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Int J Mol Sci. 2012;13(4):4807-18. doi: 10.3390/ijms13044807. Epub 2012 Apr 16.

Structural features of caspase-activating complexes.

Author information

1
Department of Biochemistry, School of Biotechnology at Yeungnam University, Gyeongsan 712-749, Korea; E-Mail: hyunho@ynu.ac.kr ; Tel.: +82-53-810-3045;

Abstract

Apoptosis, also called programmed cell death, is an orderly cellular suicide program that is critical for the development, immune regulation and homeostasis of a multi-cellular organism. Failure to control this process can lead to serious human diseases, including many types of cancer, neurodegenerative diseases, and autoimmununity. The process of apoptosis is mediated by the sequential activation of caspases, which are cysteine proteases. Initiator caspases, such as caspase-2, -8, -9, and -10, are activated by formation of caspase-activating complexes, which function as a platform to recruit caspases, providing proximity for self-activation. Well-known initiator caspase-activating complexes include (1) DISC (Death Inducing Signaling Complex), which activates caspases-8 and 10; (2) Apoptosome, which activates caspase-9; and (3) PIDDosome, which activates caspase-2. Because of the fundamental biological importance of capases, many structural and biochemical studies to understand the molecular basis of assembly mechanism of caspase-activating complexes have been performed. In this review, we summarize previous studies that have examined the structural and biochemical features of caspase-activating complexes. By analyzing the structural basis for the assembly mechanism of the caspase-activating complex, we hope to provide a comprehensive understanding of caspase activation by these important oligomeric complexes.

KEYWORDS:

DISC; PIDDosome; apoptosis; apoptosome; caspase; inflammation; protein structure

PMID:
22606010
PMCID:
PMC3344246
DOI:
10.3390/ijms13044807
[Indexed for MEDLINE]
Free PMC Article
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