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Voltage-dependent anion channel 1

VDAC1, Voltage-Dependent Anion Channel 1, VDAC, POR1
This gene encodes a voltage-dependent anion channel protein that is a major component of the outer mitochondrial membrane. The encoded protein facilitates the exchange of metabolites and ions across the outer mitochondrial membrane and may regulate mitochondrial functions. This protein also forms channels in the plasma membrane and may be involved in transmembrane electron transport. Alternate splicing results in multiple transcript variants. Multiple pseudogenes of this gene are found on chromosomes 1, 2 3, 6, 9, 12, X and Y.[provided by RefSeq, Sep 2010] (from NCBI)
Top mentioned proteins: CAN, bcl-2, ACID, V1a, Bax
Papers using VDAC1 antibodies
Mitochondrial and Nuclear Genomic Responses to Loss of LRPPRC Expression*
Mootha Vamsi K. et al., In The Journal of Biological Chemistry, 2008
... Antibodies including CO2, NDUFB8, SDHB, UQCRC2, ATP5A, and VDAC1 were purchased from Mitosciences (Eugene, OR) ...
Bioinformatics enrichment tools: paths toward the comprehensive functional analysis of large gene lists
Martelli Fabio, In PLoS ONE, 2008
... Antibody for VDAC1 (ab15895) (1∶500) was from Abcam.
The mitochondrial permeability transition, release of cytochrome c and cell death. Correlation with the duration of pore openings in situ.
Koch Karl-Wilhelm, In PLoS ONE, 2000
... Sigma; the monoclonal anti-CyP-D antibody was from Calbiochem (San Diego, CA); the rabbit polyclonal anti VDAC1 antibody was from Abcam, (Cambridge, UK); the goat ...
ARL4, an ARF-like Protein That Is Developmentally Regulated and Localized to Nuclei and Nucleoli
Aspenstrom Pontus, In PLoS ONE, 1999
... ATPase, Bax (Santa Cruz Biotechnology, Santa Cruz, CA, USA), VDAC (Cell Signaling Technology, Danvers, MA, USA), ...
Serine phosphorylation of death agonist BAD in response to survival factor results in binding to 14-3-3 not BCL-X(L)
Youle Richard J. et al., In The Journal of Cell Biology, 1995
... Human VDAC-1 (a gift from Michael Forte, Vollum Institute, Oregon Health Sciences University, Portland, OR) was cloned into the DsRed vector (CLONTECH Laboratories, Inc.) ...
Papers on VDAC1
Inhibition of VDAC1 prevents Ca(2+)-mediated oxidative stress and apoptosis induced by 5-aminolevulinic acid mediated sonodynamic therapy in THP-1 macrophages.
Tian et al., Harbin, China. In Apoptosis, 24 Nov 2014
Here we investigated the effects of inhibition of voltage-dependent anion channel 1 (VDAC1) on ALA-SDT-induced THP-1 macrophages apoptosis.
VDAC phosphorylation, a lipid sensor influencing the cell fate.
Brenner et al., Montréal, Canada. In Mitochondrion, Aug 2014
UNLABELLED: The voltage-dependent anion channel (VDAC) or porin is a major membrane protein integrated into the mitochondrial outer membrane in eukaryotes.
Measurement of mitochondrial Ca2+ transport mediated by three transport proteins: VDAC1, the Na+/Ca2+ exchanger, and the Ca2+ uniporter.
Shoshan-Barmatz et al., Beersheba, Israel. In Cold Spring Harb Protoc, Feb 2014
The first of these is Ca(2+) transport mediated by the outer mitochondrial protein, the voltage-dependent anion-selective channel protein 1 (VDAC1, also known as porin 1), both as a purified protein reconstituted into a planar lipid bilayer (PLB) or into liposomes and as a mitochondrial membrane-embedded protein.
Mcl-1 promotes lung cancer cell migration by directly interacting with VDAC to increase mitochondrial Ca(2+) uptake and reactive oxygen species generation.
White et al., North Chicago, United States. In Cell Death Dis, Dec 2013
We now report the physiological significance of an interaction between Mcl-1 and the mitochondrial outer membrane-localized voltage-dependent anion channel (VDAC) in NSCLC cell lines.
Expression profiling of mitochondrial voltage-dependent anion channel-1 associated genes predicts recurrence-free survival in human carcinomas.
Bang et al., Seoul, South Korea. In Plos One, Dec 2013
Our previous study demonstrated that the human gene VDAC1 (encoding the VDAC-1 isoform) was significantly up-regulated in lung tumor tissue compared with normal tissue.
Plasma membrane coenzyme Q: evidence for a role in autism.
Gvozdjáková et al., West Lafayette, United States. In Biologics, Dec 2013
DATA SOURCES: Correlation of porin redox activity and expression of autism is based on extensive literature, especially studies of antibodies, identification of cytosolic nicotinamide adenine dinucleotide reduced (NADH) dehydrogenase activity in the VDAC, and evidence for extreme sensitivity of the dehydrogenase to a mercurial.
Hypoxic VDAC1: a potential mitochondrial marker for cancer therapy.
Mazure et al., Nice, France. In Adv Exp Med Biol, Dec 2013
The mitochondrial voltage-dependent anion channel (VDAC) is a protein at the crossroads of metabolic and survival pathways.
Glyceraldehyde-3-Phosphate Dehydrogenase Acts as a Mitochondrial Trans-S-Nitrosylase in the Heart.
Steenbergen et al., Baltimore, United States. In Plos One, Dec 2013
Further, the overexpression of GAPDH in HepG2 cells increased SNO for a number of different mitochondrial proteins, including heat shock protein 60, voltage-dependent anion channel 1, and acetyl-CoA acetyltransferase, thus supporting the role of GAPDH as a potential mitochondrial trans-S-nitrosylase.
Auranofin promotes mitochondrial apoptosis by inducing annexin a5 expression and translocation in human prostate cancer cells.
Chun et al., Seoul, South Korea. In J Toxicol Environ Health A, Dec 2013
In addition, auranofin enhanced oligomerization of the voltage-dependent anion channel (VDAC) in a concentration- and time-dependent manner.
Intracellular ion channels and cancer.
Szabò et al., Padova, Italy. In Front Physiol, 2012
Mitochondrial K(+) channels (Ca(2+)-dependent BKCa and IKCa, ATP-dependent KATP, Kv1.3, two-pore TWIK-related Acid-Sensitive K(+) channel-3 (TASK-3)), Ca(2+) uniporter MCU, Mg(2+)-permeable Mrs2, anion channels (voltage-dependent chloride channel VDAC, intracellular chloride channel CLIC) and the Permeability Transition Pore (MPTP) contribute importantly to the regulation of function in this organelle.
Structural basis for membrane binding specificity of the Bin/Amphiphysin/Rvs (BAR) domain of Arfaptin-2 determined by Arl1 GTPase.
Wakatsuki et al., Tsukuba, Japan. In J Biol Chem, 2012
The Arl1.Arfaptin-2 BAR structure suggests that one of the two Arl1 molecules competes with Rac1, which binds to the concave face of the Arfaptin-2 BAR homodimer and may hinder its membrane association.
Mediation of the antiapoptotic activity of Bcl-xL protein upon interaction with VDAC1 protein.
Shoshan-Barmatz et al., Beersheba, Israel. In J Biol Chem, 2012
Interfering with Bcl-xL binding to the mitochondria by VDAC1-based peptides may serve to induce apoptosis in cancer cells.
Structure-based analysis of VDAC1: N-terminus location, translocation, channel gating and association with anti-apoptotic proteins.
Shoshan-Barmatz et al., Beersheba, Israel. In Biochem J, 2012
A single cysteine-residue-bearing VDAC1 demonstrates that the N-terminal region lies inside the channel pore.
Peripheral benzodiazepine receptor regulates vascular endothelial activations via suppression of the voltage-dependent anion channel-1.
Jeon et al., Taejŏn, South Korea. In Febs Lett, 2012
PBR can inhibit endothelial activation through inhibition of mitochondrial ROS and/or VDAC-1 expression in endothelial cells
Lipid dynamics and protein-lipid interactions in 2D crystals formed with the β-barrel integral membrane protein VDAC1.
Griffin et al., Cambridge, United States. In J Am Chem Soc, 2012
analysis of lipid dynamics and protein-lipid interactions in 2D crystals formed with the beta-barrel integral membrane protein VDAC1
PKCε promotes oncogenic functions of ATF2 in the nucleus while blocking its apoptotic function at mitochondria.
Ronai et al., Los Angeles, United States. In Cell, 2012
Genotoxic stress attenuates PKCε effect on ATF2; enables ATF2 nuclear export and localization at the mitochondria, where it perturbs the HK1-VDAC1 complex; increases mitochondrial permeability; and promotes apoptosis.
PINK1/Parkin-mediated mitophagy is dependent on VDAC1 and p62/SQSTM1.
Springer et al., Tübingen, Germany. In Nat Cell Biol, 2010
Data identified VDAC1 (voltage-dependent anion channel 1) as a target for Parkin-mediated Lys 27 poly-ubiquitylation and mitophagy.
Solution structure of the integral human membrane protein VDAC-1 in detergent micelles.
Wagner et al., Boston, United States. In Science, 2008
study presents NMR solution structure of recombinant VDAC-1 reconstituted in detergent micelles
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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