ArticleProceedings of the National Academy of Sciences of the United States of America2001
Arg-735 of the 100-kDa subunit a of the yeast V-ATPase is essential for proton translocation.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 66 papers.
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Who cites it
66 citing papers in PubMed, 145 citations in OpenAlex.
- Gastric Proton Pumpopathy Associated with Protein Sorting Machinery: A Narrative Review.Clinical and experimental gastroenterology · 2026Review
- Targeting vacuolar ATPase in tobacco whitefly,Journal of biosciences · 2025Review
- ModelingJournal of cellular immunology · 2025Article
- The different roles of V-ATPase a subunits in phagocytosis/endocytosis and autophagy.Autophagy · 2024Article
- Eukaryotic yeast VFrontiers in molecular biosciences · 2024Article
- Structural and functional understanding of disease-associated mutations in V-ATPase subunit a1 and other isoforms.Frontiers in molecular neuroscience · 2023Review
- The V-ATPases in cancer and cell death.Cancer gene therapy · 2022Review
- The V-ATPaseInternational journal of molecular sciences · 2021Review
- ATP6V0A1 encoding the a1-subunit of the V0 domain of vacuolar HNature communications · 2021Article
- Intracellular pH regulation: characterization and functional investigation of HBMC molecular and cell biology · 2021Article
- Variants inBrain communications · 2021Article
- Regulation and function of V-ATPases in physiology and disease.Biochimica et biophysica acta. Biomembranes · 2020Review
- Comparative Ubiquitome Analysis under Heat Stress Reveals Diverse Functions of Ubiquitination inInternational journal of molecular sciences · 2020Article
- Screening and function discussion of a hereditary renal tubular acidosis family pathogenic gene.Cell death & disease · 2020Article
- Cryo-EM studies of the rotary HBiophysics and physicobiology · 2019Review
- A cation-π interaction in a transmembrane helix of vacuolar ATPase retains the proton-transporting arginine in a hydrophobic environment.The Journal of biological chemistry · 2018Article
- PI(3,5)PMolecular biology of the cell · 2018Article
- The 3.5-Å CryoEM Structure of Nanodisc-Reconstituted Yeast Vacuolar ATPase VMolecular cell · 2018Article
- V-ATPases and osteoclasts: ambiguous future of V-ATPases inhibitors in osteoporosis.Theranostics · 2018Review
- Regulation of V-ATPase Assembly in Nutrient Sensing and Function of V-ATPases in Breast Cancer Metastasis.Frontiers in physiology · 2018Review
6 more citing papers are in PubMed but not listed here.
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
The vacuolar (H(+))-ATPases (V-ATPases) are ATP-dependent proton pumps that acidify intracellular compartments and pump protons across specialized plasma membranes. Proton translocation occurs through the integral V(0) domain, which contains five different subunits (a, d, c, c', and c"). Proton transport is critically dependent on buried acidic residues present in three different proteolipid subunits (c, c', and c"). Mutations in the 100-kDa subunit a have also influenced activity, but none of these residues has proven to be required absolutely for proton transport. On the basis of previous observations on the F-ATPases, we have investigated the role of two highly conserved arginine residues present in the last two putative transmembrane segments of the yeast V-ATPase a subunit (Vph1p). Substitution of Asn, Glu, or Gln for Arg-735 in TM8 gives a V-ATPase that is fully assembled but is totally devoid of proton transport and ATPase activity. Replacement of Arg-735 by Lys gives a V-ATPase that, although completely inactive for proton transport, retains 24% of wild-type ATPase activity, suggesting a partial uncoupling of proton transport and ATP hydrolysis in this mutant. By contrast, nonconservative mutations of Arg-799 in TM9 lead to both defective assembly of the V-ATPase complex and decreases in activity of the assembled V-ATPase. These results suggest that Arg-735 is absolutely required for proton transport by the V-ATPases and is discussed in the context of a revised model of the topology of the 100-kDa subunit a.
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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.