van Oers N S, Killeen N, Weiss A
Department of Medicine, Howard Hughes Medical Institute, University of California, San Francisco 94143, USA.
Immunity. 1994 Nov;1(8):675-85. doi: 10.1016/1074-7613(94)90038-8.
Studies with T cell lines and clones have shown that engagement of the TCR results in the tyrosine phosphorylation of the TCR subunits. This leads to the recruitment of the ZAP-70 protein tyrosine kinase, an interaction involving the two SH2-domains of ZAP-70 with tyrosine-phosphorylated zeta and CD3. However, as previously described, murine thymocytes and lymph node T cells express a constitutively tyrosine-phosphorylated zeta subunit in the basal state. Here, we show that a fraction of ZAP-70 molecules are constitutively associated with tyrosine-phosphorylated zeta. TCR ligation promotes a large increase in the tyrosine phosphorylation of ZAP-70 as well as other TCR subunits. Genetic studies reveal that the constitutive ZAP-70 association with tyrosine-phosphorylated zeta does not absolutely require either TCR or coreceptor interactions with MHC molecules.
对T细胞系和克隆的研究表明，TCR的结合会导致TCR亚基的酪氨酸磷酸化。这会导致ZAP-70蛋白酪氨酸激酶的募集，这种相互作用涉及ZAP-70的两个SH2结构域与酪氨酸磷酸化的ζ链和CD3。然而，如前所述，小鼠胸腺细胞和淋巴结T细胞在基础状态下表达组成型酪氨酸磷酸化的ζ亚基。在这里，我们表明一部分ZAP-70分子与酪氨酸磷酸化的ζ链组成型相关。TCR连接促进ZAP-70以及其他TCR亚基的酪氨酸磷酸化大幅增加。遗传学研究表明，ZAP-70与酪氨酸磷酸化的ζ链的组成型结合并不绝对需要TCR或共受体与MHC分子的相互作用。
