Abstract
Abstract To explore the mechanism(s) by which phospholipase C (PLC)-γ2 participates in B cell Ag receptor (BCR) signaling, we have studied the function of PLC-γ2 mutants in B cells deficient in PLC-γ2. Mutation of the N-terminal Src homology 2 domain [SH2(N)] resulted in the complete loss of inositol 1,4,5-trisphosphate generation upon BCR engagement. A possible explanation for the SH2(N) requirement was provided by findings that this mutation abrogates the association of PLC-γ2 with an adaptor protein BLNK. Moreover, expression of a membrane-associated form (CD16/PLC-γ2) with SH2(N) mutation required coligation of BCR and CD16 for inositol 1,4,5-trisphosphate generation. Together, our results suggest a central role for the SH2(N) domain in directing PLC-γ2 into the close proximity of BCR signaling complex by its association with BLNK, whereby PLC-γ2 becomes tyrosine phosphorylated and thereby activated.
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