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Fas (also called Apo1 or CD95) is a death domain-containing member of the TNFR (Tumor Necrosis Factor Receptor) superfamily. It has a central role in the physiological regulation of programmed cell death and has been implicated in the pathogenesis of various malignancies and diseases of the immune system. Although the FasL (Fas Ligand)-Fas system has been appreciated mainly with respect to its death-inducing function, it also transduces proliferative and activating signals through pathways that are still poorly defined. The Fas receptor induces an apoptotic signal by binding to FasL expressed on the surface of other cells. Fas is a Type-I transmembrane protein, where as FasL a Type-II transmembrane protein of TNF family and can be shed in a soluble form by action of metalloproteinase (Ref. The Fas receptor upon binding to the FasL trimerizes and induces apoptosis through a cytoplasmic domain called DD (Death Domain) that interacts with signaling adaptors like FAF-1 (Fas-Associated Factor-1), FADD (Fas-Associated Death Domain), Daxx, FAP-1, FLASH (FLICE-associated huge) and RIP (Receptor-Interacting Protein).
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