Abstract
One way or another, almost all proteins containing baculoviralIAP repeat domains (BIRs) have been associated withubiquitin (the only exception being NAIP). The RING-bearingIAPs, XIAP, ML-IAP, cIAP1, cIAP2, DIAP1, and DIAP2 act asubiquitin E3 ligases. The giant BIR containing protein BRUCEbears a ubiquitin conjugation (UBC) E2 domain, and Survivinis degraded by ubiquitin-targeted proteolysis at the end ofmitosis. Current studies of BIR containing proteins illustratethe fundamental importance of the ubiquitin system in theregulationofproteinfunctionandabundanceduringcelldeathand cell division.The finding that the zinc-binding RING domain of proteinssuch as c-cbl allows them to function as ubiquitin ligases
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