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Caspase activation: the induced-proximity model.

G S Salvesen1, V M Dixit

  • 1Programs in Cell Death and Aging Research, Burnham Institute, 10901 North Torrey Pines Road, La Jolla, CA 92037, USA. gsalvesen@burnham-inst.org

Proceedings of the National Academy of Sciences of the United States of America
|September 29, 1999
PubMed
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Initiator caspases, crucial for apoptosis, activate through self-processing within signaling complexes. The induced-proximity model explains this activation via adapter-mediated clustering of caspase zymogens.

Area of Science:

  • Biochemistry
  • Cell Biology
  • Molecular Biology

Background:

  • Caspases are key proteases regulating apoptosis in animal cells.
  • Initiator caspases are recruited to signaling complexes to trigger cell death.
  • Caspase activation involves autoprocessing of inactive zymogen forms.

Purpose of the Study:

  • To review evidence supporting the induced-proximity model for initiator caspase activation.
  • To explain the mechanism of protease generation in apoptosis signaling complexes.

Main Methods:

  • Review of existing literature and experimental evidence.
  • Analysis of the autoprocessing mechanism of caspase zymogens.
  • Examination of adapter-mediated clustering in signaling complexes.

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Main Results:

  • Initiator caspases possess intrinsic activity enabling autoprocessing.
  • Adapter proteins facilitate the clustering of initiator caspase zymogens.
  • Clustering induces proximity, leading to the generation of active caspases.

Conclusions:

  • The induced-proximity model provides a framework for understanding initiator caspase activation.
  • Autoprocessing of clustered zymogens is the primary mechanism for initiating the proteolytic cascade in apoptosis.
  • This mechanism ensures the precise and timely execution of programmed cell death.