白细胞介素2受体的跨膜信号传导。人白细胞介素2受体（p55）/胰岛素受体嵌合分子的构象与功能。
Transmembrane signaling of interleukin 2 receptor. Conformation and function of human interleukin 2 receptor (p55)/insulin receptor chimeric molecules.
作者信息
Hatakeyama M, Doi T, Kono T, Maruyama M, Minamoto S, Mori H, Kobayashi M, Uchiyama T, Taniguchi T
出版信息
J Exp Med. 1987 Aug 1;166(2):362-75. doi: 10.1084/jem.166.2.362.
Abstract
Chimeric genes were constructed which gave rise to the expression of novel receptor molecules consisting of the extracellular domain of the human interleukin 2 receptor (IL-2-R; p55 or Tac antigen) joined to the transmembrane domain and either full-length or truncated cytoplasmic domain of the human insulin receptor (Ins-R). Expression studies using mouse T cell line EL-4 revealed that the chimeric receptors are able to manifest properties indistinguishable from the authentic IL-2-R. On the other hand, stimulation of the tyrosine kinase activity by IL-2 was not observed in the chimeric receptor with the entire cytoplasmic domain of the Ins-R. These findings thus shed light on the structural conformation and functioning of the IL-2-R complex.
摘要
构建了嵌合基因，其导致由人白细胞介素2受体（IL-2-R；p55或Tac抗原）的细胞外结构域与跨膜结构域以及人胰岛素受体（Ins-R）的全长或截短细胞质结构域连接而成的新型受体分子的表达。使用小鼠T细胞系EL-4进行的表达研究表明，嵌合受体能够表现出与天然IL-2-R无法区分的特性。另一方面，在具有Ins-R整个细胞质结构域的嵌合受体中未观察到IL-2对酪氨酸激酶活性的刺激。因此，这些发现揭示了IL-2-R复合物的结构构象和功能。
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