Evidence map›Paper›PMID 24286827›Full record

ArticleDevelopmental cell2013

Homotypic vacuole fusion in yeast requires organelle acidification and not the V-ATPase membrane domain.

Emily M Coonrod, Laurie A Graham, Lindsay N Carpp, Tom M Carr, Laura Stirrat, Katherine Bowers, Nia J Bryant, Tom H Stevens

Abstract read
In one paragraph

Article in Developmental cell, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
–field-weighted citation impact
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

38 citing papers in PubMed.

  1. Article
  2. Article
  3. ModelingJournal of cellular immunology · 2025
    Article
  4. Article
  5. Article
  6. Article
  7. The role ofProceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  8. Article
  9. Review
  10. The Plant V-ATPase.Frontiers in plant science · 2022
    Review
  11. Article
  12. Article
  13. Lysosomal size matters.Traffic (Copenhagen, Denmark) · 2020
    Review
  14. Article
  15. Article
  16. Article
  17. PI(3,5)PMolecular biology of the cell · 2018
    Article
  18. Article
  19. The NaMolecular biology of the cell · 2018
    Article
  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

8 authors.

Emily M CoonrodInstitute of Molecular Biology, University of Oregon, Eugene, OR 97403, USA.
Laurie A Graham
Lindsay N Carpp
Tom M Carr
Laura Stirrat
Katherine Bowers
Nia J Bryant
Tom H Stevens

Funding

SORTING AND TRANSPORT OF YEAST MEMBRANE PROTEINSR01GM038006 · NIGMS · UNIVERSITY OF OREGON · PI STEVENS, TOM HALL · 1987 to 2016
$4.9M
Cell Biological Study of Eukaryotic Organelle AssemblyR37GM032448 · NIGMS · UNIVERSITY OF OREGON · PI STEVENS, TOM HALL · 2003 to 2012
$3.6M
CELL BIOLOGICAL STUDY OF EUKARYOTIC ORGANELLE ASSEMBLYR01GM032448 · NIGMS · UNIVERSITY OF OREGON · PI STEVENS, TOM HALL · 1985 to 2002
$970k
The role of the endocytic pathway in glucose sensing in S. cerevisiaeF32GM083572 · NIGMS · UNIVERSITY OF OREGON · PI COONROD, EMILY · 2008 to 2009
$97k
NIGMS NIH HHS F32 GM083572NIGMS NIH HHS GM32448NIGMS NIH HHS GM38006NIGMS NIH HHS GM835722NIGMS NIH HHS R01 GM032448NIGMS NIH HHS R01 GM038006NIGMS NIH HHS R37 GM032448
6 · The paper itself

Abstract

Studies of homotypic vacuole-vacuole fusion in the yeast Saccharomyces cerevisiae have been instrumental in determining the cellular machinery required for eukaryotic membrane fusion and have implicated the vacuolar H(+)-ATPase (V-ATPase). The V-ATPase is a multisubunit, rotary proton pump whose precise role in homotypic fusion is controversial. Models formulated from in vitro studies suggest that it is the proteolipid proton-translocating pore of the V-ATPase that functions in fusion, with further studies in worms, flies, zebrafish, and mice appearing to support this model. We present two in vivo assays and use a mutant V-ATPase subunit to establish that it is the H(+)-translocation/vacuole acidification function, rather than the physical presence of the V-ATPase, that promotes homotypic vacuole fusion in yeast. Furthermore, we show that acidification of the yeast vacuole in the absence of the V-ATPase rescues vacuole-fusion defects. Our results clarify the in vivo requirements of acidification for membrane fusion.

Indexed as

AnimalsArabidopsisArabidopsis ProteinsFluorescenceHydrogen-Ion ConcentrationInorganic PyrophosphataseMembrane FusionMiceMutationProton PumpsSaccharomyces cerevisiaeVacuolar Proton-Translocating ATPasesVacuolesArabidopsis ProteinsAVP1 protein, ArabidopsisInorganic PyrophosphataseProton PumpsVacuolar Proton-Translocating ATPases

Identifiers

PMID24286827
PMCPMC4086684

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Registered trials

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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.