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Volume 270, Number 20, Issue of May 19, pp. 11806-11811, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
Association of p72 with the src Homology-2 (SH2) Domains of PLC1 in B Lymphocytes

Amy L. Sillman , John G. Monroe

Phospholipase C-catalyzed inositol phospholipid hydrolysis, a critical step in B cell antigen receptor signaling leading to second messenger generation and proliferation, depends upon tyrosine kinase activation. The B cell antigen receptor-associated tyrosine kinases p53/56, p59, p55, and p72 are assumed to participate in receptor-initiated signaling. It is unknown, however, which of these kinases is involved in the tyrosine phosphorylation and resulting activation of phospholipase C in response to antigen receptor cross-linking. We have used a fusion protein containing the tandem src homology-2 (SH2) domains of phospholipase C1 (PLC1) to identify B cell kinases which associate with PLC1. Using an in vitro kinase assay, we demonstrate SH2-dependent association of tyrosine kinase activity from anti-µ-stimulated B cells. The PLC1 SH2 domains associate with a prominent 70-72-kDa tyrosine phosphoprotein from anti-µ-stimulated, but not resting, B cells. Immunoblotting and secondary immunoprecipitation studies definitively identify this protein as p72. These results imply a physical interaction between PLC1 and p72 in antigen receptor-stimulated B cells. This conclusion is confirmed by our ability to co-immunoprecipitate p72 and PLC1 from lysates of anti-µ-stimulated B cells. These results implicate p72 in the activation of phospholipase C1 during B cell antigen receptor signaling.



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