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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, Hexokinase
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
Succination is increased on select proteins in the brainstem of the Ndufs4 knockout mouse, a model of Leigh syndrome.
Frizzell et al., United States. In Mol Cell Proteomics, 08 Nov 2015
2D SDS-PAGE followed by immunoblotting for succinated proteins and MS/MS analysis of BS proteins allowed us to identify the voltage-dependent anion channels (VDAC) 1 and 2 as specific targets of succination in the Ndufs4 KO.
Cell-free production of VDAC directly into liposomes for integration with biomimetic membrane systems.
Martin et al., Grenoble, France. In Prep Biochem Biotechnol, 07 Nov 2015
UNASSIGNED: The mitochondrial voltage-dependent anion channel (VDAC) is a pivotal protein since it provides the major transport pathway between the cytosol and the mitochondrial intermembrane space and it is implicated in cell apoptosis by functioning as a gatekeeper for the trafficking of mitochondrial death molecules.
Polyphenols as mitochondria-targeted anticancer drugs.
Lewandowska et al., Łódź, Poland. In Cancer Lett, 01 Nov 2015
(2013) according to their molecular mode of action into: hexokinase inhibitors; mimickers of the Bcl-2 homology-3 (BH3) domains; thiol redox inhibitors; deregulators of voltage-dependent anionic channel (VDAC)/adenine nucleotide translocase (ANT) complex; electron redox chain-targeting agents; lipophilic cations targeting the mitochondrial inner membrane; tricarboxylic acid cycle-targeting agents; and mitochondrial DNA-targeting agents.
The mitochondrial voltage-dependent anion channel 1 in tumor cells.
Tripathi et al., Beersheba, Israel. In Biochim Biophys Acta, 31 Oct 2015
In addressing the recently solved 3D structures of VDAC1, this review will point to structure-function relationships of VDAC as critical for deciphering how this channel can perform such a variety of roles, all of which are important for cell life and death.
Motifs of VDAC2 required for mitochondrial Bak import and tBid-induced apoptosis.
Hajnóczky et al., Budapest, Hungary. In Proc Natl Acad Sci U S A, 28 Oct 2015
UNASSIGNED: Voltage-dependent anion channel (VDAC) proteins are major components of the outer mitochondrial membrane.
Vorinostat synergizes with EGFR inhibitors in NSCLC cells by increasing ROS via up-regulation of the major mitochondrial porin VDAC1 and modulation of the c-Myc-NRF2-KEAP1 pathway.
Budillon et al., Napoli, Italy. In Free Radic Biol Med, 24 Oct 2015
By knockdown experiments, we suggested that the up-regulation of voltage-dependent anion-selective channel protein 1 (VDAC1), the major mitochondrial porin of the outer mitochondrial membrane, which was induced by vorinostat and further increased by the combination, could be functionally involved in oxidative stress-dependent apoptosis.
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, 22 Oct 2015
UNASSIGNED: The voltage-dependent anion channels (VDACs), VDAC1, VDAC2, and VDAC3, are pore-forming proteins that control metabolite flux between mitochondria and cytoplasm.
Translocator protein-mediated pharmacology of cholesterol transport and steroidogenesis.
Midzak et al., Montréal, Canada. In Mol Cell Endocrinol, Jul 2015
Steroidogenesis begins with cholesterol transfer into mitochondria through the transduceosome, a complex composed of cytosolic proteins that include steroidogenesis acute regulatory protein (STAR), 14-3-3 adaptor proteins, and the outer mitochondrial membrane proteins Translocator Protein (TSPO) and Voltage-Dependent Anion Channel (VDAC).
Phosphorylation, nitrosation and plasminogen K3 modulation make VDAC-1 lucid as part of the extrinsic apoptotic pathway-Resulting thesis: Native VDAC-1 indispensible for finalisation of its 3D structure.
Thinnes, Göttingen, Germany. In Biochim Biophys Acta, Jun 2015
Furthermore, the multi-compartment expression makes expect even differing native VDAC-1 molecules.
[18 kDa translocator protein--implications in cell's functions].
Kołodziejczyk, Laizhou, China. In Postepy Hig Med Dosw (online), Dec 2014
TSPO has been shown to interact with other cellular proteins: 32 kDa voltage-dependent anion channel (VDAC), 30 kDa adenine nucleotide translocase (ANT), cyclophilin D, hexokinase, creatinine kinase, diazepam binding inhibitor (DBI), phosphate carrier and Bcl-2 family.
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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