ArticleJournal of molecular biology2010
The electrostatics of VDAC: implications for selectivity and gating.
Article in Journal of molecular biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.
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Who cites it
53 citing papers in PubMed, 87 citations in OpenAlex.
- Polarized mitochondrial respiratory chain complexes in synaptic mitochondria induced by plasticity signals.Molecular and cellular biochemistry · 2026Article
- Elliptical β-barrel deformation underlies gating in VDAC1.Protein science : a publication of the Protein Society · 2026Article
- Dynamic Coupling between Tom22 Motions and Tom40 Pore Dynamics Modulates Ion Transport in the Mitochondrial TOM Complex.Journal of chemical information and modeling · 2025Article
- Article
- The Name Is Barrel, β-Barrel.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Gating of β-Barrel Protein Pores, Porins, and Channels: An Old Problem with New Facets.International journal of molecular sciences · 2023Review
- The Single Residue K12 Governs the Exceptional Voltage Sensitivity of Mitochondrial Voltage-Dependent Anion Channel Gating.Journal of the American Chemical Society · 2022Article
- Small molecules targeting the NADH-binding pocket of VDAC modulate mitochondrial metabolism in hepatocarcinoma cells.Biomedicine & pharmacotherapy = Biomedecine & pharmacotherapie · 2022Article
- Outer membrane protein evolution.Current opinion in structural biology · 2021Review
- The Open State Selectivity of the Bean Seed VDAC Depends on Stigmasterol and Ion Concentration.International journal of molecular sciences · 2021Article
- A Calcium Guard in the Outer Membrane: Is VDAC a Regulated Gatekeeper of Mitochondrial Calcium Uptake?International journal of molecular sciences · 2021Review
- VDAC Modulation of Cancer Metabolism: Advances and Therapeutic Challenges.Frontiers in physiology · 2021Review
- The antiarrhythmic compound efsevin directly modulates voltage-dependent anion channel 2 by binding to its inner wall and enhancing mitochondrial CaBritish journal of pharmacology · 2020Article
- A lower affinity to cytosolic proteins reveals VDAC3 isoform-specific role in mitochondrial biology.The Journal of general physiology · 2020Article
- A size-modified poisson-boltzmann ion channel model in a solvent of multiple ionic species: Application to voltage-dependent anion channel.Journal of computational chemistry · 2020Article
- Insights Into the Role of Mitochondrial Ion Channels in Inflammatory Response.Frontiers in physiology · 2020Review
- Structure of voltage-dependent anion channel-tethered bilayer lipid membranes determined using neutron reflectivity.Acta crystallographica. Section D, Structural biology · 2018Article
- Article
- Proteomic profile of human spermatozoa in healthy and asthenozoospermic individuals.Reproductive biology and endocrinology : RB&E · 2018Review
- Ten Years of High Resolution Structural Research on the Voltage Dependent Anion Channel (VDAC)-Recent Developments and Future Directions.Frontiers in physiology · 2018Review
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
The voltage-dependent anion channel (VDAC) is the major pathway mediating the transfer of metabolites and ions across the mitochondrial outer membrane. Two hallmarks of the channel in the open state are high metabolite flux and anion selectivity, while the partially closed state blocks metabolites and is cation selective. Here we report the results from electrostatics calculations carried out on the recently determined high-resolution structure of murine VDAC1 (mVDAC1). Poisson-Boltzmann calculations show that the ion transfer free energy through the channel is favorable for anions, suggesting that mVDAC1 represents the open state. This claim is buttressed by Poisson-Nernst-Planck calculations that predict a high single-channel conductance indicative of the open state and an anion selectivity of 1.75--nearly a twofold selectivity for anions over cations. These calculations were repeated on mutant channels and gave selectivity changes in accord with experimental observations. We were then able to engineer an in silico mutant channel with three point mutations that converted mVDAC1 into a channel with a preference for cations. Finally, we investigated two proposals for how the channel gates between the open and the closed state. Both models involve the movement of the N-terminal helix, but neither motion produced the observed voltage sensitivity, nor did either model result in a cation-selective channel, which is observed experimentally. Thus, we were able to rule out certain models for channel gating, but the true motion has yet to be determined.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.