Voltage-dependent anion-selective channel protein 1 (VDAC1)

Voltage-dependent anion-selective channel protein 1 (VDAC1) is a β-barrel ion channel located in the outer mitochondrial membrane, ubiquitously expressed across eukaryotic cells[1][2][3][4][6]. It is the primary gateway for the movement of small hydrophilic molecules, nucleotides, and ions (such as ATP, ADP, Ca^2+^) between the mitochondria and cytosol, directly linking mitochondrial energetics to cytoplasmic metabolic demand[1][2][4]. VDAC1’s conformational state is voltage-dependent, alternating between open (anion-selective, high conductance) and closed (cation-selective, low conductance) forms[1][2][3][5]. Functionally, VDAC1 interacts with metabolic enzymes (such as hexokinase) and apoptosis-regulating proteins (such as Bcl-2 family members), acting as a central regulator of cell life and death, including the release of apoptotic factors like cytochrome c[4][6]. Dysregulation of VDAC1 is implicated in many diseases, including cancer (where it is often overexpressed), neurodegenerative disorders, diabetes, and cardiovascular disease[2][4][6]. As such, VDAC1 is considered a highly promising therapeutic target with ongoing drug development focused on modulating its function for cancer and other disorders[6].

Other names

Non-selective voltage-gated ion channel VDAC1VDACVDAC-1hVDAC1PORINOuter mitochondrial membrane protein porin 1Plasmalemmal porinPorin 31HLPorin 31HMSperm binding protein 1a

Blocking or modulating VDAC1 affects mitochondrial permeability and apoptosis. Disruption of interaction with Bcl-2 family proteins or hexokinase promotes apoptosis in cancer cells. Modulation of Ca^2+^ and ATP flux through outer mitochondrial membrane.