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

By N. Holler, Rossana Zaru, O. Micheau, M. Thome, A. Attinger, S. Valitutti, J. Bodmer, P. Schneider, Brian Seed, J. Tschopp. Nature Immunology, 2000

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ZBP1 and TAK1: Master Regulators of NLRP3 Inflammasome/Pyroptosis, Apoptosis, and Necroptosis (PAN-optosis) (2019, background): “Studies focused on the RHIM domain-containing proteins (RIPK1 and RIPK3) and their crosstalk with FADD–caspase-8–mediated pathways improved our understanding of the apoptotic and necroptotic pathways and their intricate regulatory mechanisms (Holler et al., 2000; He et al., 2009; Zhang et al., 2009;”
Cellular Stress Responses: Cell Survival and Cell Death (2010, background): “Studies in RIP1-deficient leukemia cells revealed that RIP1 is required for death receptor-induced necrosis [66, 67].”
Cell Death Signaling. (2015, background): “In many cases, however, apoptosis does not proceed upon TNFR1 ligation, at least in part because the activation of NF-kB induces the expression of the caspase-8-like protein FLICE-like inhibitory protein (FLIP) (Micheau et al. 2001).”
Receptor interacting protein kinase-3 determines cellular necrotic response to TNF-alpha. (2009, background): “One essential protein in TNF-a, TRAIL, and CD95 ligandinduced necrotic cell death is RIPK1 (Holler et al., 2000).”