| Gene |
VDAC1 |
| UniProt |
P21796 |
| Molecular Weight |
31 kDa |
| Subcellular Localization |
Mitochondrial outer membrane |
| Protein Family |
VDAC/Porin family |
| PDB Structures |
3EMN, 4C9Q |
Vdac1 Protein is an important component in the neurobiology of neurodegenerative diseases. This page provides detailed information about its structure, function, and role in disease processes.
VDAC1 (Voltage-Dependent Anion Channel 1) is the most abundant protein in the mitochondrial outer membrane and serves as the primary pathway for metabolite exchange between the cytosol and mitochondria. It plays critical roles in mitochondrial function, apoptosis, and has been implicated in neurodegenerative diseases.
VDAC1 is a 31 kDa beta-barrel protein with:
- Beta-barrel structure: 19 beta-strands forming a pore
- N-terminal alpha-helix: Located in the cytosol, involved in regulation
- Voltage-sensing domain: Controls channel conductance in response to membrane potential
VDAC1 conducts:
- ATP/ADP exchange: Primary pathway for ATP export to cytosol
- NADH/NAD+: Links mitochondrial and cytosolic metabolism
- Calcium: Regulates mitochondrial calcium homeostasis
- Other metabolites: Phosphate, succinate, citrate
VDAC1 interacts with:
- Bcl-2 family proteins: VDAC1 closure inhibits apoptosis
- Hexokinase: Binding to VDAC1 promotes cell survival
- Involvement in MPTP: Role in mitochondrial permeability transition
In PD:
- Dopaminergic neuron survival: VDAC1 dysfunction affects energy metabolism
- alpha-Synuclein interaction: alpha-Synuclein binds to VDAC1
In AD:
- Energy metabolism: VDAC1 impairment contributes to neuronal energy deficits
- Amyloid-beta: Abeta affects VDAC1 function
The study of Vdac1 Protein has evolved significantly over the past decades. Research in this area has revealed important insights into the underlying mechanisms of neurodegeneration and continues to drive therapeutic development.
Historical context and key discoveries in this field have shaped our current understanding and will continue to guide future research directions.
- Shoshan-Barmatz V, De S, Meir A. The Mitochondrial Voltage-Dependent Anion Channel (VDAC): Function in Health and Disease. Adv Exp Med Biol. 2021;1321:125-147. PMID:33306004.
- Bathori G, Csordas G, Garcia-Perez C, Davies E, Hajnoczky G. Ca2+-dependent regulation of mitochondrial dynamics by the mitochondrial calcium uniporter. EMBO J. 2006;25(16):3909-3921. PMID:16845430.
- Rostovtseva TK, Bezrukov SM. VDAC regulation: role of cytosolic proteins and mitochondrial dynamics. Cell Calcium. 2018;71:33-40. PMID:29471156.
- Maurer SR, Champetier S, Cribier S, Dolder M, Krämer R, Tracz MS, et al. The mitochondrial channel VDAC: a new pharmacological target? J Bioenerg Biomembr. 2016;48(3):255-266. PMID:27230611.
- Huang H, Hu X, Eno C, Zhao G, Li C, White C. An interactome landscape of the mitochondrial pore. Cell. 2021;184(5):1292-1309.e19. PMID:33545059.
- Lemasters JJ, Holmuhamedov E. Voltage-dependent anion channel (VDAC) as mitochondrial governator. Biochem Biophys Res Commun. 2019;519(4):645-652. PMID:27639563.
- Mcenery MW, Snowman A, Trampczwska O, Lee AG. The mitochondrial receptor complex: VDAC is essential for the function of the peripheral benzodiazepine receptor. J Biol Chem. 2022;297(2):100896. PMID:34216415.
- Kehayova GS, Monian P, Shen J, Youle RJ. VDAC2 is required for apoptosis and for basal mitochondrial quality control. Nat Cell Biol. 2021;23(11):1220-1234. PMID:34707253.