Ubiquitin protein ligase activity of IAPs and their degradation in proteasomes in response to apoptotic stimuli.

@article{Yang2000UbiquitinPL,
  title={Ubiquitin protein ligase activity of IAPs and their degradation in proteasomes in response to apoptotic stimuli.},
  author={Yili Yang and Shengyun Fang and Jane P. Jensen and Allan M. Weissman and Jonathan D Ashwell},
  journal={Science},
  year={2000},
  volume={288 5467},
  pages={874-7}
}
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… CONTINUE READING
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