Caspase-9 and APAF-1 form an active holoenzyme

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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URL: http://www.ncbi.nlm.nih.gov/pubmed/10617566

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: http://repository.cshl.edu/id/eprint/26395

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