ArticleScientific reports2016
Yeast V-ATPase Proteolipid Ring Acts as a Large-conductance Transmembrane Protein Pore.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed, 45 citations in OpenAlex.
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- Structural and functional understanding of disease-associated mutations in V-ATPase subunit a1 and other isoforms.Frontiers in molecular neuroscience · 2023Review
- Reversible binding of divalent cations toFrontiers in molecular biosciences · 2023Review
- Mitochondrial ATP synthase c-subunit leak channel triggers cell death upon loss of its FCell death and differentiation · 2022Article
- Current noise of a protein-selective biological nanopore.Proteomics · 2022Article
- Disentangling the recognition complexity of a protein hub using a nanopore.Nature communications · 2022Article
- Oxidative stress protein Oxr1 promotes V-ATPase holoenzyme disassembly in catalytic activity-independent manner.The EMBO journal · 2022Article
- The Plant V-ATPase.Frontiers in plant science · 2022Review
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- Insertion state of modular protein nanopores into a membrane.Biochimica et biophysica acta. Biomembranes · 2021Article
- The HAmerican journal of physiology. Cell physiology · 2021Review
- The Activity of Native Vacuolar Proton-ATPase in an Oscillating Electric Field - Demystifying an Apparent Effect of Music on a Biomolecule.Frontiers in molecular biosciences · 2021Article
- Protein Ligand-Induced Amplification in the 1/Langmuir : the ACS journal of surfaces and colloids · 2020Article
- Identification of the Genetic Requirements for Zinc Tolerance and Toxicity inG3 (Bethesda, Md.) · 2020Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
The vacuolar H(+)-ATPase (V-ATPase) is a rotary motor enzyme that acidifies intracellular organelles and the extracellular milieu in some tissues. Besides its canonical proton-pumping function, V-ATPase's membrane sector, Vo, has been implicated in non-canonical functions including membrane fusion and neurotransmitter release. Here, we report purification and biophysical characterization of yeast V-ATPase c subunit ring (c-ring) using electron microscopy and single-molecule electrophysiology. We find that yeast c-ring forms dimers mediated by the c subunits' cytoplasmic loops. Electrophysiology measurements of the c-ring reconstituted into a planar lipid bilayer revealed a large unitary conductance of ~8.3 nS. Thus, the data support a role of V-ATPase c-ring in membrane fusion and neuronal communication.
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Registered trials
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