ACTIVATION-INDUCED UBIQUITINATION OF THE T-CELL ANTIGEN RECEPTOR
ACTIVATION-INDUCED UBIQUITINATION OF THE T-CELL ANTIGEN RECEPTOR
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DOI：
10.1126/science.1323144
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发表时间：
1992-08-07
期刊：
影响因子：
56.9
通讯作者：
WEISSMAN, AM
中科院分区：
文献类型：
--
作者：
CENCIARELLI, C;HOU, D;WEISSMAN, AM
T细胞抗原受体（TCR）的ζ亚基主要以二硫键连接的同源二聚体存在。该受体亚基在TCR介导的信号转导中是重要的，并且是TCR活化的蛋白酪氨酸激酶的底物。发现ζ链响应于受体接合而经历泛素化。这种翻译后修饰发生在正常T细胞和肿瘤细胞系中。非磷酸化和磷酸化的ζ分子都被修饰，并且至少一个其他TCR亚基CD 3-δ在受体活化后也被泛素化。这些发现表明泛素化在跨膜受体功能中的作用扩大。
The zeta-subunit of the T cell antigen receptor (TCR) exists primarily as a disulfide-linked homodimer. This receptor subunit is important in TCR-mediated signal transduction and is a substrate for a TCR-activated protein tyrosine kinase. The zeta-chain was found to undergo ubiquitination in response to receptor engagement. This posttranslational modification occurred in normal T cells and tumor lines. Both nonphosphorylated and phosphorylated zeta-molecules were modified, and at least one other TCR subunit, CD3-delta, was also ubiquitinated after activation of the receptor. These findings suggest an expanded role for ubiquitination in transmembrane receptor function.