Mammalian mitochondrial IAP binding proteins

Biochem Biophys Res Commun. 2003 May 9;304(3):499-504. doi: 10.1016/s0006-291x(03)00622-3.

Abstract

Four mitochondrial proteins have been identified that immunoprecipitate with the mammalian inhibitor of apoptosis (IAP) protein XIAP. Each of them interacts via a processed amino terminus that resembles those of the insect pro-apoptotic IAP binding proteins Grim, HID, Reaper, and Sickle. Two, Diablo/Smac and HrtA2/Omi, have been extensively characterized. Both Diablo and HtrA2 can bind to IAPs and promote apoptosis when over-expressed in transfected cells, but unlike the insect IAP antagonists, to date there is scant evidence that they are important regulators of apoptosis in more physiological circumstances.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • Apoptosis Regulatory Proteins
  • Apoptosis*
  • Carrier Proteins / metabolism*
  • High-Temperature Requirement A Serine Peptidase 2
  • Inhibitor of Apoptosis Proteins
  • Intracellular Signaling Peptides and Proteins
  • Mammals / metabolism
  • Mitochondrial Proteins / metabolism*
  • Models, Biological
  • Neoplasms / drug therapy
  • Neoplasms / pathology
  • Proteins / metabolism*
  • Serine Endopeptidases / metabolism
  • X-Linked Inhibitor of Apoptosis Protein

Substances

  • Apoptosis Regulatory Proteins
  • Carrier Proteins
  • DIABLO protein, human
  • Inhibitor of Apoptosis Proteins
  • Intracellular Signaling Peptides and Proteins
  • Mitochondrial Proteins
  • Proteins
  • X-Linked Inhibitor of Apoptosis Protein
  • Serine Endopeptidases
  • HTRA2 protein, human
  • High-Temperature Requirement A Serine Peptidase 2