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pubmed-article:15371430pubmed:abstractTextInhibitor of apoptosis (IAP) proteins are involved in the suppression of apoptosis, signal transduction, cell cycle control and gene regulation. Here we describe the cloning and characterization of viral IAP-associated factor (VIAF), a highly conserved, ubiquitously expressed phosphoprotein with limited homology to members of the phosducin family that associates with baculovirus Op-IAP. VIAF bound Op-IAP both in vitro and in intact cells, with each protein displaying a predominantly cytoplasmic localization. VIAF lacks a consensus IAP binding motif, and overexpression of VIAF failed to prevent Op-IAP from protecting human cells from a variety of apoptotic stimuli, suggesting that VIAF does not function as an IAP antagonist. VIAF was unable to directly inhibit caspase activation in vitro and a reduction of VIAF protein levels by RNA interference led to a decrease in Bax-mediated caspase activation, suggesting that VIAF functions to co-regulate the apoptotic cascade. Finally, VIAF is a substrate for ubiquitination mediated by Op-IAP. Thus, VIAF is a novel IAP-interacting factor that functions in caspase activation during apoptosis.lld:pubmed
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pubmed-article:15371430pubmed:articleTitleVIAF, a conserved inhibitor of apoptosis (IAP)-interacting factor that modulates caspase activation.lld:pubmed
pubmed-article:15371430pubmed:affiliationDepartment of Pathology, University of Michigan, Ann Arbor, Michigan 48109, USA.lld:pubmed
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pubmed-article:15371430pubmed:publicationTypeResearch Support, U.S. Gov't, P.H.S.lld:pubmed
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