Evidence map›Paper›PMID 31189779›Full record

ReviewProceedings of the Japan Academy. Series B, Physical and biological sciences2019

Vacuolar-type ATPase: A proton pump to lysosomal trafficking.

Masamitsu Futai, Ge-Hong Sun-Wada, Yoh Wada, Naomi Matsumoto, Mayumi Nakanishi-Matsui

Open access · diamondAbstract readReview
In one paragraph

Review in Proceedings of the Japan Academy. Series B, Physical and biological sciences, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 69 papers.

0numbers the graph read from it
0cells of the map it votes in
69citing papers in PubMed
4.3field-weighted citation impact, top 5% 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

69 citing papers in PubMed, 110 citations in OpenAlex.

  1. Review
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  6. Review
  7. Review
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  10. Article
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  13. Article
  14. Review
  15. Interaction of yeast V-ATPase with TLDc protein Rtc5p.bioRxiv : the preprint server for biology · 2025
    Article
  16. Autophagy · 2025
    Article
  17. Article
  18. Article
  19. Article
  20. Article

9 more citing papers are in PubMed but not listed here.

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

5 authors at 3 institutions in 1 country.

Masamitsu FutaiDepartment of Biochemistry, Faculty of Pharmaceutical Sciences, Iwate Medical University.
Ge-Hong Sun-WadaDepartment of Biochemistry, Faculty of Pharmaceutical Sciences, Doshisha Women's College.
Yoh WadaDepartment of Biological Sciences, Institute of Scientific and Industrial Research, Osaka University.
Naomi MatsumotoDepartment of Biochemistry, Faculty of Pharmaceutical Sciences, Iwate Medical University.
Mayumi Nakanishi-MatsuiDepartment of Biochemistry, Faculty of Pharmaceutical Sciences, Iwate Medical University.
Iwate Medical University · JPOsaka University · JPDoshisha Women's College of Liberal Arts · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Vacuolar-type ATPase (V-ATPase), initially identified in yeast and plant vacuoles, pumps protons into the lumen of organelles coupled with ATP hydrolysis. The mammalian counterpart is found ubiquitously in endomembrane organelles and the plasma membrane of specialized cells such as osteoclasts. V-ATPase is also present in unique organelles such as insulin secretory granules, neural synaptic vesicles, and acrosomes of spermatozoa. Consistent with its diverse physiological roles and unique localization, the seven subunits of V-ATPase have 2-4 isoforms that are organelle- or cell-specific. Subunits of the enzyme function in trafficking organelles and vesicles by interacting with small molecule GTPases. During osteoclast differentiation, one of the four isoforms of subunit a, a3, is indispensable for secretory lysosome trafficking to the plasma membrane. Diseases such as osteopetrosis, renal acidosis, and hearing loss are related to V-ATPase isoforms. In addition to its role as an enzyme, V-ATPase has versatile physiological roles in eukaryotic cells.

Indexed as

AnimalsBiological TransportCell MembraneHumansLysosomesOsteoclastsVacuolar Proton-Translocating ATPasesVacuolar Proton-Translocating ATPaseslysosomeosteoclastplasma membranesecretionsubunit isoformV-ATPase

Identifiers

PMID31189779
PMCPMC6751294
OpenAlexW2951796864

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.