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Int. J. Mol. Sci. 2012, 13(4), 4807-4818; doi:10.3390/ijms13044807
Review

Structural Features of Caspase-Activating Complexes

Received: 7 March 2012; in revised form: 28 March 2012 / Accepted: 10 April 2012 / Published: 16 April 2012
(This article belongs to the Special Issue Protein Crystallography in Molecular Biology)
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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: apoptosis; inflammation; caspase; apoptosome; DISC; PIDDosome; protein structure apoptosis; inflammation; caspase; apoptosome; DISC; PIDDosome; protein structure
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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MDPI and ACS Style

Park, H.H. Structural Features of Caspase-Activating Complexes. Int. J. Mol. Sci. 2012, 13, 4807-4818.

AMA Style

Park HH. Structural Features of Caspase-Activating Complexes. International Journal of Molecular Sciences. 2012; 13(4):4807-4818.

Chicago/Turabian Style

Park, Hyun Ho. 2012. "Structural Features of Caspase-Activating Complexes." Int. J. Mol. Sci. 13, no. 4: 4807-4818.


Int. J. Mol. Sci. EISSN 1422-0067 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert