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Holler, N, Zaru, R, Micheau, O, Thome, M, Attinger, A, Valitutti, S, Bodmer, JL, Schneider, P, Seed, B and Tschopp, J (2000) Fas triggers an alternative, caspase-8-independent cell death pathway using the kinase RIP as effector molecule. Nat. Immunol. 1:489-95


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.


PubMed Online version:10.1038/82732


Adaptor Proteins, Signal Transducing; Animals; Antigens, CD95/metabolism; Apoptosis/physiology; Apoptosis Regulatory Proteins; Carrier Proteins/metabolism; Caspase 8; Caspase 9; Caspases/metabolism; Cell Death/physiology; Fas Ligand Protein; Fas-Associated Death Domain Protein; Humans; Jurkat Cells; Membrane Glycoproteins/metabolism; Mice; Mice, Inbred BALB C; Models, Biological; Necrosis; Proteins/metabolism; Receptor-Interacting Protein Serine-Threonine Kinases; Signal Transduction; T-Lymphocytes/cytology; T-Lymphocytes/metabolism; TNF-Related Apoptosis-Inducing Ligand; Tumor Necrosis Factor-alpha/metabolism