Abstract
Caspase activity and apoptosis can be inhibited by members of the inhibitor of apoptosis (IAP) family. Selected IAPs are activated by effector caspase cleavage and recruitment of UBR-domain ubiquitin ligases (UBR-E3s). Caspases have been previously shown to undergo ubiquitylation, but the effect of this modification on caspase activity remained unclear. Ditzel et al. now report that caspase activity is regulated by a negative-feedback loop in which effector caspases activate Drosophila IAP1 (DIAP1) and are in turn inhibited by DIAP1-mediated non-degradative ubiquitylation.
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