Protein v-crk
;
Phosphorylation
;
Phosphotyrosine
;
Precipitin Tests
;
Protein Binding
;
Protein-Tyrosine Kinases/*metabolism
;
Proto-Oncogene Proteins/*metabolism
;
Retroviridae Proteins/*metabolism
;
*Signal Transduction
;
Tyrosine/*analogs & derivatives/metabolism
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
