VDAC Channels

  title={VDAC Channels},
  author={Elizabeth Blachly‐Dyson and Michael Forte},
  journal={IUBMB Life},
Trafficking of metabolites across the outer mitochondrial membrane is believed to be mediated primarily by the pore‐forming voltage‐dependent anion channel, VDAC (also known as mitochondrial porin). An expanding body of in vitro studies have strongly suggest that the pore formed by VDAC can be regulated in a number of ways that implicate it as a site for the regulation of mitochondrial function, yet technical limitations have prevented the extension these studies to a relevant cellular context… 
Structure of the human voltage-dependent anion channel
The 3D structure of human VDAC1, which was solved conjointly by NMR spectroscopy and x-ray crystallography, is presented, showing a β-barrel architecture composed of 19 β-strands with an α-helix located horizontally midway within the pore.
Channels of the Outer Membrane of Saccharomyces cerevisiae Mitochondria: Cooperation and Regulation
  • H. Kmita
  • Biology
    Toxicology mechanisms and methods
  • 2004
Using a simple model of Saccharomyces cerevisiae mitochondria, it is possible to study the functional relationships among the channels as well as their regulation by cellular protein.
The Diversity of the Mitochondrial Outer Membrane Protein Import Channels: Emerging Targets for Modulation
This review focuses on the channel structure, properties and transported molecules as well as aspects important to their modulation, which could be used for future studies of the cellular processes mediated by these channels, mitochondrial functioning and therapies for mitochondria-linked diseases.
Properties of the permeability transition in VDAC1(-/-) mitochondria.
Structure, gating and interactions of the voltage-dependent anion channel
The sensitivity of VDAC structure to variations in the membrane environment is explored, comparing DMPC-only, DMPC with cholesterol, and near-native lipid compositions, and using magic-angle spinning NMR spectroscopy to locate cholesterol on the outside of the β-barrel.
Pathogen inducible voltage-dependent anion channel (AtVDAC) isoforms are localized to mitochondria membrane in Arabidopsis
It is shown that the heterologous expression of AtVDAC proteins can functionally complement a yeast mutant lacking the endogenous mitochondrial VDAC gene and be rapidly up-regulated in response to a bacterial pathogen.
Modulation of the voltage-dependent anion-selective channel by cytoplasmic proteins from wild type and the channel depleted cells of Saccharomyces cerevisiae.
It is reported that the cytoplasm of wild type and Deltapor1 cells of S. cerevisiae contains a VDAC-modulating activity as measured in a reconstituted system and with intact mitochondria, and it might be concluded that VD AC may influence the properties of the involved cy toplasmic proteins.
The molecular composition of the mitochondrial permeability transition pore.
  • C. Baines
  • Biology
    Journal of molecular and cellular cardiology
  • 2009
VDAC, located in the mitochondrial outer membrane, shows high selectivity for ATP over comparably sized ions and PorA/C1 from Neisseria meningitidis achieves high cationic selectivity and large.