Caspase-8 is the most upstream protease of the activation cascade of caspases responsible for the TNFRSF6/FAS mediated and TNFRSF1A induced cell death. Caspase-8 binding to the adapter molecule FADD recruits the complex to either receptor. The resulting aggregate called death-inducing signaling complex (DISC) triggers caspase-8 proteolytic activation. The active dimeric enzyme is then liberated from the DISC and free to activate downstream apoptotic proteases. The enzyme then cleaves and activates caspase-3, caspase-4, caspase-6, caspase-7, caspase-9 and caspase-10. Granzyme B and CPP32 cleave caspase-8 at Asp 315 and Asp 330 respectively to generate the two active subunits.