ArticleThe Journal of biological chemistry2011
Definition of membrane topology and identification of residues important for transport in subunit a of the vacuolar ATPase.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
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Who cites it
39 citing papers in PubMed, 59 citations in OpenAlex.
- Exploring the Anticancer Potential of Proton Pump Inhibitors by Targeting GRP78 and V-ATPase: Molecular Docking, Molecular Dynamics, PCA, and MM-GBSA Calculations.International journal of molecular sciences · 2025Article
- Tender love and disassembly: How a TLDc domain protein breaks the V-ATPase.BioEssays : news and reviews in molecular, cellular and developmental biology · 2023Article
- Structural and Functional Diversity of Two ATP-Driven Plant Proton Pumps.International journal of molecular sciences · 2023Review
- 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 a subunit isoforms of vacuolar-type proton ATPase exhibit differential distribution in mouse perigastrulation embryos.Scientific reports · 2022Article
- The Plant V-ATPase.Frontiers in plant science · 2022Review
- Vacuolar-type proton ATPase is required for maintenance of apicobasal polarity of embryonic visceral endoderm.Scientific reports · 2021Article
- Regulation and function of V-ATPases in physiology and disease.Biochimica et biophysica acta. Biomembranes · 2020Review
- Structures of a Complete Human V-ATPase Reveal Mechanisms of Its Assembly.Molecular cell · 2020Article
- Cryo-EM and MD infer water-mediated proton transport and autoinhibition mechanisms of VScience advances · 2020Article
- Screening and function discussion of a hereditary renal tubular acidosis family pathogenic gene.Cell death & disease · 2020Article
- A novel potent autophagy inhibitor ECDD-S27 targets vacuolar ATPase and inhibits cancer cell survival.Scientific reports · 2019Article
- Structural comparison of the vacuolar and Golgi V-ATPases fromProceedings of the National Academy of Sciences of the United States of America · 2019Article
- Vacuolar-type ATPase: A proton pump to lysosomal trafficking.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 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
- The 3.5-Å CryoEM Structure of Nanodisc-Reconstituted Yeast Vacuolar ATPase VMolecular cell · 2018Article
- Molecular mechanisms of cutis laxa- and distal renal tubular acidosis-causing mutations in V-ATPaseThe Journal of biological chemistry · 2018Article
- Regulation of V-ATPase Assembly in Nutrient Sensing and Function of V-ATPases in Breast Cancer Metastasis.Frontiers in physiology · 2018Review
- Breaking up and making up: The secret life of the vacuolar HProtein science : a publication of the Protein Society · 2017Review
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Subunit a of the vacuolar H(+)-ATPases plays an important role in proton transport. This membrane-integral 100-kDa subunit is thought to form or contribute to proton-conducting hemichannels that allow protons to gain access to and leave buried carboxyl groups on the proteolipid subunits (c, c', and c″) during proton translocation. We previously demonstrated that subunit a contains a large N-terminal cytoplasmic domain followed by a C-terminal domain containing eight transmembrane (TM) helices. TM7 contains a buried arginine residue (Arg-735) that is essential for proton transport and is located on a helical face that interacts with the proteolipid ring. To further define the topology of the C-terminal domain, the accessibility of 30 unique cysteine residues to the membrane-permeant reagent N-ethylmaleimide and the membrane-impermeant reagent polyethyleneglycol maleimide was determined. The results further define the borders of transmembrane segments in subunit a. To identify additional buried polar and charged residues important in proton transport, 25 sites were individually mutated to hydrophobic amino acids, and the effect on proton transport was determined. These and previous results identify a set of residues important for proton transport located on the cytoplasmic half of TM7 and TM8 and the lumenal half of TM3, TM4, and TM7. Based upon these data, we propose a tentative model in which the cytoplasmic hemichannel is located at the interface of TM7 and TM8 of subunit a and the proteolipid ring, whereas the lumenal hemichannel is located within subunit a at the interface of TM3, TM4, and TM7.
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