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• W2000877238 abstract "Key structural and catalytic features are conserved across the entire family of cysteine-dependent aspartate-specific proteases (caspases). Of the caspases involved in apoptosis signal transduction, the initiator caspases-2, -8 and -9 are activated at multi-protein activation platforms, and activation is thought to involve homo-dimerisation of the monomeric zymogens. Caspase-9, the essential initiator caspase required for apoptosis signalling through the mitochondrial pathway, is activated on the apoptosome complex, and failure to activate caspase-9 has profound pathophysiological consequences. Here, we review the pertinent literature on which the currently prevalent understanding of caspase-9 activation is based, extend this view by insight obtained from recent structural and kinetic studies on caspase-9 signalling, and describe an emerging model for the regulation of caspase-9 activation and activity that arise from the complexity of multi-protein interactions at the apoptosome. This integrated view allows us to postulate and to discuss functional consequences for caspase-9 activation and apoptosis execution that may take centre stage in future experimental cell research on apoptosis signalling." @default.
• W2000877238 created "2016-06-24" @default.
• W2000877238 creator A5063932219 @default.
• W2000877238 creator A5064758952 @default.
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• W2000877238 date "2012-07-01" @default.
• W2000877238 modified "2023-10-10" @default.
• W2000877238 title "The central role of initiator caspase-9 in apoptosis signal transduction and the regulation of its activation and activity on the apoptosome" @default.
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• W2000877238 doi "https://doi.org/10.1016/j.yexcr.2012.02.013" @default.
• W2000877238 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/22406265" @default.
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