Park Sun-Mi, Schickel Robert, Peter Marcus E
The Ben May Institute for Cancer Research, University of Chicago, 924 E. 57th Street., Chicago, Illinois 60637, USA.
Curr Opin Cell Biol. 2005 Dec;17(6):610-6. doi: 10.1016/j.ceb.2005.09.010. Epub 2005 Oct 13.
Death receptors (DRs) are surface receptors that when triggered have the capacity to induce apoptosis in cells by forming the death-inducing signaling complex (DISC). The first protein recruited to form the DISC is the adaptor protein FADD/Mort1. Some members of the DR family, CD95 and the TRAIL receptors DR4 and DR5, directly bind FADD, whereas others, such as TNF receptor I and DR3, initially bind another adaptor protein, TRADD, which then recruits FADD. While all DRs can activate both apoptotic and non-apoptotic pathways, it has been widely assumed that the main physiological role of FADD-binding death receptors is to trigger apoptosis. However, recent work has ascribed multiple non-apoptotic activities to these receptors and/or the signaling components of the DISC.
死亡受体（DRs）是一类表面受体，当其被触发时，能够通过形成死亡诱导信号复合物（DISC）诱导细胞凋亡。招募形成DISC的首个蛋白质是衔接蛋白FADD/Mort1。DR家族的一些成员，如CD95以及肿瘤坏死因子相关凋亡诱导配体（TRAIL）受体DR4和DR5，可直接结合FADD，而其他成员，如肿瘤坏死因子受体I（TNF receptor I）和DR3，则首先结合另一种衔接蛋白TRADD，然后由TRADD招募FADD。虽然所有的死亡受体都能激活凋亡和非凋亡途径，但人们普遍认为，与FADD结合的死亡受体的主要生理作用是触发细胞凋亡。然而，最近的研究表明，这些受体和/或DISC的信号成分具有多种非凋亡活性。
