Evidence map›Paper›PMID 27335445›Full record

ReviewPhysiological reviews2016

The Function of V-ATPases in Cancer.

Laura Stransky, Kristina Cotter, Michael Forgac

Open access · bronzeAbstract readReview
In one paragraph

Review in Physiological reviews, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 175 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
175citing papers in PubMed, 1 pooled it
12.9field-weighted citation impact, top 1% 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

175 citing papers in PubMed, 1 synthesis or guideline pooled it, 283 citations in OpenAlex.

  1. Pooled it
  2. Trial
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. NaFrontiers in chemistry · 2026
    Article
  11. Review
  12. Review
  13. Article
  14. ATG16L1 controls mammalian vacuolar proton ATPase.The Journal of cell biology · 2025
    Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

115 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

3 authors at 1 institution in 1 country.

Laura StranskyDepartment of Developmental, Molecular and Chemical Biology, Tufts University School of Medicine, and Program in Cellular and Molecular Physiology, Program in Biochemistry, and Program in Cell, Molecular and Developmental Biology, Sackler School of Graduate Biomedical Sciences, Tufts University, Boston, Massachusetts.
Kristina CotterDepartment of Developmental, Molecular and Chemical Biology, Tufts University School of Medicine, and Program in Cellular and Molecular Physiology, Program in Biochemistry, and Program in Cell, Molecular and Developmental Biology, Sackler School of Graduate Biomedical Sciences, Tufts University, Boston, Massachusetts.
Michael ForgacDepartment of Developmental, Molecular and Chemical Biology, Tufts University School of Medicine, and Program in Cellular and Molecular Physiology, Program in Biochemistry, and Program in Cell, Molecular and Developmental Biology, Sackler School of Graduate Biomedical Sciences, Tufts University, Boston, Massachusetts.
Tufts University · US

Funding

Structure, Mechanism and Regulation of the V-ATPasesR37GM034478 · NIGMS · TUFTS UNIVERSITY BOSTON · PI FORGAC, MICHAEL D · 2001 to 2010
$5.0M
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 F31 CA189321NCI NIH HHS F31 CA192500NIGMS NIH HHS R01 GM034478NIGMS NIH HHS R37 GM034478
6 · The paper itself

Abstract

The vacuolar ATPases (V-ATPases) are a family of proton pumps that couple ATP hydrolysis to proton transport into intracellular compartments and across the plasma membrane. They function in a wide array of normal cellular processes, including membrane traffic, protein processing and degradation, and the coupled transport of small molecules, as well as such physiological processes as urinary acidification and bone resorption. The V-ATPases have also been implicated in a number of disease processes, including viral infection, renal disease, and bone resorption defects. This review is focused on the growing evidence for the important role of V-ATPases in cancer. This includes functions in cellular signaling (particularly Wnt, Notch, and mTOR signaling), cancer cell survival in the highly acidic environment of tumors, aiding the development of drug resistance, as well as crucial roles in tumor cell invasion, migration, and metastasis. Of greatest excitement is evidence that at least some tumors express isoforms of V-ATPase subunits whose disruption is not lethal, leading to the possibility of developing anti-cancer therapeutics that selectively target V-ATPases that function in cancer cells.

Indexed as

AnimalsCell DeathCell MembraneHumansNeoplasm MetastasisNeoplasmsProtein SubunitsSignal TransductionVacuolar Proton-Translocating ATPasesProtein SubunitsVacuolar Proton-Translocating ATPases

Identifiers

PMID27335445
PMCPMC4982037
OpenAlexW2465929875

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.