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The mitochondrial outer membrane channel, VDAC, is modulated by a soluble protein

Authors
Journal
FEBS Letters
0014-5793
Publisher
Wiley Blackwell (John Wiley & Sons)
Publication Date
Volume
241
Identifiers
DOI: 10.1016/0014-5793(88)81040-8
Keywords
  • Ion Channel
  • Voltage-Dependent Channel
  • Mitochondria
  • Regulation
  • Mitochondrial Membrane
  • (Neurospora Crassa)
Disciplines
  • Biology

Abstract

Abstract The mitochondrial outer membrane channel, VDAC, serves as the primary permeability pathway for metabolite flux between cytoplasmic and mitochondrial compartments. VDAC can occupy several conformational states differing in ion conductivity. Small transmembrane potentials cause transitions from open- to closed-channel conformations. A soluble mitochondrial protein enhances the channel's response to voltage by increasing the rate of channel closing; inducing the occupation of lower conductance states; and decreasing the rate of channel reopening. This protein modulator acts at very low concentrations and its role in the cell may be to regulate the permeability of the mitochondrial outer membrane by inducing channel closure.

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