Controlling the Caspases
- 16 November 2001
- journal article
- perspective
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 294 (5546) , 1477-1478
- https://doi.org/10.1126/science.1062236
Abstract
Enzymes called caspases are the executioners of programmed cell death. The IAP (inhibitor of apoptosis) proteins suppress apoptosis by blocking caspase activity and this suppression can be relieved by Smac/DIABLO, a mitochondrial protein released into the cytosol in response to apoptotic stimuli. In their Perspective, Fesik and Shi discuss recent structural and biochemical studies that reveal the molecular basis for the inhibition of caspases by IAPs and the relief of IAP inhibition by Smac/DIABLO.Keywords
This publication has 23 references indexed in Scilit:
- Structural Analysis of a Functional DIAP1 Fragment Bound to Grim and Hid PeptidesMolecular Cell, 2001
- Structural Basis for the Inhibition of Caspase-3 by XIAPCell, 2001
- Structural Basis of Caspase-7 Inhibition by XIAPCell, 2001
- Molecular Determinants of the Caspase-promoting Activity of Smac/DIABLO and Its Role in the Death Receptor PathwayJournal of Biological Chemistry, 2000
- NMR Structure and Mutagenesis of the Third Bir Domain of the Inhibitor of Apoptosis Protein XIAPJournal of Biological Chemistry, 2000
- Identification of DIABLO, a Mammalian Protein that Promotes Apoptosis by Binding to and Antagonizing IAP ProteinsCell, 2000
- Smac, a Mitochondrial Protein that Promotes Cytochrome c–Dependent Caspase Activation by Eliminating IAP InhibitionCell, 2000
- Biochemical Pathways of Caspase Activation During ApoptosisAnnual Review of Cell and Developmental Biology, 1999
- A Single BIR Domain of XIAP Sufficient for Inhibiting CaspasesJournal of Biological Chemistry, 1998
- Apoptosis in the Pathogenesis and Treatment of DiseaseScience, 1995