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

Voltage-dependent anion-selective channel protein 1 (VDAC1), frequently referred to as mitochondrial porin, is a 30 kDa beta-barrel protein located in the outer mitochondrial membrane. It functions as the primary conduit for the exchange of ions and essential metabolites, such as ATP, ADP, and respiratory substrates, between the mitochondria and the cytoplasm, thereby acting as a gatekeeper of mitochondrial metabolism (1.2.1, 1.2.3). In cancer cells, VDAC1 is typically overexpressed and associates with hexokinase to promote the Warburg effect and suppress apoptosis, making its inhibition or the disruption of its protein-protein interactions a viable strategy for inducing tumor cell death (1.3.2, 1.3.5). Conversely, in neurodegenerative conditions like Alzheimer's and Parkinson's diseases, VDAC1 is implicated in pathological mitochondrial permeabilization and cell death, where its modulation may offer neuroprotective benefits (1.2.4, 1.3.1). Drugs targeting VDAC1, such as erastin and VBIT-4, aim to either induce ferroptosis or prevent harmful oligomerization, highlighting its versatility as a therapeutic target across multiple disease areas (1.3.3, 1.3.4).

Other names

Mitochondrial porinVDAC1VDAC-1Porin 31HLPorin 31HMOuter mitochondrial membrane protein porin 1Plasmalemmal porin

Modulation of mitochondrial outer membrane permeability, inhibition of VDAC1 oligomerization, and disruption of VDAC1-hexokinase interactions to regulate metabolic flux and apoptosis.