ZAP-70 IS CONSTITUTIVELY ASSOCIATED WITH TYROSINE-PHOSPHORYLATED TCR-ZETA IN MURINE THYMOCYTES AND LYMPH-NODE T-CELLS
ZAP-70 IS CONSTITUTIVELY ASSOCIATED WITH TYROSINE-PHOSPHORYLATED TCR-ZETA IN MURINE THYMOCYTES AND LYMPH-NODE T-CELLS
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DOI：
10.1016/1074-7613(94)90038-8
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发表时间：
1994-11-01
期刊：
影响因子：
32.4
通讯作者：
WEISS, A
中科院分区：
文献类型：
--
作者：
VANOERS, NSC;KILLEEN, N;WEISS, A
对T细胞系和克隆的研究表明，TCR的参与导致TCR亚基的酪氨酸磷酸化。这导致ZAP-70蛋白酪氨酸激酶的募集，涉及ZAP-70的两个SH 2结构域与酪氨酸磷酸化的zeta和CD 3的相互作用。然而，如前所述，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ζ亚基。在这里，我们表明，一部分ZAP-70分子组成型与酪氨酸磷酸化ζ。TCR连接促进ZAP-70以及其他TCR亚基的酪氨酸磷酸化的大幅增加。遗传学研究表明，组成性ZAP-70与酪氨酸磷酸化zeta的关联并不绝对需要TCR或辅助受体与MHC分子的相互作用。
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.