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Volume 270, Number 16, Issue of April 21, pp. 9115-9120, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
Identification of the Major Tyrosine Kinase Substrate in Signaling Complexes Formed after Engagement of Fc Receptors

Antonio Marcilla , Octavio M. Rivero-Lezcano , Alka Agarwal , Keith C. Robbins

We have recently identified the protein product of the c- cbl proto-oncogene as an SH3 binding protein expressed in macrophages. To investigate the possibility that p120is involved in signaling pathways initiated by cell surface receptors for IgG (FcR), lysates of HL60 cells were examined for tyrosine phosphorylation of p120upon FcR engagement. Our findings demonstrate that p120is tyrosine-phosphorylated upon FcR engagement and that this molecule represents the major tyrosine kinase substrate in this signaling pathway. Protein complexes containing p120, p72, and p56 were observed either in resting or activated cells. In vitro studies showed that the direct association between p120and p56 was mediated by the SH3 domain of p56.




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G. Panchamoorthy, T. Fukazawa, S. Miyake, S. Soltoff, K. Reedquist, B. Druker, S. Shoelson, L. Cantley, and H. Band
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