The 70-kDa ζ chain-associated protein (ZAP70) is a protein tyrosine kinase (PTK) that associates with the ζ subunit of the T cell antigen receptor (TCR) and undergoes tyrosine phosphorylation following TCR stimulation. ZAP70 contains two SH2-like domains with the PTK domain located at the C-terminus. It appears that both ZAP70 and Syk are recruited to the phosphorylated CD3 and ζ subunits after TCR stimulation. TCR-mediated Lck activity leads to phosphorylation of ZAP70 on Tyrosine 493 (Y493) in the regulatory loop of the kinase domain leading to upregulation of ZAP70 kinase activity. The significance of ZAP70 activation in mediating TCR signal transduction has been confirmed by showing that ZAP70 activity is absent in an autosomal recessive form of severe combined immunodeficiency (SCID). This is due to mutations affecting the ZAP70 kinase domain which affect the stability of the protein and TCR signaling.
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