Referenced in: none

Automatically associated channels: Kir2.3

Title: The mitochondrial permeability transition pore may comprise VDAC molecules. II. The electrophysiological properties of VDAC are compatible with those of the mitochondrial megachannel.

Authors: I Szabò, V De Pinto, M Zoratti

Journal, date & volume: FEBS Lett., 1993 Sep 13 , 330, 206-10

PubMed link: http://www.ncbi.nlm.nih.gov/pubmed/7689984

Abstract
The electrophysiological properties of isolated mitochondrial porin (VDAC), reconstituted in planar bilayers or proteoliposomes, resemble those of the mitochondrial megachannel believed to be the permeability transition pore. In particular, a correspondence was found with regard to the voltage dependence: VDAC was driven to closed states by potentials of either sign, but the effect was not symmetrical; voltages negative in the compartment to which VDAC was added were more effective. The results are consistent with the hypothesis that the PTP may consist of two cooperating VDAC channels, plus presumably an adenine nucleotide carrier dimer and a third component known to be part of the mitochondrial benzodiazepine receptor.