Rodriguez, J., Lazebnik, Y. (1999) Caspase-9 and APAF-1 form an active holoenzyme. Genes & Development, 13 (24). pp. 3179-3184. ISSN 0890-9369
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Abstract
Autocatalytic activation of initiator caspases is the link between pro-apoptotic signals and the destruction machinery of apoptosis. Activation of caspase-9, which mediates oncogene and drug-induced apoptosis, requires binding to the protein APAF-1. We found that the proteolytic activity of caspase-9 in a complex with APAF-1 is several orders of magnitude higher than that of the free enzyme. Thus, this complex functions as a holoenzyme in which caspase-9 is the catalytic subunit and APAF-1 its allosteric regulator. We argue that caspase-9 is activated by allosteric regulation and suggest that this mechanism is common for other initiator caspases.
| Item Type: | Paper |
|---|---|
| Uncontrolled Keywords: | Allosteric Regulation Apoptosis Apoptotic Protease-Activating Factor 1 Caspase 9 Caspases Catalytic Domain Cell Line Cell-Free System Centrifugation, Density Gradient Humans Kinetics Proteins Substrate Specificity |
| Subjects: | organs, tissues, organelles, cell types and functions > cell types and functions > cell functions > apoptosis organs, tissues, organelles, cell types and functions > cell types and functions > cell functions |
| CSHL Authors: | |
| Communities: | CSHL labs > Labeznik lab |
| Depositing User: | Matt Covey |
| Date: | 1999 |
| Date Deposited: | 12 Dec 2012 17:30 |
| Last Modified: | 12 Dec 2012 17:30 |
| PMCID: | PMC317200 |
| Related URLs: | |
| URI: | https://repository.cshl.edu/id/eprint/26395 |
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