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被撕裂致死。

Ripped to death.

机构信息

Department of Immunology, St. Jude Children's Research Hospital, Memphis, TN 38105, USA.

出版信息

Trends Cell Biol. 2011 Nov;21(11):630-7. doi: 10.1016/j.tcb.2011.09.002. Epub 2011 Oct 4.

DOI:10.1016/j.tcb.2011.09.002
PMID:21978761
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC3205316/
Abstract

An old puzzle in the field of cell death was solved recently: the mysterious embryonic lethality of animals deficient in caspase-8 or Fas-associated death domain (FADD), proteins involved in a pathway of apoptosis. This lethality is caused by a failure to develop the yolk sac vasculature rather than a lack of apoptosis. Remarkably, development is rescued by ablation of either of two receptor interacting serine-threonine kinases (RIPKs). Despite being well known cell killers, caspase-8 and FADD act together to block RIPK-mediated necrosis. To manifest this newly elucidated pro-survival function, FADD and caspase-8 depend on FLIP(Long), a catalytically inactive caspase-8 homolog. In this review, the mechanism by which RIPK necrotic death is inhibited by this trio is discussed, as well as how RIPKs might themselves mediate cell death.

摘要

最近，细胞死亡领域的一个古老谜题被解开了：即 caspase-8 或 Fas 相关死亡结构域（FADD）缺乏的动物的神秘胚胎致死性，这些蛋白参与了细胞凋亡途径。这种致死性是由于卵黄囊血管系统发育失败而不是凋亡缺乏引起的。值得注意的是，通过消融两种受体相互作用丝氨酸-苏氨酸激酶（RIPK）中的任何一种，都可以挽救发育。尽管 caspase-8 和 FADD 是众所周知的细胞杀手，但它们共同作用以阻断 RIPK 介导的坏死。为了表现出这种新阐明的促生存功能，FADD 和 caspase-8 依赖于 FLIP(Long)，一种无催化活性的 caspase-8 同源物。在这篇综述中，讨论了该三组分抑制 RIPK 坏死死亡的机制，以及 RIPKs 如何自身介导细胞死亡。

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