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首页> 外文期刊>Molecular biology of the cell >Integrin-mediated tyrosine phosphorylation of Shc in T cells is regulated by protein kinase C-dependent phosphorylations of Lck
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Integrin-mediated tyrosine phosphorylation of Shc in T cells is regulated by protein kinase C-dependent phosphorylations of Lck

机译：T细胞中Shc的整合素介导的酪氨酸磷酸化受蛋白激酶C依赖性Lck磷酸化的调节

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Integrin receptor signals are costimulatory for mitogenesis with the T-cell receptor during T-cell activation. A subset of integrin receptors can link to the adapter protein Shc and provide a mitogenic stimulus. Using a combination of genetic and pharmacological approaches, we show herein that integrin signaling to Shc in T cells requires the receptor tyrosine phosphatase CD45, the Src family kinase member Lck, and protein kinase C. Our results suggest a model in which integrin-dependent serine phosphorylation of Lck is the critical step that determines the efficiency of Shc tyrosine phosphorylation in T cells. Serine phosphorylation of Lck is dependent on PKC and is also linked to CD45 dephosphorylation. Mutants of Lck that cannot be phosphorylated on the critical serine residues do not signal efficiently to Shc and have greatly reduced kinase activity. This signaling from integrins to Lck may be an important step in the costimulation with the T-cell receptor during lymphocyte activation. [References: 53]
机译：整联蛋白受体信号在T细胞活化过程中与T细胞受体共同促有丝分裂。整联蛋白受体的一个子集可以链接到衔接蛋白Shc并提供促有丝分裂的刺激。使用遗传学和药理学方法的结合，我们在这里表明，T细胞中Shc的整合素信号传导需要受体酪氨酸磷酸酶CD45，Src家族激酶成员Lck和蛋白激酶C。 Lck的磷酸化是决定T细胞中Shc酪氨酸磷酸化效率的关键步骤。 Lck的丝氨酸磷酸化依赖于PKC，也与CD45的去磷酸化有关。无法在关键丝氨酸残基上磷酸化的Lck突变体无法有效地向Shc发出信号，并且激酶活性大大降低。从整联蛋白到Lck的信号传导可能是淋巴细胞活化过程中与T细胞受体共刺激的重要步骤。 [参考：53]

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