Mit Vdac

Function

forms a channel through the mitochondrial outer membrane & also the plasma membrane
the channel at the outer mitochondrial membrane allows diffusion of small hydrophilic molecules
in the plasma membrane it is involved in cell volume regulation & apoptosis.
it adopts an open conformation at low or zero membrane potential & a closed conformation at potentials > 30-40 mV
the open state has a weak anion selectivity
the closed state is cation-selective
in association with ANT ( inner mitochondrial membrane), may form the permeability transition pore complex ( PTPC)
VDAC-1 may serve as the mitochondrial binding site for:

closure of the VDAC-1 channel is the earliest observed mitochondrial change during apoptosis, blocking passage of ADP/ ATP
it is thought that bcl-2 may stablize the open conformation of VDAC-1
interacts with hexokinases ( putative)
interacts with BCL2L1
interacts with influenza A virus PB1-F2 protein

consists mainly of a membrane-spanning beta-barrel formed by 19 beta-strands
the helical N-terminus folds back into the pore opening & plays a role in voltage-gated channel activity
belongs to the eukaryotic mitochondrial porin family

Entrez gene: 7416
Kegg: [1]
OMIM: 604492
Prosite: [2]
UniProt: [3]

UniProt [4]
Benz R. Biophysical properties of porin pores from mitochondrial outer membrane of eukaryotic cells. Experientia. 1990 Feb 15;46(2):131-7. Review. PMID: [5]
Dermietzel R, Hwang TK, Buettner R, Hofer A, Dotzler E, Kremer M, Deutzmann R, Thinnes FP, Fishman GI, Spray DC, et al. Cloning and in situ localization of a brain-derived porin that constitutes a large-conductance anion channel in astrocytic plasma membranes. Proc Natl Acad Sci U S A. 1994 Jan 18;91(2):499-503. PMID: [6]
Adams JM, Cory S. Life-or-death decisions by the Bcl-2 protein family. Trends Biochem Sci. 2001 Jan;26(1):61-6. Review. PMID: [7]