ArticleThe Journal of general physiology2019
Helix-strand interaction regulates stability and aggregation of the human mitochondrial membrane protein channel VDAC3.
Article in The Journal of general physiology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 15 citations in OpenAlex.
- Therapeutic Hypothermia Ameliorates Apoptosis and Cerebral Injury by Upregulating HECTD1-mediated Ubiquitination and VDAC3 Degradation in a Rat CPR Model.International journal of medical sciences · 2026Article
- Mitochondrial Transmembrane β-Barrels: Deducing Thermodynamic Regulators of Folding and Stability.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Structural characterization of intra- and intermolecular disulfide bonds in voltage-dependent anion channel 3 (VDAC3) protein from Rattus norvegicus by high-resolution mass spectrometry.Analytical and bioanalytical chemistry · 2025Article
- Monomeric Amyloid Peptide-induced Toxicity in Human Oligodendrocyte Cell Line and Mouse Brain Primary Mixed-glial Cell Cultures: Evidence for a Neuroprotective Effect of Neurosteroid 3α-O-allyl-allopregnanolone.Neurotoxicity research · 2024Article
- Exploiting the intrinsic misfolding propensity of the KRAS oncoprotein.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Engineering a HyperstableJournal of the American Chemical Society · 2022Article
- Evolutionary selection of a 19-stranded mitochondrial β-barrel scaffold bears structural and functional significance.The Journal of biological chemistry · 2020Article
- Evaluation of Peptide/Protein Self-Assembly and Aggregation by Spectroscopic Methods.Molecules (Basel, Switzerland) · 2020Review
- A High Resolution Mass Spectrometry Study Reveals the Potential of Disulfide Formation in Human Mitochondrial Voltage-Dependent Anion Selective Channel Isoforms (hVDACs).International journal of molecular sciences · 2020Article
- Single-residue physicochemical characteristics kinetically partition membrane protein self-assembly and aggregation.The Journal of biological chemistry · 2020Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Voltage-dependent anion channels (VDACs) are β-sheet-rich transmembrane β-barrels that are vital for metabolite transport across the mitochondrial membrane. Under cellular stress, human VDACs hetero-oligomerize and coaggregate with proteins that can form amyloidogenic and neurodegenerative deposits, implicating a role for VDACs in proteotoxicity. However, whether VDACs possess intrinsic interaction sites that can lead to protein aggregation is not known. Here, we couple a systematic thiol replacement strategy with far-UV circular dichroism spectropolarimetry and UV scattering spectroscopy to map aggregation-prone regions of human VDACs, using isoform 3 as our model VDAC. We show that the region comprising strands β7-β9 is highly aggregation prone. Further, we find that an α1-β7-β9 interaction (involving the hVDAC3 N-terminal α1 helix) can lower protein aggregation, whereas perturbations of this interaction promote VDAC aggregation. We also show that hVDAC3 aggregation proceeds via a partially unfolded structure. Our findings allow us to propose a plausible mechanism for the role of human VDACs in forming proteotoxic aggregates in the cell. The key target sites on VDACs-strands β7-β9-may be useful for developing VDAC aggregation inhibitors.
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