c-IAP2 is a member of the IAP family of proteins that inhibit apoptosis by binding to tumor necrosis factor receptor-associated factors TRAF1 and TRAF2, probably by interfering with activation of ICE-like proteases. These proteins contain a BIR (baculovirus IAP repeat) domain near the amino-terminus. The BIR domain can bind some caspases. Many members of the IAP family of proteins block proteolytic activation of caspase-3 and caspase-7. For example, XIAP, c-IAP1 and c-IAP2 appear to block cytochrome c-induced activation of caspase-9, thereby preventing initiation of the caspase cascade. Since c-IAP1 and c-IAP2 were first identified as components in the cytosolic death domain-induced complex associated with the TNF family of receptors, they may inhibit apoptosis by additional mechanisms.
