Evidence map›Paper›PMID 26410601›Full record

ReviewTrends in biochemical sciences2015

Recent Insights into the Structure, Regulation, and Function of the V-ATPases.

Kristina Cotter, Laura Stransky, Christina McGuire, Michael Forgac

Abstract readReview
In one paragraph

Review in Trends in biochemical sciences, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 189 papers.

0numbers the graph read from it
0cells of the map it votes in
189citing 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

189 citing papers in PubMed.

  1. Article
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  7. Review
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  17. Article
  18. Autophagy · 2025
    Article
  19. Pharmaceuticals (Basel, Switzerland) · 2025
    Article
  20. Article

129 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

4 authors.

Kristina CotterProgram in Cellular and Molecular Physiology, Sackler School of Graduate Biomedical Sciences, Tufts University School of Medicine, 136 Harrison Avenue, Boston, MA 02111, USA.
Laura StranskyProgram in Cellular and Molecular Physiology, Sackler School of Graduate Biomedical Sciences, Tufts University School of Medicine, 136 Harrison Avenue, Boston, MA 02111, USA.
Christina McGuireProgram in Biochemistry, Sackler School of Graduate Biomedical Sciences, Tufts University School of Medicine, 136 Harrison Avenue, Boston, MA 02111, USA.
Michael ForgacProgram in Cellular and Molecular Physiology, Sackler School of Graduate Biomedical Sciences, Tufts University School of Medicine, 136 Harrison Avenue, Boston, MA 02111, USA; Program in Biochemistry, Sackler School of Graduate Biomedical Sciences, Tufts University School of Medicine, 136 Harrison Avenue, Boston, MA 02111, USA; Department of Developmental, Molecular, and Chemical Biology, Tufts University School of Medicine, 136 Harrison Avenue, Boston, MA 02111, USA. Electronic address: michael.forgac@tufts.edu.

Funding

STRUCTURE, MECHANISM AND REGULATION OF THE V-ATPASESR01GM034478 · NIGMS · TUFTS UNIVERSITY BOSTON · PI FORGAC, MICHAEL D · 1985 to 2015
$1.9M
Elucidating the mechanism of mTORC1 activation by amino acidsF31CA189321 · NCI · TUFTS UNIVERSITY BOSTON · PI STRANSKY, LAURA ALICE · 2015 to 2016
$75k
Elucidating the Role of Plasma Membrane V-ATPases in Breast Cancer MetastasisF31CA192500 · NCI · TUFTS UNIVERSITY BOSTON · PI COTTER, KRISTINA · 2015 to 2015
$31k
NCI NIH HHS F31CA189321NCI NIH HHS F31CA192500NIGMS NIH HHS R01 GM034478NIGMS NIH HHS R01GM34478
6 · The paper itself

Abstract

The vacuolar (H(+))-ATPases (V-ATPases) are ATP-dependent proton pumps that acidify intracellular compartments and are also present at the plasma membrane. They function in such processes as membrane traffic, protein degradation, virus and toxin entry, bone resorption, pH homeostasis, and tumor cell invasion. V-ATPases are large multisubunit complexes, composed of an ATP-hydrolytic domain (V1) and a proton translocation domain (V0), and operate by a rotary mechanism. This review focuses on recent insights into their structure and mechanism, the mechanisms that regulate V-ATPase activity (particularly regulated assembly and trafficking), and the role of V-ATPases in processes such as cell signaling and cancer. These developments have highlighted the potential of V-ATPases as a therapeutic target in a variety of human diseases.

Indexed as

AnimalsCell MembraneHumansProton-Translocating ATPasesStructure-Activity RelationshipProton-Translocating ATPasesacidificationcancercell signalingmembrane trafficproton transportV-ATPase

Identifiers

PMID26410601
PMCPMC4589219

What OpenQuestion holds

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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.