Weber J R, Bell G M, Han M Y, Pawson T, Imboden J B
Department of Medicine, University of California, San Francisco.
J Exp Med. 1992 Aug 1;176(2):373-9. doi: 10.1084/jem.176.2.373.
Stimulation of the T cell antigen receptor (TCR) activates a protein tyrosine kinase and leads to the tyrosine phosphorylation of phosphoinositide-specific phospholipase C-gamma 1 (PLC gamma 1). The molecular interactions involved in this phosphorylation are not known. After stimulation of the TCR on Jurkat T cells, tyrosine-phosphorylated proteins of 36, 38, 58, and 63 kD coprecipitate with PLC gamma 1. An identical pattern of proteins precipitate with TrpE fusion proteins that contain the Src homology (SH) 2 domains of PLC gamma 1, indicating that these regions of PLC gamma 1 are responsible for binding. TCR stimulation leads to an association between the SH2 domains of PLC gamma 1 and a protein tyrosine kinase, which, by peptide mapping, is identical to p56lck. These studies establish that p56lck associates with PLC gamma 1 as a result of TCR stimulation of Jurkat cells, suggesting that p56lck plays a central role in coupling the TCR to the activation of PLC gamma 1.
T细胞抗原受体（TCR）的刺激会激活一种蛋白酪氨酸激酶，并导致磷酸肌醇特异性磷脂酶C-γ1（PLCγ1）的酪氨酸磷酸化。参与这种磷酸化的分子相互作用尚不清楚。在刺激Jurkat T细胞上的TCR后，36、38、58和63 kD的酪氨酸磷酸化蛋白与PLCγ1共沉淀。含有PLCγ1的Src同源（SH）2结构域的TrpE融合蛋白沉淀出相同模式的蛋白，表明PLCγ1的这些区域负责结合。TCR刺激导致PLCγ1的SH2结构域与一种蛋白酪氨酸激酶之间发生关联，通过肽图谱分析，该激酶与p56lck相同。这些研究表明，由于Jurkat细胞的TCR刺激，p56lck与PLCγ1结合，提示p56lck在将TCR与PLCγ1的激活偶联中起核心作用。
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