alpha L beta 2 integrin/LFA-1 binding to ICAM-1 induced by cytohesin-1, a cytoplasmic regulatory molecule
alpha L beta 2 integrin/LFA-1 binding to ICAM-1 induced by cytohesin-1, a cytoplasmic regulatory molecule
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DOI：
10.1016/s0092-8674(00)80095-1
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发表时间：
1996-07-26
期刊：
影响因子：
64.5
通讯作者：
Seed, B
中科院分区：
文献类型：
--
作者：
Kolanus, W;Nagel, W;Seed, B
整合素粘附受体对细胞外配体的亲合力受到细胞内程序的动态调节，但这些程序尚未阐明。我们在这里描述一种蛋白质，cytohesin-1，它特异性地与整合素β 2链（CD 18）的细胞内部分相互作用。该分子显示与酵母SEC 7基因产物的同源性，并带有普列克底物蛋白同源（PH）结构域。过表达全长细胞粘连素-1或SEC 7结构域诱导Jurkat细胞与ICAM-1的β 2整合素依赖性结合，而表达分离的细胞粘连素-1 PH结构域抑制T细胞受体刺激的粘附。从其他蛋白质中提取的PH结构域没有表现出类似的抑制作用，这表明相互作用是特异性的，并且单个PH结构域能够区分替代靶标。
The avidity of integrin adhesion receptors for extracellular ligands is subject to dynamic regulation by intracellular programs that have yet to be elucidated. We describe here a protein, cytohesin-1, which specifically interacts with the intracellular portion of the integrin beta 2 chain (CD18). The molecule shows homology to the yeast SEC7 gene product and bears a pleckstrin homology (PH) domain. Overexpression of either the full-length cytohesin-1 or the SEC7 domain induces beta 2 integrin-dependent binding of Jurkat cells to ICAM-1, whereas expression of the isolated cytohesin-1 PH domain inhibits T cell receptor-stimulated adhesion. Similar inhibition is not exhibited by PH domains taken from other proteins, showing that the interaction is specific and that individual PH domains are capable of discriminating between alternative targets.