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Journal of Biochemistry 2005 137(1):61-67; doi:10.1093/jb/mvi011
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© 2005 The Japanese Biochemical Society

BIOCHEMISTRY

Association of c-Src with p52Shc in Mitotic NIH3T3 Cells as Revealed by Src-Shc Binding Site–Specific Antibodies

Ken-ichi Sato*, Tetsushi Iwasaki and Yasuo Fukami

Research Center for Environmental Genomics, Kobe University, Nada, Kobe 657-8501

In a previous study, we presented evidence that the adaptor protein Shc interacts with and activates the tyrosine kinase c-Src without affecting the phosphorylation state of Tyr-527 in c-Src. Here we show that Shc-mediated c-Src activation occurs in mitotic NIH 3T3 cells. Co-immunoprecipitation studies demonstrate that the c-Src–p52Shc complex involves the activation segment/inter-DFG-APE (IDA) region of c-Src and the amino-terminal region of p52Shc. The complex formation contributes to the c-Src activation, because (i) specific activity of c-Src associated with p52Shc is higher than that of the total c-Src, and (ii) a recombinant protein containing the c-Src IDA sequence disrupts the complex and decreases the c-Src activity. Anti–Src IDA antibody can activate c-Src in vitro, and synthetic peptides that cover the carboxyl-terminal half of the Src IDA region interfere with the kinase-activating effect of anti–Src IDA antibody. These results support the idea that dephosphorylation-independent activation of c-Src by Shc is mediated by a molecular interaction involving the c-Src IDA region.

* To whom correspondence should be addressed. Tel: +81-78-803-5953, Fax: +81-78-803-5951, E-mail: kksato{at}kobe-u.ac.jp


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