title: Caspases and IAPs: a dance of death ensures cell survival.
abstract: In this issue of Molecular Cell, Ditzel et al. (2008) show that DIAP1 polyubiquitinates DRONC, DCP-1, and drICE, leading to their nondegradative inactivation. Surprisingly, activation of DIAP1 requires caspase-mediated cleavage, revealing an elegant feedback mechanism by which caspases regulate their own fate.
authors.affiliation: Department of Pathology, The University of Michigan Medical School, Ann Arbor, MI 48109, USA.
authors.forename: Stefanie
authors.initials: S
authors.lastname: Galbán
authors.forename: Graham F
authors.initials: GF
authors.lastname: Brady
authors.forename: Colin S
authors.initials: CS
authors.lastname: Duckett
mesh_terms: D000818:Animals; D017209:Apoptosis / Q000235:genetics / Q000502:physiology*; D020169:Caspases / Q000235:genetics / Q000378:metabolism*; D002470:Cell Survival; D004330:Drosophila / Q000166:cytology / Q000235:genetics / Q000378:metabolism; D025461:Feedback, Physiological; D051034:Inhibitor of Apoptosis Proteins / Q000235:genetics / Q000378:metabolism*; D008954:Models, Biological; D054875:Ubiquitination
chemical_list: D051034:Inhibitor of Apoptosis Proteins; D020169:Caspases