Evidence map›Paper›PMID 33633298›Full record

ArticleScientific reports2021

Role of the V1G1 subunit of V-ATPase in breast cancer cell migration.

Maria De Luca, Roberta Romano, Cecilia Bucci

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.6field-weighted citation impact, top 16% 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

17 citing papers in PubMed, 27 citations in OpenAlex.

  1. Article
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  4. V-ATPase in glioma stem cells: a novel metabolic vulnerability.Journal of experimental & clinical cancer research : CR · 2025
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  15. A perspective on the role of autophagy in cancer.Biochimica et biophysica acta. Molecular basis of disease · 2021
    Review
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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.

Maria De LucaDepartment of Biological and Environmental Sciences and Technologies, University of Salento, Via Provinciale Lecce-Monteroni n. 165, 73100, Lecce, Italy. maria.deluca@unisalento.it.
Roberta RomanoDepartment of Biological and Environmental Sciences and Technologies, University of Salento, Via Provinciale Lecce-Monteroni n. 165, 73100, Lecce, Italy.
Cecilia BucciDepartment of Biological and Environmental Sciences and Technologies, University of Salento, Via Provinciale Lecce-Monteroni n. 165, 73100, Lecce, Italy. cecilia.bucci@unisalento.it.
University of Salento · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

V-ATPase is a large multi-subunit complex that regulates acidity of intracellular compartments and of extracellular environment. V-ATPase consists of several subunits that drive specific regulatory mechanisms. The V1G1 subunit, a component of the peripheral stalk of the pump, controls localization and activation of the pump on late endosomes and lysosomes by interacting with RILP and RAB7. Deregulation of some subunits of the pump has been related to tumor invasion and metastasis formation in breast cancer. We observed a decrease of V1G1 and RAB7 in highly invasive breast cancer cells, suggesting a key role of these proteins in controlling cancer progression. Moreover, in MDA-MB-231 cells, modulation of V1G1 affected cell migration and matrix metalloproteinase activation in vitro, processes important for tumor formation and dissemination. In these cells, characterized by high expression of EGFR, we demonstrated that V1G1 modulates EGFR stability and the EGFR downstream signaling pathways that control several factors required for cell motility, among which RAC1 and cofilin. In addition, we showed a key role of V1G1 in the biogenesis of endosomes and lysosomes. Altogether, our data describe a new molecular mechanism, controlled by V1G1, required for cell motility and that promotes breast cancer tumorigenesis.

Indexed as

Cell MovementBreast NeoplasmsCell Line, TumorFemaleHumansLysosomesMicroscopy, FluorescenceNeoplasm Invasivenessrab7 GTP-Binding Proteinsrac1 GTP-Binding ProteinReal-Time Polymerase Chain ReactionVacuolar Proton-Translocating ATPasesATP6V1G1 protein, humanrab7 GTP-Binding Proteinsrab7 GTP-binding proteins, humanrac1 GTP-Binding ProteinRAC1 protein, humanVacuolar Proton-Translocating ATPases

Identifiers

PMID33633298
PMCPMC7907067
OpenAlexW3131568512

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.