Document Detail


Possible v-Crk-induced transformation through activation of Src kinases.
MedLine Citation:
PMID:  8537387     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
p47gag-crk (v-Crk) encoded by avian sarcoma virus CT10, causes an elevation of tyrosine phosphorylation of several cellular proteins. The lack of a protein-tyrosine kinase domain in v-Crk suggests its co-operation with cellular protein-tyrosine kinase activity. We have shown that suppression of a certain fraction of c-Src activity by Csk may require the binding of Csk to tyrosine-phosphorylated paxillin. In this study, we detected co-immunoprecipitation of tyrosine-phosphorylated paxillin with v-Crk in CT10-transformed chicken embryo fibroblasts (CEF), and demonstrated that v-Crk binding to paxillin can inhibit Csk binding to paxillin. A phosphotyrosine peptide, which can inhibit v-Crk binding to paxillin, did not inhibit Csk binding to paxillin, suggesting that v-Crk and Csk bind to different tyrosine-phosphorylated sites in paxillin. We also found that the kinase activity of the endogenous c-Src in CEF is elevated severalfold after CT10-transformation. We therefore suggest that the competitive binding of overexpressed v-Crk affects an efficient interaction of Csk with tyrosine-phosphorylated paxillin in CT10-transformed CEF. This would result in a failure in the suppression of the kinase activities of a population of c-Src and other Src family protein-tyrosine kinases as well, and these kinases may then contribute to the phosphorylation of cellular proteins in CT10-transformed CEF.
Authors:
H Sabe; S E Shoelson; H Hanafusa
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  The Journal of biological chemistry     Volume:  270     ISSN:  0021-9258     ISO Abbreviation:  J. Biol. Chem.     Publication Date:  1995 Dec 
Date Detail:
Created Date:  1996-02-08     Completed Date:  1996-02-08     Revised Date:  2009-11-19    
Medline Journal Info:
Nlm Unique ID:  2985121R     Medline TA:  J Biol Chem     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  31219-24     Citation Subset:  IM    
Affiliation:
Laboratory of Molecular Oncology, Rockefeller University, New York, New York 10021-6399, USA.
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Animals
Cell Transformation, Viral*
Cells, Cultured
Chick Embryo
Cytoskeletal Proteins / metabolism
Enzyme Activation
Molecular Sequence Data
Oncogene Protein pp60(v-src) / metabolism*
Oncogene Protein v-crk
Paxillin
Phosphoproteins / metabolism
Phosphorylation
Protein-Tyrosine Kinases / metabolism*
Retroviridae Proteins, Oncogenic / metabolism*
Substrate Specificity
Grant Support
ID/Acronym/Agency:
CA44356/CA/NCI NIH HHS
Chemical
Reg. No./Substance:
0/Cytoskeletal Proteins; 0/Oncogene Protein v-crk; 0/Paxillin; 0/Phosphoproteins; 0/Retroviridae Proteins, Oncogenic; EC 2.7.10.1/Protein-Tyrosine Kinases; EC 2.7.10.2/Oncogene Protein pp60(v-src)

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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