The Fas receptor （CD95） mediates apoptotic signaling by Fas-ligand expressed on the surface of other cells. The Fas-FasL interaction plays an important role in the immune system and lack of this system leads to autoimmunity， indicating that Fas-mediated apoptosis removes self-reactive lymphocytes. Fas signaling is also involved in immune surveillance to remove transformed cells and virus infected cells. Binding of FAS to oligimerized FasL on another cell activates apoptotic signaling through a cytoplasmic domain termed the death domain that interacts with signaling adaptors including FAF， FADD and DAX to activate the caspase proteolytic cascade. Caspase-8 and caspase-10 are first activated， to then cleave and activate downstream caspases， and a variety of cellular substrates that lead to cell death. Caspases cleave nuclear lamins， causing the nucleus to break down and lose its normal structure and another caspase substrate is DFF， inducing cleavage and degradation of the genome. Other caspase substrates are involved in cytoskeletal structure， cell cycle regulation and signaling pathways. Activation of JNK kinase， activation of Jun， and production of ceramide may also play roles in Fas-mediated apoptosis. Activation of fas-mediated apoptosis is opposed by I-FLICE and FAP. Viruses and tumors may escape immune surveillance in part through suppression of fas-mediated apoptosis using similar mechanisms.
