Voltage gating of the mitochondrial outer membrane channel VDAC is regulated by a very conserved protein.
Soluble protein preparations obtained from the mitochondrial fractions of three very different organisms, Neurospora crassa, rat, and potato, were discovered to greatly enhance the voltage sensitivity of the mitochondrial outer membrane channel, VDAC. The active ingredient, referred to as the VDAC modulator, increased the rate of voltage-dependent channel closure by approximately 10-fold. The modulator from one species increased the closing rate of VDAC channels from all three species. The activity is pronase sensitive and not mimicked by another negatively charged protein, BSA. The highly conserved property of this modulator suggests an important physiological role in regulating mitochondrial function.
Liu
M Y
MY
Department of Zoology, University of Maryland, College Park 20742.
Colombini
M
M
D000818:Animals; D015640:Ion Channel Gating; D007473:Ion Channels / Q000187:drug effects / Q000502:physiology*; D007700:Kinetics; D008565:Membrane Proteins / Q000502:physiology*; D008928:Mitochondria / Q000502:physiology*; D008930:Mitochondria, Liver / Q000502:physiology*; D009492:Neurospora crassa / Q000502:physiology; D018272:Porins; D011506:Proteins / Q000502:physiology*; D051381:Rats; D012710:Serum Albumin, Bovine / Q000494:pharmacology; D011198:Solanum tuberosum; D013045:Species Specificity; D050994:Voltage-Dependent Anion Channels
D007473:Ion Channels; D008565:Membrane Proteins; D018272:Porins; D011506:Proteins; D050994:Voltage-Dependent Anion Channels; D012710:Serum Albumin, Bovine