Caspase-8 (CASP8) is a ~55 kDa protein. Thiol protease that plays a key role in programmed cell death by acting as a molecular switch for apoptosis, necroptosis and pyroptosis, and is required to prevent tissue damage during embryonic development and adulthood. Initiator protease that induces extrinsic apoptosis by mediating cleavage and activation of effector caspases responsible for FAS/CD95-mediated and TNFRSF1A-induced cell death. Cleaves and activates effector caspases CASP3, CASP4, CASP6, CASP7, CASP9 and CASP10. Binding to the adapter molecule FADD recruits it to either receptor FAS/CD95 or TNFRSF1A. The resulting aggregate called the death-inducing signaling complex (DISC) performs CASP8 proteolytic activation. 1. Benchoua, A. et al. (2002) The Journal of biological chemistry 277, 34217-22. PMID: 120655913. Orning, P. et al. (2018) Science (New York, N.Y.) 362, 1064-1069. PMID: 303613834. Sarhan, J. et al. (2018) Proceedings of the National Academy of Sciences of the United States of America 115, E10888-E10897. PMID: 303814587. Muendlein, HI. et al. (2021) Nature communications 12, 86. PMID: 33397971 | 
