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Related Experiment Videos

Caspase-9 and APAF-1 form an active holoenzyme.

J Rodriguez1, Y Lazebnik

  • 1Cold Spring Harbor Laboratory, Cold Spring Harbor, New York 11724 USA.

Genes & Development
|January 5, 2000
PubMed
Summary

Initiator caspases like caspase-9 are activated by allosteric regulation. Binding to APAF-1 dramatically enhances caspase-9

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Background:

  • Autocatalytic activation of initiator caspases links pro-apoptotic signals to apoptosis execution.
  • Caspase-9 activation is crucial for oncogene and drug-induced apoptosis.
  • Caspase-9 activation requires binding to the protein APAF-1.

Purpose of the Study:

  • To investigate the mechanism of caspase-9 activation by APAF-1.
  • To determine the role of the caspase-9/APAF-1 complex in apoptosis.

Main Methods:

  • Biochemical assays to measure proteolytic activity.
  • Protein complex formation studies.

Main Results:

  • The caspase-9/APAF-1 complex exhibits proteolytic activity several orders of magnitude higher than free caspase-9.
  • APAF-1 acts as an allosteric regulator for caspase-9, forming a holoenzyme.

Conclusions:

  • Caspase-9 activation is mediated by allosteric regulation through APAF-1.
  • The caspase-9/APAF-1 complex functions as an active holoenzyme.
  • Allosteric activation may be a common mechanism for initiator caspase activation.

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