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Comment
. 2008 Nov 21;32(4):462-3.
doi: 10.1016/j.molcel.2008.11.005.

Caspases and IAPs: a dance of death ensures cell survival

Stefanie Galbán  1 , Graham F Brady, Colin S Duckett
Affiliations
Comment

Caspases and IAPs: a dance of death ensures cell survival

Stefanie Galbán et al. Mol Cell. .

Abstract

In this issue of Molecular Cell, Ditzel et al. (2008) show that DIAP1 polyubiquitinates DRONC, DCP-1, and drICE, leading to their nondegradative inactivation. Surprisingly, activation of DIAP1 requires caspase-mediated cleavage, revealing an elegant feedback mechanism by which caspases regulate their own fate.

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Figures

Figure 1
Figure 1. The caspase-DIAP1 autoregulatory loop
Basal proteolytic activity of drICE cleaves DIAP1 to generate processed, fully competent DIAP1, which is then capable of binding to and ubiquitinating both drICE and DRONC. Inactivation of drICE by DIAP1 requires the exposed UBR docking domain at the new amino-terminus but is independent of proteasomal degradation of drICE.
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