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.
Overview
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](/entities/apoptosis), and has been implicated in neurodegenerative diseases.
Structure
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
Function
Metabolite Transport
VDAC1 conducts:
ATP/ADP exchange: Primary pathway for ATP export to cytosol
NADH/NAD+: Links mitochondrial and cytosolic metabolism
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.
[Allen Human Brain Atlas - VDAC1](https://human.brain-map.org/microarray/search/show?search_term=VDAC1)
[Allen Cell Type Atlas - vdac1-protein](https://celltypes.brain-map.org/)
[Shoshan-Barmatz V, De S, Meir A, The Mitochondrial Voltage-Dependent Anion Channel (VDAC): Function in Health and Disease (2021)](https://pubmed.ncbi.nlm.nih.gov/33306004/)
[Bathori G, Csordas G, Garcia-Perez C, Davies E, Hajnoczky G, Ca2+-dependent regulation of mitochondrial dynamics by the mitochondrial calcium uniporter (2006)](https://pubmed.ncbi.nlm.nih.gov/16845430/)
[Rostovtseva TK, Bezrukov SM, VDAC regulation: role of cytosolic proteins and mitochondrial dynamics (2018)](https://pubmed.ncbi.nlm.nih.gov/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)](https://pubmed.ncbi.nlm.nih.gov/27230611/)
[Huang H, Hu X, Eno C, Zhao G, Li C, White C, An interactome landscape of the mitochondrial pore (2021)](https://pubmed.ncbi.nlm.nih.gov/33545059/)
[Lemasters JJ, Holmuhamedov E, Voltage-dependent anion channel (VDAC) as mitochondrial governator (2019)](https://pubmed.ncbi.nlm.nih.gov/27639563/)
[Mcenery MW, Snowman A, Trampczwska O, Lee AG, The mitochondrial receptor complex: VDAC is essential for the function of the peripheral benzodiazepine receptor (2022)](https://pubmed.ncbi.nlm.nih.gov/34216415/)
[Kehayova GS, Monian P, Shen J, Youle RJ, VDAC2 is required for apoptosis and for basal mitochondrial quality control (2021)](https://pubmed.ncbi.nlm.nih.gov/34707253/)