Evidence map›Paper›PMID 26906430›Full record

ReviewBiochimica et biophysica acta2016

Regulation of V-ATPase assembly and function of V-ATPases in tumor cell invasiveness.

Christina McGuire, Kristina Cotter, Laura Stransky, Michael Forgac

Abstract readReview
In one paragraph

Review in Biochimica et biophysica acta, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
3.8field-weighted citation impact, top 7% 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

43 citing papers in PubMed, 69 citations in OpenAlex.

  1. Ubiquitination-Driven Reprogramming of Proteostasis in Metastasis.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Review
  2. Article
  3. Article
  4. Review
  5. Article
  6. Review
  7. V-ATPase in cancer: mechanistic insights and therapeutic potentials.Cell communication and signaling : CCS · 2024
    Review
  8. Article
  9. Review
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Inducing indigestion in malaria parasites: Genetic manipulations of a proton pump.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  16. Regulation of mTORC1 by the Rag GTPases.Biochemical Society transactions · 2023
    Review
  17. Article
  18. Article
  19. Review
  20. Article
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 at 1 institution in 1 country.

Christina McGuireDepartment of Developmental, Molecular and Chemical Biology, Tufts University School of Medicine, 136 Harrison Ave., Boston, MA 02111, United States.
Kristina CotterDepartment of Developmental, Molecular and Chemical Biology, Tufts University School of Medicine, 136 Harrison Ave., Boston, MA 02111, United States.
Laura StranskyDepartment of Developmental, Molecular and Chemical Biology, Tufts University School of Medicine, 136 Harrison Ave., Boston, MA 02111, United States.
Michael ForgacDepartment of Developmental, Molecular and Chemical Biology, Tufts University School of Medicine, 136 Harrison Ave., Boston, MA 02111, United States.
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 CA189321NCI NIH HHS CA192500NCI NIH HHS F31 CA189321NCI NIH HHS F31 CA192500NIGMS NIH HHS GM034478NIGMS NIH HHS R01 GM034478NIGMS NIH HHS R37 GM034478
6 · The paper itself

Abstract

V-ATPases are ATP-driven proton pumps that function within both intracellular compartments and the plasma membrane in a wide array of normal physiological and pathophysiological processes. V-ATPases are composed of a peripheral V(1) domain that hydrolyzes ATP and an integral V(0) domain that transports protons. Regulated assembly of the V-ATPase represents an important mechanism of regulating V-ATPase activity in response to a number of environmental cues. Our laboratory has demonstrated that glucose-dependent assembly of the V-ATPase complex in yeast is controlled by the Ras/cAMP/PKA pathway. By contrast, increased assembly of the V-ATPase during dendritic cell maturation involves the PI-3 kinase and mTORC1 pathways. Recently, we have shown that amino acids regulate V-ATPase assembly in mammalian cells, possibly as a means to maintain adequate levels of amino acids upon nutrient starvation. V-ATPases have also been implicated in cancer cell survival and invasion. V-ATPases are targeted to different cellular membranes by isoforms of subunit a, with a3 targeting V-ATPases to the plasma membrane of osteoclasts. We have shown that highly invasive human breast cancer cell lines express higher levels of the a3 isoform than poorly invasive lines and that knockdown of a3 reduces both expression of V-ATPases at the plasma membrane and in vitro invasion of breast tumor cells. Moreover, overexpression of a3 in a non-invasive breast epithelial line increases both plasma membrane V-ATPases and in vitro invasion. Finally, specific ablation of plasma membrane V-ATPases in highly invasive human breast cancer cells using either an antibody or small molecule approach inhibits both in vitro invasion and migration. These results suggest that plasma membrane and a3-containing V-ATPases represent a novel and important target in the development of therapeutics to limit breast cancer metastasis. This article is part of a Special Issue entitled 'EBEC 2016: 19th European Bioenergetics Conference, Riva del Garda, Italy, July 2-6, 2016', edited by Prof. Paolo Bernardi.

Indexed as

Gene Expression Regulation, NeoplasticCell Line, TumorCell MovementCyclic AMPCyclic AMP-Dependent Protein KinasesEpithelial CellsFemaleHumansMammary Glands, HumanMechanistic Target of Rapamycin Complex 1Multiprotein ComplexesNeoplasm InvasivenessProtein Subunitsras ProteinsSaccharomyces cerevisiaeSignal TransductionCyclic AMPCyclic AMP-Dependent Protein KinasesMechanistic Target of Rapamycin Complex 1Multiprotein ComplexesProtein Subunitsras ProteinsTOR Serine-Threonine KinasesVacuolar Proton-Translocating ATPases

Identifiers

PMID26906430
PMCPMC4922897
OpenAlexW2283686323

What OpenQuestion holds

Textmetadata
LicenceTDM
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.