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Related Experiment Videos

Mammalian mitochondrial IAP binding proteins.

David L Vaux1, John Silke

  • 1The Walter and Eliza Hall Institute of Medical Research, 1G Royal Parade, Parkville, Victoria 3050, Australia. vaux@wehi.edu.au

Biochemical and Biophysical Research Communications
|May 6, 2003
PubMed
Summary

Researchers found four mitochondrial proteins that bind to XIAP, a protein regulating cell death. Two proteins, Diablo/Smac and HtrA2/Omi, promote apoptosis but their physiological roles in regulating cell death remain unclear.

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • The inhibitor of apoptosis (IAP) protein XIAP plays a critical role in regulating programmed cell death.
  • Insect IAP antagonists, such as Grim and Reaper, are well-characterized pro-apoptotic proteins.
  • Understanding mammalian regulators of apoptosis is crucial for deciphering cell death pathways.

Purpose of the Study:

  • To identify and characterize mitochondrial proteins that interact with the mammalian IAP protein XIAP.
  • To investigate the role of these interacting proteins in the regulation of apoptosis.

Main Methods:

  • Immunoprecipitation assays were used to identify proteins interacting with XIAP.
  • Overexpression studies in transfected cells were performed to assess the pro-apoptotic function of identified proteins.

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Main Results:

  • Four mitochondrial proteins were identified that immunoprecipitate with XIAP.
  • These proteins interact with XIAP via a processed amino terminus similar to insect IAP-binding proteins.
  • Two proteins, Diablo/Smac and HtrA2/Omi, were extensively characterized and shown to bind IAPs.
  • Overexpression of Diablo and HtrA2 promoted apoptosis in transfected cells.

Conclusions:

  • Mitochondrial proteins Diablo/Smac and HtrA2/Omi interact with XIAP and can induce apoptosis.
  • Despite their pro-apoptotic activity in vitro, their physiological significance in regulating apoptosis requires further investigation.