ArticleMolecular and cellular biology1998
Reversible association between the V1 and V0 domains of yeast vacuolar H+-ATPase is an unconventional glucose-induced effect.
Article in Molecular and cellular biology, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 108 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
108 citing papers in PubMed, 212 citations in OpenAlex.
- AP-3 and the V-ATPase modulate CTP synthase assembly through spatial association at the yeast vacuole.Molecular biology of the cell · 2026Article
- AP-3 and the V-ATPase Modulate CTP Synthase Assembly Through Spatial Association at the Yeast Vacuole.bioRxiv : the preprint server for biology · 2026Article
- A heterotrimeric protein complex assembles the metazoan V-ATPase upon dissipation of proton gradients.Nature structural & molecular biology · 2025Article
- V-ATPase and Lysosomal Energy Sensing in Periodontitis and Medicine-Related Osteonecrosis of the Jaw.Biomolecules · 2025Review
- Interaction of yeast V-ATPase with TLDc protein Rtc5p.bioRxiv : the preprint server for biology · 2025Article
- V-ATPase Disassembly at the Yeast Lysosome-Like Vacuole Is a Phenotypic Driver of Lysosome Dysfunction in Replicative Aging.Aging cell · 2025Article
- Eeukaryotic-like Sppsk1 from Vibrio splendidus AJ01 mediates phagosome escape via inhibiting phagosome acidification and maturation.Cellular and molecular life sciences : CMLS · 2025Article
- Monoclonal nanobodies alter the activity and assembly of the yeast vacuolar HbioRxiv : the preprint server for biology · 2025Article
- PI(3,5)P2 asymmetry during mitosis is essential for asymmetric vacuolar inheritance.The Journal of cell biology · 2025Article
- V-ATPase Disassembly at the Yeast Lysosome-Like Vacuole Is a Phenotypic Driver of Lysosome Dysfunction in Replicative Aging.bioRxiv : the preprint server for biology · 2024Article
- Yeast TLDc domain proteins regulate assembly state and subcellular localization of the V-ATPase.The EMBO journal · 2024Article
- Reversible assembly and disassembly of V-ATPase during the lysosome regeneration cycle.Molecular biology of the cell · 2024Article
- Molecular mechanism of Oxr1p mediated disassembly of yeast V-ATPase.EMBO reports · 2024Article
- Eukaryotic yeast VFrontiers in molecular biosciences · 2024Article
- Impaired Autophagic Flux in Glucose-Deprived Cells: An Outcome of Lysosomal Acidification Failure Exacerbated by Mitophagy Dysfunction.Molecules and cells · 2023Review
- Tender love and disassembly: How a TLDc domain protein breaks the V-ATPase.BioEssays : news and reviews in molecular, cellular and developmental biology · 2023Article
- Chimeric a-subunit isoforms generate functional yeast V-ATPases with altered regulatory properties in vitro and in vivo.Molecular biology of the cell · 2023Article
- Structural and functional understanding of disease-associated mutations in V-ATPase subunit a1 and other isoforms.Frontiers in molecular neuroscience · 2023Review
- Effects of pH alterations on stress- and aging-induced protein phase separation.Cellular and molecular life sciences : CMLS · 2022Review
- Review
48 more citing papers are in PubMed but not listed here.
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The yeast vacuolar H+-ATPase (V-ATPase) is a multisubunit complex responsible for organelle acidification. The enzyme is structurally organized into two major domains: a peripheral domain (V1), containing the ATP binding sites, and an integral membrane domain (V0), forming the proton pore. Dissociation of the V1 and V0 domains inhibits ATP-driven proton pumping, and extracellular glucose concentrations regulate V-ATPase activity in vivo by regulating the extent of association between the V1 and V0 domains. To examine the mechanism of this response, we quantitated the extent of V-ATPase assembly in a variety of mutants with known effects on other glucose-responsive processes. Glucose effects on V-ATPase assembly did not involve the Ras-cyclic AMP pathway, Snf1p, protein kinase C, or the general stress response protein Rts1p. Accumulation of glucose 6-phosphate was insufficient to maintain or induce assembly of the V-ATPase, suggesting that further glucose metabolism is required. A transient decrease in ATP concentration with glucose deprivation occurs quickly enough to help trigger disassembly of the V-ATPase, but increases in cellular ATP concentrations with glucose readdition cannot account for reassembly. Disassembly was inhibited in two mutant enzymes lacking ATPase and proton pumping activities or in the presence of the specific V-ATPase inhibitor, concanamycin A. We propose that glucose effects on V-ATPase assembly occur by a novel mechanism that requires glucose metabolism beyond formation of glucose 6-phosphate and generates a signal that can be sensed efficiently only by a catalytically competent V-ATPase.
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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.