Evidence map›Paper›PMID 24706019›Full record

ReviewEukaryotic cell2014

Saccharomyces cerevisiae vacuolar H+-ATPase regulation by disassembly and reassembly: one structure and multiple signals.

Karlett J Parra, Chun-Yuan Chan, Jun Chen

Abstract readReview
In one paragraph

Review in Eukaryotic cell, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing 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

29 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Review
  6. Eukaryotic yeast VFrontiers in molecular biosciences · 2024
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Review
  13. Article
  14. Article
  15. Article
  16. Interaction between the yeast RAVE complex and Vph1-containing VThe Journal of biological chemistry · 2020
    Article
  17. Review
  18. Article
  19. Functional reconstitution of vacuolar HThe Journal of biological chemistry · 2019
    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

3 authors.

Karlett J ParraDepartment of Biochemistry and Molecular Biology of the School of Medicine, University of New Mexico Health Sciences Center, Albuquerque, New Mexico, USA kjparra@salud.unm.edu.
Chun-Yuan ChanDepartment of Biochemistry and Molecular Biology of the School of Medicine, University of New Mexico Health Sciences Center, Albuquerque, New Mexico, USA.
Jun ChenDepartment of Biochemistry and Molecular Biology of the School of Medicine, University of New Mexico Health Sciences Center, Albuquerque, New Mexico, USA.

Funding

V-ATPase H+ PUMP REGULATION IN FUEL ENERGY SELECTIONR01GM086495 · NIGMS · UNIVERSITY OF NEW MEXICO HEALTH SCIS CTR · PI PARRA, KARLETT J · 2009 to 2013
$1.7M
NIGMS NIH HHS R01 GM086495NIGMS NIH HHS R01GM086495
6 · The paper itself

Abstract

Vacuolar H(+)-ATPases (V-ATPases) are highly conserved ATP-driven proton pumps responsible for acidification of intracellular compartments. V-ATPase proton transport energizes secondary transport systems and is essential for lysosomal/vacuolar and endosomal functions. These dynamic molecular motors are composed of multiple subunits regulated in part by reversible disassembly, which reversibly inactivates them. Reversible disassembly is intertwined with glycolysis, the RAS/cyclic AMP (cAMP)/protein kinase A (PKA) pathway, and phosphoinositides, but the mechanisms involved are elusive. The atomic- and pseudo-atomic-resolution structures of the V-ATPases are shedding light on the molecular dynamics that regulate V-ATPase assembly. Although all eukaryotic V-ATPases may be built with an inherent capacity to reversibly disassemble, not all do so. V-ATPase subunit isoforms and their interactions with membrane lipids and a V-ATPase-exclusive chaperone influence V-ATPase assembly. This minireview reports on the mechanisms governing reversible disassembly in the yeast Saccharomyces cerevisiae, keeping in perspective our present understanding of the V-ATPase architecture and its alignment with the cellular processes and signals involved.

Indexed as

Protein MultimerizationSignal TransductionProtein Structure, TertiarySaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsVacuolar Proton-Translocating ATPasesSaccharomyces cerevisiae ProteinsVacuolar Proton-Translocating ATPases

Identifiers

PMID24706019
PMCPMC4054264

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.