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. 2000 Dec;1(6):489-95.
doi: 10.1038/82732.

Fas triggers an alternative, caspase-8-independent cell death pathway using the kinase RIP as effector molecule

N Holler  1 , R Zaru, O Micheau, M Thome, A Attinger, S Valitutti, J L Bodmer, P Schneider, B Seed, J Tschopp
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Fas triggers an alternative, caspase-8-independent cell death pathway using the kinase RIP as effector molecule

N Holler et al. Nat Immunol. 2000 Dec.

Abstract

Cell death is achieved by two fundamentally different mechanisms: apoptosis and necrosis. Apoptosis is dependent on caspase activation, whereas the caspase-independent necrotic signaling pathway remains largely uncharacterized. We show here that Fas kills activated primary T cells efficiently in the absence of active caspases, which results in necrotic morphological changes and late mitochondrial damage but no cytochrome c release. This Fas ligand-induced caspase-independent death is absent in T cells that are deficient in either Fas-associated death domain (FADD) or receptor-interacting protein (RIP). RIP is also required for necrotic death induced by tumor necrosis factor (TNF) and TNF-related apoptosis-inducing ligand (TRAIL). In contrast to its role in nuclear factor kappa B activation, RIP requires its own kinase activity for death signaling. Thus, Fas, TRAIL and TNF receptors can initiate cell death by two alternative pathways, one relying on caspase-8 and the other dependent on the kinase RIP VSports手机版. .

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