On the role of VDAC in apoptosis: fact and fiction

J Bioenerg Biomembr. 2005 Jun;37(3):129-42. doi: 10.1007/s10863-005-6566-8.

Abstract

Research on VDAC has accelerated as evidence grows of its importance in mitochondrial function and in apoptosis. New investigators entering the field are often confounded by the VDAC literature and its many apparent conflicts and contradictions. This review is an effort to shed light on the situation and identify reliable information from more questionable claims. Our views on the most important controversial issues are as follows: VDAC is only present in the mitochondrial outer membrane. VDAC functions as a monomer. VDAC functions normally with or without Ca(2+). It does not form channels that mediate the flux of proteins through membranes (peptides and unfolded proteins are excluded from this statement). Closure of VDAC, not VDAC opening, leads to mitochondria outer membrane permeabilization and apoptosis.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Apoptosis / physiology*
  • Calcium / metabolism
  • Dimerization
  • Hexokinase / metabolism
  • Humans
  • Ion Channel Gating
  • Ion Channels / physiology*
  • Mitochondria / physiology*
  • Mitochondrial Membrane Transport Proteins
  • Mitochondrial Membranes / physiology*
  • Mitochondrial Permeability Transition Pore
  • Proto-Oncogene Proteins c-bcl-2 / physiology
  • Reactive Oxygen Species / metabolism
  • Voltage-Dependent Anion Channels / physiology*

Substances

  • Ion Channels
  • Mitochondrial Membrane Transport Proteins
  • Mitochondrial Permeability Transition Pore
  • Proto-Oncogene Proteins c-bcl-2
  • Reactive Oxygen Species
  • Voltage-Dependent Anion Channels
  • Hexokinase
  • Calcium