Evidence map›Paper›PMID 27295975›Full record

ArticleThe EMBO journal2016

Crystal structure of yeast V1-ATPase in the autoinhibited state.

Rebecca A Oot, Patricia M Kane, Edward A Berry, Stephan Wilkens

Abstract read
In one paragraph

Article in The EMBO journal, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
3.3field-weighted citation impact, top 8% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

37 citing papers in PubMed, 51 citations in OpenAlex.

  1. Article
  2. ATG16L1 controls mammalian vacuolar proton ATPase.The Journal of cell biology · 2025
    Article
  3. Review
  4. Interaction of yeast V-ATPase with TLDc protein Rtc5p.bioRxiv : the preprint server for biology · 2025
    Article
  5. Article
  6. Structure of yeast RAVE bound to a partial VProceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  7. Article
  8. Article
  9. Article
  10. Eukaryotic yeast VFrontiers in molecular biosciences · 2024
    Article
  11. Tender love and disassembly: How a TLDc domain protein breaks the V-ATPase.BioEssays : news and reviews in molecular, cellular and developmental biology · 2023
    Article
  12. Structural and Functional Diversity of Two ATP-Driven Plant Proton Pumps.International journal of molecular sciences · 2023
    Review
  13. Review
  14. Review
  15. Article
  16. Coordinated conformational changes in the VNature structural & molecular biology · 2022
    Article
  17. Article
  18. FFrontiers in microbiology · 2022
    Review
  19. The V-ATPaseInternational journal of molecular sciences · 2021
    Review
  20. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 1 institution in 1 country.

Rebecca A OotDepartment of Biochemistry and Molecular Biology, SUNY Upstate Medical University, Syracuse, NY, USA.
Patricia M KaneDepartment of Biochemistry and Molecular Biology, SUNY Upstate Medical University, Syracuse, NY, USA.
Edward A BerryDepartment of Biochemistry and Molecular Biology, SUNY Upstate Medical University, Syracuse, NY, USA.
Stephan WilkensDepartment of Biochemistry and Molecular Biology, SUNY Upstate Medical University, Syracuse, NY, USA wilkenss@upstate.edu.ORCID 0000-0002-2721-2789
SUNY Upstate Medical University · US

Funding

ZINC FINGER-DNA COMPLEXP41RR001646 · NCRR · CORNELL UNIVERSITY ITHACA · PI ROSE, ROBERT C · 1985 to 2011
$23.8M
Overall (pp. 40-62)P41GM103485 · NIGMS · CORNELL UNIVERSITY · PI CERIONE, RICHARD A. · 2012 to 2018
$15.5M
STRUCTURE OF THE VACUOLAR ATPASE BY ELECTRON MICROSCOPYR01GM058600 · NIGMS · UPSTATE MEDICAL UNIVERSITY · PI WILKENS, STEPHAN · 1999 to 2020
$4.8M
NCRR NIH HHS P41 RR001646NIGMS NIH HHS P41 GM103485NIGMS NIH HHS R01 GM058600
6 · The paper itself

Abstract

Vacuolar ATPases (V-ATPases) are essential proton pumps that acidify the lumen of subcellular organelles in all eukaryotic cells and the extracellular space in some tissues. V-ATPase activity is regulated by a unique mechanism referred to as reversible disassembly, wherein the soluble catalytic sector, V1, is released from the membrane and its MgATPase activity silenced. The crystal structure of yeast V1 presented here shows that activity silencing involves a large conformational change of subunit H, with its C-terminal domain rotating ~150° from a position near the membrane in holo V-ATPase to a position at the bottom of V1 near an open catalytic site. Together with biochemical data, the structure supports a mechanistic model wherein subunit H inhibits ATPase activity by stabilizing an open catalytic site that results in tight binding of inhibitory ADP at another site.

Indexed as

Adenosine DiphosphateCatalytic DomainCrystallography, X-RayModels, BiologicalModels, MolecularProtein ConformationProtein SubunitsSaccharomyces cerevisiaeVacuolar Proton-Translocating ATPasesAdenosine DiphosphateProtein SubunitsVacuolar Proton-Translocating ATPasesautoinhibitionreversible disassemblyV1‐ATPasevacuolar ATPaseX‐ray crystallography

Identifiers

PMID27295975
PMCPMC4969575
OpenAlexW2433610117

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.