Fas death receptor (Fas)

The Fas death receptor (CD95, APO-1, TNFRSF6) is a member of the tumor necrosis factor receptor superfamily, recognized as a key apoptosis-inducing receptor that contains a death domain in its intracellular region[3][5][7]. Upon binding its ligand, FasL, the receptor oligomerizes, recruits the adaptor protein FADD, and forms the death-inducing signaling complex (DISC), leading to the activation of caspase-8 and/or caspase-10 and ultimately resulting in cell death by apoptosis[1][3][7]. Fas can also induce alternative non-apoptotic signaling cascades via recruitment of molecules including RIPK1, leading to necroptosis, NF-κB, PI3K/Akt, and MAPK pathway activation, depending on cell type and signaling context[2][4][8]. While an important target in cancer, autoimmune diseases, and immune regulation, direct therapeutic targeting has been problematic due to safety concerns and broad biological effects.

Other names

CD95APO-1TNFRSF6

Activation by Fas ligand (or agonistic antibody) leads to recruitment of FADD, formation of the death-inducing signaling complex (DISC), activation of caspase-8/10, and induction of apoptosis. Non-apoptotic signaling: Activation of PI3K/Akt, MAPK, and NF-κB pathways leads to cell survival, proliferation, or inflammatory responses, depending on cellular context and regulatory co-factors.