RIP - A NOVEL PROTEIN CONTAINING A DEATH DOMAIN THAT INTERACTS WITH FAS/APO-1 (CD95) IN YEAST AND CAUSES CELL-DEATH
RIP - A NOVEL PROTEIN CONTAINING A DEATH DOMAIN THAT INTERACTS WITH FAS/APO-1 (CD95) IN YEAST AND CAUSES CELL-DEATH
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DOI：
10.1016/0092-8674(95)90072-1
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发表时间：
1995-05-19
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：
STANGER, BZ;LEDER, P;SEED, B
细胞表面受体Fas/APO-1(CD95)胞外区的连接在易感细胞中引起特征性的程序性死亡反应。利用酵母中基于蛋白质-蛋白质相互作用的遗传选择，我们已经鉴定出两种与PAS胞内结构域相关的基因产物：PAS本身和一种新的74 kDa蛋白，我们将其命名为RIP，即受体相互作用蛋白。RIP还与p55肿瘤坏死因子受体(TNFR1)胞内结构域弱相互作用，但不与对应于小鼠LPR(CG)突变的PAS突变版本相互作用。RIP包含一个与蛋白激酶同源的N-末端区域和一个包含存在于PAS和TNFR1胞内域的细胞质基序(死亡结构域)的C-末端区域。瞬时过表达RIP可导致转基因细胞发生以细胞凋亡为特征的形态变化。综上所述，这些特性表明RIP是一种新的凋亡诱导蛋白。
Ligation of the extracellular domain of the cell surface receptor Fas/APO-1 (CD95) elicits a characteristic programmed death response in susceptible cells. Using a genetic selection based on protein-protein interaction in yeast, we have identified two gene products that associate with the intracellular domain of Pas: Pas itself, and a novel 74 kDa protein we have named RIP, for receptor interacting protein. RIP also interacts weakly with the p55 tumor necrosis factor receptor (TNFR1) intracellular domain, but not with a mutant version of Pas corresponding to the murine lpr(cg) mutation. RIP contains an N-terminal region with homology to protein kinases and a C-terminal region containing a cytoplasmic motif (death domain) present in the Pas and TNFR1 intracellular domains. Transient overexpression of RIP causes transfected cells to undergo the morphological changes characteristic of apoptosis. Taken together, these properties indicate that RIP is a novel form of apoptosis-inducing protein.