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The Amino-Terminal Src Homology 2 Domain of Phospholipase C1 Is Essential for TCR-Induced Tyrosine Phosphorylation of Phospholipase C1

Laboratory of Immunobiology, Division of Monoclonal Antibodies, OTRR, Center for Biologics Evaluation and Research, Bethesda, MD 20892

TCR engagement activates phospholipase C1 (PLC1) via a tyrosine phosphorylation-dependent mechanism. PLC1 contains a pair of Src homology 2 (SH2) domains whose function is that of promoting protein interactions by binding phosphorylated tyrosine and adjacent amino acids. The role of the PLC1 SH2 domains in PLC1 phosphorylation was explored by mutational analysis of an epitope-tagged protein transiently expressed in Jurkat T cells. Mutation of the amino-terminal SH2 domain (SH2(N) domain) resulted in defective tyrosine phosphorylation of PLC1 in response to TCR/CD3 perturbation. In addition, the PLC1 SH2(N) domain mutant failed to associate with Grb2 and a 36- to 38-kDa phosphoprotein (p36–38), which has previously been recognized to interact with PLC1, Grb2, and other molecules involved in TCR signal transduction. Conversely, mutation of the carboxyl-terminal SH2 domain (SH2(C) domain) did not affect TCR-induced tyrosine phosphorylation of PLC1. Furthermore, binding of p36–38 to PLC1 was not abrogated by mutations of the SH2(C) domain. In contrast to TCR/CD3 ligation, treatment of cells with pervanadate induced tyrosine phosphorylation of either PLC1 SH2(N) or SH2(C) domain mutants to a level comparable with that of the wild-type protein, indicating that pervanadate treatment induces an alternate mechanism of PLC1 phosphorylation. These data indicate that the SH2(N) domain is required for TCR-induced PLC1 phosphorylation, presumably by participating in the formation of a complex that promotes the association of PLC1 with a tyrosine kinase.

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