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  • Title: Ubiquitin protein ligase activity of IAPs and their degradation in proteasomes in response to apoptotic stimuli.
    Author: Yang Y, Fang S, Jensen JP, Weissman AM, Ashwell JD.
    Journal: Science; 2000 May 05; 288(5467):874-7. PubMed ID: 10797013.
    Abstract:
    To determine why proteasome inhibitors prevent thymocyte death, we examined whether proteasomes degrade anti-apoptotic molecules in cells induced to undergo apoptosis. The c-IAP1 and XIAP inhibitors of apoptosis were selectively lost in glucocorticoid- or etoposide-treated thymocytes in a proteasome-dependent manner before death. IAPs catalyzed their own ubiquitination in vitro, an activity requiring the RING domain. Overexpressed wild-type c-IAP1, but not a RING domain mutant, was spontaneously ubiquitinated and degraded, and stably expressed XIAP lacking the RING domain was relatively resistant to apoptosis-induced degradation and, correspondingly, more effective at preventing apoptosis than wild-type XIAP. Autoubiquitination and degradation of IAPs may be a key event in the apoptotic program.
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