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Volume 271, Number 43, Issue of October 25, 1996 pp. 27130-27137
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.

Specific Association of Tyrosine-phosphorylated c-Cbl with Fyn Tyrosine Kinase in T Cells

(Received for publication, May 13, 1996, and in revised form, July 24, 1996)

Alexander Y. Tsygankov Dagger , Sandeep Mahajan , John E. Fincke Dagger and Joseph B. Bolen par

From the Dagger  Department of Microbiology and Immunology, Temple University School of Medicine, Philadelphia, Pennsylvania 19140,  Biotherapy Program, University of Minnesota School of Medicine, Roseville, Minnesota 55113, and par  DNAX Research Institute of Molecular and Cellular Biology, Palo Alto, California 94304

Fyn is a Src family protein-tyrosine kinase functionally associated with the T-cell antigen receptor (TcR)/CD3 receptor complex. We have demonstrated earlier that the TcR/CD3-induced activation of Fyn results in tyrosine phosphorylation of several Fyn-associated proteins, including a protein of 116 kDa. In this report, we identify the Fyn-associated 116-kDa phosphoprotein (p116) as c-Cbl. The identity of p116 has been demonstrated by its specific reactivity with anti-Cbl and similarity of phosphopeptides generated by V8 proteolysis of phospho-Cbl and p116. We demonstrate here that the association of Fyn and c-Cbl is direct and does not require the presence of other proteins. We also demonstrate that Fyn is the Src family kinase that preferentially interacts with c-Cbl in T cells. The fraction of c-Cbl capable of coprecipitating with Fyn is increased by TcR/CD3 ligation. This increase is likely due to the involvement of Fyn SH2 in the interactions between Fyn and tyrosine-phosphorylated c-Cbl.


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