Hatakeyama M, Kono T, Kobayashi N, Kawahara A, Levin S D, Perlmutter R M, Taniguchi T
Institute for Molecular and Cellular Biology, Osaka University, Japan.
Science. 1991 Jun 14;252(5012):1523-8. doi: 10.1126/science.2047859.
In the interleukin-2 (IL-2) system, intracellular signal transduction is triggered by the beta chain of the IL-2 receptor (IL-2R beta); however, the responsible signaling mechanism remains unidentified. Evidence for the formation of a stable complex of IL-2R beta and the lymphocyte-specific protein tyrosine kinase p56lck is presented. Specific association sites were identified in the tyrosine kinase catalytic domain of p56lck and in the cytoplasmic domain of IL-2R beta. As a result of interaction, IL-2R beta became phosphorylated in vitro by p56lck. Treatment of T lymphocytes with IL-2 promotes p56lck kinase activity. These data suggest the participation of p56lck as a critical signaling molecule downstream of IL-2R via a novel interaction.
在白细胞介素-2（IL-2）系统中，细胞内信号转导由IL-2受体（IL-2Rβ）的β链触发；然而，其负责的信号传导机制仍未明确。本文提供了IL-2Rβ与淋巴细胞特异性蛋白酪氨酸激酶p56lck形成稳定复合物的证据。在p56lck的酪氨酸激酶催化结构域和IL-2Rβ的胞质结构域中鉴定出了特异性结合位点。相互作用的结果是，IL-2Rβ在体外被p56lck磷酸化。用IL-2处理T淋巴细胞可促进p56lck激酶活性。这些数据表明，p56lck通过一种新的相互作用作为IL-2R下游的关键信号分子参与其中。
