ZAP-70, a Syk-family protein tyrosine kinase, plays a critical role in mediating T cell signal transduction in response to T cell antigen receptor (TCR) activation (1). Its involvement in pre-TCR and TCR signaling affects the adaptive immune response and thymocyte development (2). TCR-mediated activation of the Src-family kinases, Lck and Fyn, results in tyrosine phosphorylation of the TCR zeta and CD3 chains. These domains serve as targets for binding of ZAP-70 via its tandem SH2 domains. This binding correlates with the recruitment of ZAP-70, a critical event in T cell activation (3). Following TCR engagement, ZAP-70 is phosphorylated by several tyrosine residues in the activation loop of the catalytic domain (2). Phosphorylation of Tyr315 and Tyr319 is required for full activation and increased signal propagation of downstream target molecules by ZAP-70 (4).
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