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Product Reference
Caspase-9 and APAF-1 form an active holoenzyme.
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| Author |
Rodriguez, J and Lazebnik, Y |
| Citation Information |
Genes Dev., 13: 3179-84 (1999), : (1999) |
| Related Products |
05-572 |
| Pub Med ID |
10617566 |
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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.
