Caspase activation, inhibition, and reactivation: A mechanistic view

Caspases, a unique family of cysteine proteases, execute programmed cell death (apoptosis). Caspases exist as inactive zymogens in cells and undergo a cascade of catalytic activation at the onset of apoptosis. The activated caspases are subject to inhibition by the inhibitor‐of‐apoptosis (IAP) famil...

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Bibliographic Details
Published inProtein science Vol. 13; no. 8; pp. 1979 - 1987
Main Author Shi, Yigong
Format Journal Article
LanguageEnglish
Published Bristol Cold Spring Harbor Laboratory Press 01.08.2004
Subjects
activation and inhibition
Amino Acid Motifs
Animals
apoptosis
Apoptosis - physiology
caspase
Caspases - chemistry
Caspases - metabolism
Drosophila - metabolism
Enzyme Activation - physiology
Enzyme Reactivators - metabolism
Humans
IAP
Inhibitor of Apoptosis Proteins
Mammals - metabolism
Protein Structure, Tertiary
Proteins - chemistry
Proteins - metabolism
Review
Smac/DIABLO
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Summary:Caspases, a unique family of cysteine proteases, execute programmed cell death (apoptosis). Caspases exist as inactive zymogens in cells and undergo a cascade of catalytic activation at the onset of apoptosis. The activated caspases are subject to inhibition by the inhibitor‐of‐apoptosis (IAP) family of proteins. This inhibition can be effectively removed by diverse proteins that share an IAP‐binding tetrapeptide motif. Recent structural and biochemical studies have revealed the underlying molecular mechanisms for these processes in mammals and in Drosophila. This paper reviews these latest advances.
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Article and publication are at http://www.proteinscience.org/cgi/doi/10.1110/ps.04789804.
Reprint requests to: Yigong Shi, Department of Molecular Biology, Lewis Thomas Laboratory, Princeton University, Princeton, NJ 08544, USA; e-mail: yshi@molbio.princeton.edu; fax: (609) 258-6730.
ISSN:0961-8368
1469-896X
DOI:10.1110/ps.04789804