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Ubiquitin protein ligase activity of IAPs and their degradation in proteasomes in response to apoptotic stimuli | | Y Yang
; S Fang
; J P Jensen
; A M Weissman
; J D Ashwell
; | | Date: |
5 May 2000 | | Journal: | Science, 288 (5467), 874-7 | | 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. | | Source: | PubMed, pmid10797013 doi: 8502 | | Services: | Forum | Review | Favorites | |
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