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.
journal_name
Int J Mol Scijournal_title
International journal of molecular sciencesauthors
Park HHdoi
10.3390/ijms13044807subject
Has Abstractpub_date
2012-01-01 00:00:00pages
4807-18issue
4issn
1422-0067pii
ijms-13-04807journal_volume
13pub_type
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journal_title：International journal of molecular sciences
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更新日期：2018-03-27 00:00:00
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journal_title：International journal of molecular sciences
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journal_title：International journal of molecular sciences
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