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The Journal of Immunology, 1999, 163: 6435-6441.
Copyright © 1999 by The American Association of Immunologists

Regulated Association Between the Tyrosine Kinase Emt/Itk/Tsk and Phospholipase-C{gamma}1 in Human T Lymphocytes1

Juan J. Perez-Villar2 and Steven B. Kanner

Immunology, Inflammation, and Pulmonary Drug Discovery, Bristol-Myers Squibb Pharmaceutical Research Institute, Princeton, NJ 08543

The Emt/Itk/Tsk tyrosine kinase is involved in intracellular signaling events induced by several lymphocyte surface receptors. Modulation of TCR/CD3-induced phospholipase-C{gamma}1 (PLC{gamma}1) activity by the tyrosine kinase Emt/Itk/Tsk has been demonstrated based on studies of Itk-deficient murine T lymphocytes. Here we report a TCR/CD3-regulated association between Emt and PLC{gamma}1 in both normal and leukemic T cells. In addition, this association was enhanced following independent ligation of the CD2, CD4, or CD28 costimulatory molecules, but not of CD5 or CD6 surface receptors, correlating to the induced tyrosine phosphorylation of Emt. Before Ab-induced T cell activation, we found that the Emt-SH3 domain was crucial for the constitutive Emt/PLC{gamma}1 association; however, upon TCR/CD3 engagement, the Emt-SH2 domain was more efficient in mediating the enhanced Emt/PLC{gamma}1 interaction. Furthermore, the PLC{gamma}1-SH3 domain, but not the two PLC{gamma}1-SH2 domains, contributed to formation of the protein complex. Thus, we describe a regulated interaction between Emt and PLC{gamma}1, and based on our studies with individual Emt and PLC{gamma}1 SH2/SH3 domains, we propose a mechanism for this association.




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