Fas-associated death domain (FADD, also known as MORT1) is an important apoptosis adapter molecule involved in the Fas-mediated cell death pathway. FADD associates with the intracellular domain of FAS (CD95/APO-1) through their respective C-terminal death domains (DD). The N-terminal region of FADD contains a death effectors domain (DED) which recruits and binds cytosolic proteins such as FLICE/caspase-8. The subsequent activation of FLICE by proteolytic cleavage leads to the activation of the caspase-mediated (ICE-related proteases) apoptotic cascade. Overexpression of FADD induces apoptosis which is inhibited by CrmA, a specific inhibitor of the interleukin-1beta-converting enzyme. FADD has also been shown under certain circumstances to promote cell survival and proliferation.1-6