Scientific background: |
The voltage-dependent anion channel (VDAC) of the outer mitochondrial membrane is a small,
abundant outer membrane pore-forming protein found in the outer membranes of all eukaryotic
mitochondria. The VDAC protein is thought to form the major pathway for movement of adenine
nucleotides through the outer membrane and to be the mitochondrial binding site for hexokinase and
glycerol kinase. At low transmembrane voltage, VDAC is open for anions such as phosphate, chloride,
and adenine nucleotides. At higher transmembrane voltage, VDAC functions as a selective channel for
cations and uncharged molecules. These features make VDAC likely to play a role in mitochondrial
energy metabolism. Huizing et al. studied by Northern and Western blot analyses the human tissue
distribution of mitochondrial transmembrane metabolite carriers. They found that VDAC1 mRNA has a
ubiquitous distribution, with most pronounced expression in heart, liver, and skeletal muscle, whereas
the VDAC2 isoform appears to be expressed only in the heart. |
References: |
1. Blachly-Dyson, E., Zambronicz, E. B., Yu, W. H., Adams, V., McCabe, E. R. B., Adelman, J.,
Colombini, M., Forte, M.Cloning and functional expression in yeast of two human isoforms of the
outer mitochondrial membrane channel, the voltage-dependent anion channel.J. Biol. Chem. 268:
1835-1841, 1993.
2. Geisler, S., Holmstrom, K. M., Skujat, D., Fiesel, F. C., Rothfuss, O. C., Kahle, P. J., Springer,
W.PINK1/Parkin-mediated mitophagy is dependent on VDAC1 and p62/SQSTM1.Nature Cell Biol.
12: 119-131, 2010.
3. Huizing, M., Ruitenbeek, W., van den Heuvel, L. P., Dolce, V., Iacobazzi, V., Smeitink, J. A. M.,
Palmieri, F., Trijbels, J. M. F.Human mitochondrial transmembrane metabolite carriers: tissue
distribution and its implication for mitochondrial disorders.J. Bioenerg. Biomembr. 30: 277-284,
1998. |