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首页> 外文期刊>Molecular and Cellular Biology >The kinase, SH3, and SH2 domains of Lck play critical roles in T-cell activation after ZAP-70 membrane localization.
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The kinase, SH3, and SH2 domains of Lck play critical roles in T-cell activation after ZAP-70 membrane localization.

机译：ZAP-70膜定位后，Lck的激酶，SH3和SH2域在T细胞活化中起关键作用。

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摘要

Antigenic stimulation of the T-cell antigen receptor initiates signal transduction through the immunoreceptor tyrosine-based activation motifs (ITAMs). When its two tyrosines are phosphorylated, ITAM forms a binding site for ZAP-70, one of the cytoplasmic protein tyrosine kinases essential for T-cell activation. The signaling process that follows ZAP-70 binding to ITAM has been analyzed by the construction of fusion proteins that localize ZAP-70 to the plasma membrane. We found that membrane-localized forms of ZAP-70 induce late signaling events such as activation of nuclear factor of activated T cells without any stimulation. This activity was observed only when Lck was expressed and functional. In addition, each mutation that affects the function of Lck in the kinase, Src homology 2 (SH2), and SH3 domains greatly impaired the signaling ability of the chimeric protein. Therefore, Lck functions in multiple manners in T-cell activation for the steps following ZAP-70 binding to ITAM.
机译：T细胞抗原受体的抗原刺激通过基于免疫受体酪氨酸的激活基序（ITAM）启动信号转导。当其两个酪氨酸被磷酸化时，ITAM形成ZAP-70的结合位点，ZAP-70是T细胞活化所必需的一种细胞质蛋白酪氨酸激酶。 ZAP-70与ITAM结合后的信号传导过程已通过构建将ZAP-70定位于质膜的融合蛋白进行了分析。我们发现ZAP-70的膜定位形式可诱导晚期信号传导事件，例如活化T细胞的核因子活化而无任何刺激。仅当表达Lck并起作用时才观察到该活性。此外，每个影响Lck在激酶，Src同源性2（SH2）和SH3域中的功能的突变都大大削弱了嵌合蛋白的信号传导能力。因此，对于ZAP-70与ITAM结合后的步骤，Lck在T细胞激活中以多种方式起作用。

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