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Voltage-dependent anion channel 3

This gene encodes a voltage-dependent anion channel (VDAC), and belongs to the mitochondrial porin family. VDACs are small, integral membrane proteins that traverse the outer mitochondrial membrane and conduct ATP and other small metabolites. They are known to bind several kinases of intermediary metabolism, thought to be involved in translocation of adenine nucleotides, and are hypothesized to form part of the mitochondrial permeability transition pore, which results in the release of cytochrome c at the onset of apoptotic cell death. Alternatively transcript variants encoding different isoforms have been described for this gene. [provided by RefSeq, Oct 2011] (from NCBI)
Top mentioned proteins: VDAC1, VDAC2, CAN, V1a, fibrillin-1
Papers on VDAC3
VDAC3 as a sensor of oxidative state of the intermembrane space of mitochondria: the putative role of cysteine residue modifications.
De Pinto et al., Catania, Italy. In Oncotarget, Feb 2016
In mammals VDAC3, the least characterized isoform, presents a set of cysteines predicted to be exposed toward the intermembrane space.
VDAC3 gating is activated by suppression of disulfide-bond formation between the N-terminal region and the bottom of the pore.
Sodeoka et al., Wako, Japan. In Biochim Biophys Acta, Dec 2015
The voltage-dependent anion channels (VDACs), VDAC1, VDAC2, and VDAC3, are pore-forming proteins that control metabolite flux between mitochondria and cytoplasm.
Impact of sex differences in brain response to infection with Plasmodium berghei.
Al-Quraishy et al., Riyadh, Saudi Arabia. In Parasitol Res, Nov 2015
At the molecular level, P. berghei was able to induce upregulations of Adam23, Cabp1, Cacnb4, Glrb, and Vdac3-mRNA in the brain of mice.
Impact of gold nanoparticles on brain of mice infected with Schistosoma mansoni.
Al-Quraishy et al., Riyadh, Saudi Arabia. In Parasitol Res, Oct 2015
In addition, S. mansoni was able to disregulate the infected mice brain Cacnb4, Cabp4, Vdac3, Glrb, and Adam23 messenger RNA (mRNA).
MnSOD downregulation induced by extremely low 0.1 mGy single and fractionated X-rays and microgravity treatment in human neuroblastoma cell line, NB-1.
Majima et al., Kagoshima, Japan. In J Clin Biochem Nutr, Sep 2015
After 0.1 mGy fractionation irradiation, there was increased expression of proapoptotic APAF1 and downregulation of proapoptotic CYTC, VDAC2, VDAC3, CASP8, AIF, ANT1, and ANT2, as well as an increase in expression of antiapoptotic BCL2.
The interactions between mitochondria and sarcoplasmic reticulum and the proteome characterization of mitochondrion-associated membrane from rabbit skeletal muscle.
Chang et al., Beijing, China. In Proteomics, Aug 2015
This result indicated mitochondria physically linked with SR in rabbit skeletal muscle, voltage-dependent anion channel 1 (VDAC1), VDAC2, and VDAC3 might participate in formation of the tethers between SR and mitochondria.
Arabidopsis mitochondrial voltage-dependent anion channel 3 (AtVDAC3) protein interacts with thioredoxin m2.
Zhang et al., Harbin, China. In Febs Lett, Jun 2015
A yeast two-hybrid screen identified interaction between Arabidopsis VDAC3 and the chloroplast protein thioredoxin m2 (AtTrx m2).
Non-Overlapping Distributions and Functions of the VDAC Family in Ciliogenesis.
Fisk et al., Columbus, United States. In Cells, 2014
We recently showed that mitochondrial outer membrane porin VDAC3 localizes to centrosomes where it negatively regulates ciliogenesis.
Translocation of glycogen synthase kinase-3β (GSK-3β), a trigger of permeability transition, is kinase activity-dependent and mediated by interaction with voltage-dependent anion channel 2 (VDAC2).
Miura et al., Sapporo, Japan. In J Biol Chem, 2014
Knockdown of VDAC2, but not VDAC1 or VDAC3, by siRNA attenuated both the mitochondrial translocation of GSK-3β and mPTP opening under stress conditions.
Expression of the Bcl-2 family genes and complexes involved in the mitochondrial transport in prostate cancer cells.
Hinsch et al., In Int J Oncol, 2014
We investigated the expression of genes of the Bcl-2 family, i.e., pro-apoptotic Bak and Bid, and anti-apoptotic Bcl-2; VDAC gene, i.e., VDAC1, VDAC2 and VDAC3; and TOMM genes, i.e., TOMM20, TOMM22 and TOMM40.
Quantitative immunofluorescence assay to measure the variation in protein levels at centrosomes.
Fisk et al., United States. In J Vis Exp, 2013
Utilizing this assay in combination with BrdU pulse and chase strategy to study unperturbed cell cycles, we have quantitatively validated our recent observation that the centrosomal pool of VDAC3 is regulated at centrosomes during the cell cycle, likely by proteasome-mediated degradation specifically at centrosomes.
Warburg revisited: regulation of mitochondrial metabolism by voltage-dependent anion channels in cancer cells.
Lemasters et al., Charleston, United States. In J Pharmacol Exp Ther, 2012
Knockdown of different VDAC isoforms, especially of the least abundant isoform, VDAC3, also decreases ΔΨ(m), cellular ATP, and NADH/NAD+, suggesting that VDAC1 and VDAC2 are most inhibited by free tubulin.
VDAC3 has differing mitochondrial functions in two types of striated muscles.
Craigen et al., Houston, United States. In Biochim Biophys Acta, 2011
(n VDAC3 deficient mice the defect is restricted to the heart and only to complex IV.
Swapping of the N-terminus of VDAC1 with VDAC3 restores full activity of the channel and confers anti-aging features to the cell.
De Pinto et al., Catania, Italy. In Febs Lett, 2010
The substitution of the VDAC3 N-terminus with the VDAC1 N-terminus caused the chimaera to become more active than VDAC1.
Characterization of human VDAC isoforms: a peculiar function for VDAC3?
Mazzoni et al., Catania, Italy. In Biochim Biophys Acta, 2010
VDAC3 has a limited ability to support mitochondrial respiration and has no influence in the control of ROS production.
Assembly of the mitochondrial apoptosis-induced channel, MAC.
Kinnally et al., New York City, United States. In J Biol Chem, 2009
Bid catalyzes MAC formation in isolated mitochondria containing Bax and/or Bak with a time course of minutes and does not require VDAC1 or VDAC3.
Genetic strategies for dissecting mammalian and Drosophila voltage-dependent anion channel functions.
Graham et al., Houston, United States. In J Bioenerg Biomembr, 2008
The mammalian genome contains three VDAC loci termed Vdac1, Vdac2, and Vdac3, raising the question as to what function each isoform may be performing.
Human spermatozoa contain multiple targets for protein S-nitrosylation: an alternative mechanism of the modulation of sperm function by nitric oxide?
Barratt et al., Birmingham, United Kingdom. In Proteomics, 2007
VDAC3 is a novel target for protein S-nigrosylation in spermatozoa.
RAS-RAF-MEK-dependent oxidative cell death involving voltage-dependent anion channels.
Stockwell et al., New York City, United States. In Nature, 2007
RNA-interference-mediated knockdown of VDAC2 or VDAC3 caused resistance to erastin, implicating these two VDAC isoforms in the mechanism of action of erastin.
Voltage-dependent anion channels are dispensable for mitochondrial-dependent cell death.
Molkentin et al., Cincinnati, United States. In Nat Cell Biol, 2007
Vdacs are dispensable for both MPT and Bcl-2 family member-driven cell death.
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