NEGATIVE REGULATION OF T-CELL RECEPTOR SIGNALING BY TYROSINE PROTEIN-KINASE P50(CSK)
NEGATIVE REGULATION OF T-CELL RECEPTOR SIGNALING BY TYROSINE PROTEIN-KINASE P50(CSK)
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DOI：
10.1038/365156a0
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发表时间：
1993-09-09
期刊：
影响因子：
64.8
通讯作者：
VEILLETTE, A
中科院分区：
文献类型：
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作者：
CHOW, LML;FOURNEL, M;VEILLETTE, A
酪氨酸蛋白磷酸化是抗原受体介导的T淋巴细胞活化所必需的1。该信号至少部分由Src相关酪氨酸蛋白激酶p56 lck和p59 fynT产生（参考文献2，3）。这两种酶的活性被保守的羧基末端酪氨酸残基的磷酸化抑制2，3。最近的研究表明，这种抑制性磷酸化可能是由p50 csk（C-末端Src激酶）引起的，p50 csk是一种酪氨酸蛋白激酶，在胸腺和脾脏中积累最丰富4 -8。为了研究Csk在T淋巴细胞中的功能并表征调节T细胞受体（TCR）信号传导的过程，我们研究了Csk过表达对抗原特异性小鼠T细胞系的生理学的影响。我们在这里报告，p50 csk负调控TCR诱导的酪氨酸蛋白磷酸化和淋巴因子的生产。这为Csk参与调节T细胞活化提供了证据。
TYROSINE protein phosphorylation is necessary for antigen receptor-mediated activation of T lymphocytes1. This signal is generated at least in part by the Src-related tyrosine protein kinases p56lck and p59fynT (refs 2, 3). The activity of these two enzymes is repressed by phosphorylation of a conserved carboxy-terminal tyrosine residue2,3. Recent studies suggest that this inhibitory phosphorylation may be caused by p50csk (for C-terminal Src kinase), a tyrosine protein kinase which accumulates most abundantly in thymus and spleen4-8. To investigate the function of Csk in T lymphocytes and characterize the processes regulating T-cell receptor (TCR) signalling, we examined the effects of overexpression of Csk on the physiology of an antigen-specific mouse T-cell line. We report here that p50csk negatively regulates TCR-induced tyrosine protein phosphorylation and lymphokine production. This provides evidence for the involvement of Csk in the regulation of T-cell activation.