Unable to load your collection due to an error The human Bcl-2 family member Bcl-rambo and voltage-dependent anion channels manifest a genetic interaction in Drosophila and cooperatively promote the activation of effector caspases in human cultured cells. In PD, VDAC1 increases calcium ion levels within the mitochondria, resulting in increased mitochondrial permeability, disrupted mitochondrial membrane potential, elevated ROS production, cell death, and neuronal degeneration.VDAC1 acts as a scaffold for many proteins as well as allows for the flux of ions and metabolites through interactions within the pore. Protein knowledgebase. VDAC forms a channel through the mitochondrial membrane and is involved in small molecule diffusion, cell volume regulation and apoptosis.

Sequence clusters. Introduction. Sabirov RZ, Sheiko T, Liu H, Deng D, Okada Y, Craigen WJ.J Biol Chem. 2015 May;44(1):224-31. doi: 10.1016/j.fsi.2014.12.012. Roy SW, Gilbert W.

This major protein of the outer mitochondrial membrane of eukaryotes forms a voltage-dependent anion-selective channel (VDAC) that behaves as a general diffusion pore for small hydrophilic molecules. Ital J Biochem. Because of their role, dysfunction of the channels can lead to various diseases. Users can perform simple and advanced searches based on annotations relating to sequence, structure and function. Since this achievement VDAC has been extensively investigated: its functional features have been sharply defined upon reconstitution in artificial membranes and its sequence has been determined in many genomes.
A prominent feature of the pore emerged: when reconstituted into planar More than 30 years after its initial discovery, in 2008, three independent structural projects of VDAC-1 were completed.

voltage-dependent anion-selective channel protein 1, outer mitochondrial membrane protein porin 1, plasmalemmal porin, porin 31HL, porin 31HM, sperm binding protein 1a. 1. Despite this established knowledge, in the last few years this protein has attracted renewed interest. 1994 Mar 1;20(1):62-7. doi: 10.1006/geno.1994.1127.Hinsch KD, De Pinto V, Aires VA, Schneider X, Messina A, Hinsch E.J Biol Chem. It is involved in the transport of Yeast contains two members of this family (genes POR1 and POR2); vertebrates have at least three members (genes VDAC1, VDAC2 and VDAC3).Humans, like most higher eukaryotes, encode three different VDACs; Plants have the largest number of VDACs. The arrows denote the antiparallel beta sheets that form the characteristic beta-barrelThis article incorporates text from the public domain
Epub 2020 Mar 9.Paschon V, Morena BC, Correia FF, Beltrame GR, Dos Santos GB, Cristante AF, Kihara AH.Sci Rep. 2019 Oct 1;9(1):14063. doi: 10.1038/s41598-019-50506-4.Sherman HG, Jovanovic C, Stolnik S, Baronian K, Downard AJ, Rawson FJ.Front Mol Biosci. The three VDAC isoforms (VDAC1, VDAC2, and VDAC3) have highly conserved DNA sequences as well as 3D structures forming a wide β-barrel structure, inside of which the alpha helical N-terminal segment resides to partially close the pore.Structural analysis of mVDAC1's structure showed a barrel-like channel composed of 19 amphipathic β-strands, with the N-terminus and C-terminus both facing towards the inter membrane space of the mitochondrion.VDAC1 belongs to the mitochondrial porin family and is expected to share similar biological functions to the other VDAC isoforms.VDAC1 allows for the conductance of molecules into and out of the mitochondrion. VDAC1 (Voltage Dependent Anion Channel 1) is a Protein Coding gene. 2010 Oct 1;431(1):13-22. doi: 10.1042/BJ20100371.Eur Biophys J. Epub 2005 Nov 16.Blachly-Dyson E, Baldini A, Litt M, McCabe ER, Forte M.Genomics. NX_P21796 - VDAC1 - Voltage-dependent anion-selective channel protein 1 - Function. Please enable it to take advantage of the complete set of features!

Epub 2014 Dec 23. At low voltage (10mV), the pore is in an "open" state where the channel is weakly anion selective and allows for a greater flux of metabolites. 2017 Apr 10;7:60. doi: 10.3389/fonc.2017.00060.

doi: 10.1016/j.biocel.2004.05.013. 1. eCollection 2017. Exp Cell Res 381:223-234 (2019).