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

By Yili Yang, Shengyun Fang, J. P. Jensen, A. Weissman, J. Ashwell. Science, 2000

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Structural basis of caspase-7 inhibition by XIAP. (2001, positive): “A model of caspase-7 in complex with ( Yang et al., 2000 ).”
Proteases for Cell Suicide: Functions and Regulation of Caspases (2000, background): “For example, during thymocyte death, c-IAP-1 and x-IAP are degraded in proteasomes after autoubiquitination, which is catalyzed by the ubiquitin ligase activity of their zinc ring domains (248).”
Tumor necrosis factor signaling (2003, background): “involved in the proteasomal degradation of caspase-3 and – 7,(217) and cIAP1 and cIAP2 themselves.(216) Although TRAF2 mediates recruitment of cAP1 and cIAP2 into the TNF-R2 signalling complex with comparable efficiencies,(210) only cIAP1 seems to ubiquitinate TRAF2.”
NF-κB Signals Induce the Expression of c-FLIP (2001, background): “The ring finger domain of IAPs has been found to have ubiquitin E3 ligase activity, resulting in the transfer of ubiquitin to IAP and thus in its own degradation (29).”