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Gene Review

Vdac1  -  voltage-dependent anion channel 1

Mus musculus

Synonyms: AL033343, Outer mitochondrial membrane protein porin 1, Plasmalemmal porin, VDAC-1, VDAC-5, ...
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Disease relevance of Vdac1

  • We have investigated the cellular localization of VDAC and its relationship with the antiestrogen-activated Maxi Cl- current in C1300 neuroblastoma cells [1].

High impact information on Vdac1


Biological context of Vdac1


Anatomical context of Vdac1

  • A mitochondrial porin (voltage-dependent anion channel (VDAC)) located in the plasma membrane has long been considered as the molecule underlying the maxianion channel activity, based upon similarities in the biophysical properties of these two channels and the purported presence of VDAC protein in the plasma membrane [7].
  • We have deleted each of the three genes encoding the VDAC isoforms individually and collectively and demonstrate that maxianion channel (approximately 400 picosiemens) activity in VDAC-deficient mouse fibroblasts is unaltered [7].
  • Photolabeling of 35-kDa protein with [(3)H]6-AziP was reduced 85% in brain membranes prepared from VDAC-1-deficient mice but was unaffected by deficiency of VDAC-3 [8].
  • Isolated mitochondria exhibit large differences in their outer membrane permeability to NADH depending on which of the mouse VDAC proteins was expressed [9].
  • VDAC1 protein levels in the uterus also correlated well with the apoptotic index of the luminal epithelium [10].

Associations of Vdac1 with chemical compounds

  • This study examines the contribution of steroid binding to VDAC proteins to modulation of GABA(A) receptor function and anesthesia [8].
  • Finally, the neuroactive steroid pregnanolone [(3alpha,5beta)-3-hydroxypregnan-20-one] produced anesthesia (loss of righting reflex) in VDAC-1- and VDAC-3-deficient mice, and there was no difference in the recovery time between the VDAC-deficient mice and wild-type controls [8].
  • To test whether VDAC1 is required for creatine stimulation of mitochondrial respiration in oxidative muscles, the apparent Km((ADP)) and Vmax were determined in the presence of 25 mm creatine [11].
  • Well-differentiated cultures from nasal and tracheal epithelia of VDAC-1 (-/-) mice exhibited less ATP release in response to luminal hypotonic challenge than WT mice [5].
  • An involvement of VDAC is also supported by responses of the patches to the presence of polyanion or treatment with succinic anhydride, both of which affect VDAC [12].

Physical interactions of Vdac1

  • These results provide strong evidence that PBR is not a single protein receptor but a multimeric complex in which the IQ binding site is on the M(r) 18,000 subunit and expression of the BZ binding site requires both the M(r) 18,000 and 34,000 voltage-dependent anion channel subunits [13].

Regulatory relationships of Vdac1


Other interactions of Vdac1

  • The photolabeled 35-kDa protein in membranes from VDAC-1-deficient mice was identified by two-dimensional electrophoresis and electrospray ionization-tandem mass spectrometry as VDAC-2 [8].
  • Pathological relevance is demonstrated by the cytotoxic synergism between HAL and the Alzheimer disease-related peptide beta-amyloid(1-40), which correlates with Bcl-XS expression and its interaction with VDAC, and with cytosolic cytochrome c translocation [15].
  • Altered mitochondrial sensitivity for ADP and maintenance of creatine-stimulated respiration in oxidative striated muscles from VDAC1-deficient mice [11].
  • The mPT pore is thought to consist of the adenine nucleotide translocator, a voltage-dependent anion channel, and cyclophilin D (the Ppif gene product), a prolyl isomerase located within the mitochondrial matrix [16].

Analytical, diagnostic and therapeutic context of Vdac1

  • The mouse vdac1 gene has been disrupted by gene targeting, and the resulting mutant mice have been examined for defects in muscle physiology [11].
  • Confocal microscopy studies revealed that cell volume acutely increased in airway epithelia from both VDAC-1 (-/-) and WT mice after luminal hypotonic challenge, but VDAC-1 (-/-) cells exhibited a slower regulatory volume decrease (RVD) than WT cells [5].
  • The presence of a plasma membrane VDAC was demonstrated by immunoblotting of membrane fractions with monoclonal antibodies against the VDAC and by reverse transcription-PCR using primers that hybridize to a VDAC sequence coding for an N-terminal leader peptide required for its plasma membrane sorting [1].


  1. Plasma membrane voltage-dependent anion channel mediates antiestrogen-activated maxi Cl- currents in C1300 neuroblastoma cells. Bahamonde, M.I., Fernández-Fernández, J.M., Guix, F.X., Vázquez, E., Valverde, M.A. J. Biol. Chem. (2003) [Pubmed]
  2. Bcl-xL prevents cell death following growth factor withdrawal by facilitating mitochondrial ATP/ADP exchange. Vander Heiden, M.G., Chandel, N.S., Schumacker, P.T., Thompson, C.B. Mol. Cell (1999) [Pubmed]
  3. Evidence for secretory pathway localization of a voltage-dependent anion channel isoform. Buettner, R., Papoutsoglou, G., Scemes, E., Spray, D.C., Dermietzel, R. Proc. Natl. Acad. Sci. U.S.A. (2000) [Pubmed]
  4. The voltage-dependent anion channel-1 modulates apoptotic cell death. Zaid, H., Abu-Hamad, S., Israelson, A., Nathan, I., Shoshan-Barmatz, V. Cell Death Differ. (2005) [Pubmed]
  5. Voltage-dependent anion channel-1 (VDAC-1) contributes to ATP release and cell volume regulation in murine cells. Okada, S.F., O'Neal, W.K., Huang, P., Nicholas, R.A., Ostrowski, L.E., Craigen, W.J., Lazarowski, E.R., Boucher, R.C. J. Gen. Physiol. (2004) [Pubmed]
  6. A novel mouse mitochondrial voltage-dependent anion channel gene localizes to chromosome 8. Sampson, M.J., Lovell, R.S., Davison, D.B., Craigen, W.J. Genomics (1996) [Pubmed]
  7. Genetic demonstration that the plasma membrane maxianion channel and voltage-dependent anion channels are unrelated proteins. Sabirov, R.Z., Sheiko, T., Liu, H., Deng, D., Okada, Y., Craigen, W.J. J. Biol. Chem. (2006) [Pubmed]
  8. Neuroactive steroid interactions with voltage-dependent anion channels: lack of relationship to GABA(A) receptor modulation and anesthesia. Darbandi-Tonkabon, R., Manion, B.D., Hastings, W.R., Craigen, W.J., Akk, G., Bracamontes, J.R., He, Y., Sheiko, T.V., Steinbach, J.H., Mennerick, S.J., Covey, D.F., Evers, A.S. J. Pharmacol. Exp. Ther. (2004) [Pubmed]
  9. Mouse VDAC isoforms expressed in yeast: channel properties and their roles in mitochondrial outer membrane permeability. Xu, X., Decker, W., Sampson, M.J., Craigen, W.J., Colombini, M. J. Membr. Biol. (1999) [Pubmed]
  10. Mouse uterine epithelial apoptosis is associated with expression of mitochondrial voltage-dependent anion channels, release of cytochrome C from mitochondria, and the ratio of Bax to Bcl-2 or Bcl-X. Takagi-Morishita, Y., Yamada, N., Sugihara, A., Iwasaki, T., Tsujimura, T., Terada, N. Biol. Reprod. (2003) [Pubmed]
  11. Altered mitochondrial sensitivity for ADP and maintenance of creatine-stimulated respiration in oxidative striated muscles from VDAC1-deficient mice. Anflous, K., Armstrong, D.D., Craigen, W.J. J. Biol. Chem. (2001) [Pubmed]
  12. Properties of channels in the mitochondrial outer membrane. Tedeschi, H., Kinnally, K.W., Mannella, C.A. J. Bioenerg. Biomembr. (1989) [Pubmed]
  13. In vitro reconstitution of a functional peripheral-type benzodiazepine receptor from mouse Leydig tumor cells. Garnier, M., Dimchev, A.B., Boujrad, N., Price, J.M., Musto, N.A., Papadopoulos, V. Mol. Pharmacol. (1994) [Pubmed]
  14. Negative regulation of mitochondrial VDAC channels by C-Raf kinase. Le Mellay, V., Troppmair, J., Benz, R., Rapp, U.R. BMC Cell Biol. (2002) [Pubmed]
  15. Haloperidol induces apoptosis via the sigma2 receptor system and Bcl-XS. Wei, Z., Mousseau, D.D., Dai, Y., Cao, X., Li, X.M. Pharmacogenomics J. (2006) [Pubmed]
  16. Loss of cyclophilin D reveals a critical role for mitochondrial permeability transition in cell death. Baines, C.P., Kaiser, R.A., Purcell, N.H., Blair, N.S., Osinska, H., Hambleton, M.A., Brunskill, E.W., Sayen, M.R., Gottlieb, R.A., Dorn, G.W., Robbins, J., Molkentin, J.D. Nature (2005) [Pubmed]
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