Evidence map›Paper›PMID 32398681›Full record

ArticleCell death & disease2020

Galectin-3 modulates epithelial cell adaptation to stress at the ER-mitochondria interface.

Lucie Coppin, Arnaud Jannin, Emilie Ait Yahya, Caroline Thuillier, Céline Villenet, Meryem Tardivel, Antonino Bongiovanni, Cécile Gaston, Simon de Beco, Nicolas Barois and 10 more

Open access · goldAbstract read
In one paragraph

Article in Cell death & disease, 2020. 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
1.5field-weighted citation impact, top 17% 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, 35 citations in OpenAlex.

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  9. Mitochondria and cell death-associated inflammation.Cell death and differentiation · 2023
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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

20 authors at 3 institutions in 1 country.

Lucie CoppinUniversity of Lille, CNRS, Inserm, CHU Lille, UMR9020 - UMR-S 1277 - Canther - Cancer Heterogeneity, Plasticity and Resistance to Therapies, F-59000, Lille, France.
Arnaud JanninUniversity of Lille, CNRS, Inserm, CHU Lille, UMR9020 - UMR-S 1277 - Canther - Cancer Heterogeneity, Plasticity and Resistance to Therapies, F-59000, Lille, France.
Emilie Ait YahyaCHU Lille, Institut de Biochimie & Biologie Moléculaire, Centre de Biologie et Pathologie, F-59000, Lille, France.
Caroline ThuillierCHU Lille, Institut de Génétique, Centre de Biologie et Pathologie, F-59000, Lille, France.
Céline VillenetUniversity of Lille, CHU Lille, Plate-forme de génomique fonctionnelle, Centre de Biologie et Pathologie, F-59000, Lille, France.
Meryem TardivelUniversity of Lille, F-59000, Lille, France.
Antonino BongiovanniUniversity of Lille, F-59000, Lille, France.
Cécile GastonEquipe Cell adhesion and mechanics, Institut Jacques Monod - UMR 7592 CNRS - Université Paris Diderot, F-75205, Paris Cedex 13, France.
Simon de BecoEquipe Cell adhesion and mechanics, Institut Jacques Monod - UMR 7592 CNRS - Université Paris Diderot, F-75205, Paris Cedex 13, France.
Nicolas BaroisUniversity of Lille, CNRS, Inserm, CHU Lille, Institut Pasteur de Lille, U1019 - UMR 8204 - CIIL - Center for Infection and Immunity of Lille, F-59000, Lille, France.
Isabelle van SeuningenUniversity of Lille, CNRS, Inserm, CHU Lille, UMR9020 - UMR-S 1277 - Canther - Cancer Heterogeneity, Plasticity and Resistance to Therapies, F-59000, Lille, France.ORCID http://orcid.org/0000-0002-3131-2694
Emmanuelle DurandUniversity of Lille, CNRS, CHU Lille, Institut Pasteur de Lille, UMR 8199, EGID, F-59000, Lille, France.
Amélie BonnefondUniversity of Lille, CNRS, CHU Lille, Institut Pasteur de Lille, UMR 8199, EGID, F-59000, Lille, France.
Jean-Claude VienneCHU Lille, Institut de Biochimie & Biologie Moléculaire, Centre de Biologie et Pathologie, F-59000, Lille, France.
Joseph VamecqCHU Lille, Institut de Biochimie & Biologie Moléculaire, Centre de Biologie et Pathologie, F-59000, Lille, France.
Martin FigeacUniversity of Lille, CHU Lille, Plate-forme de génomique fonctionnelle, Centre de Biologie et Pathologie, F-59000, Lille, France.
Audrey Vincent *University of Lille, CNRS, Inserm, CHU Lille, UMR9020 - UMR-S 1277 - Canther - Cancer Heterogeneity, Plasticity and Resistance to Therapies, F-59000, Lille, France.
Delphine Delacour *Equipe Cell adhesion and mechanics, Institut Jacques Monod - UMR 7592 CNRS - Université Paris Diderot, F-75205, Paris Cedex 13, France.
Nicole Porchet *University of Lille, CNRS, Inserm, CHU Lille, UMR9020 - UMR-S 1277 - Canther - Cancer Heterogeneity, Plasticity and Resistance to Therapies, F-59000, Lille, France.
Pascal PignyUniversity of Lille, CNRS, Inserm, CHU Lille, UMR9020 - UMR-S 1277 - Canther - Cancer Heterogeneity, Plasticity and Resistance to Therapies, F-59000, Lille, France. pascal.pigny@inserm.fr.ORCID http://orcid.org/0000-0003-3926-4487
Centre National de la Recherche Scientifique · FRCentre Hospitalier Universitaire de Lille · FRUniversité de Lille · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cellular stress response contributes to epithelial defense in adaptation to environment changes. Galectins play a pivotal role in the regulation of this response in malignant cells. However, precise underlying mechanisms are largely unknown. Here we demonstrate that Galectin-3, a pro and anti-apoptotic lectin, is required for setting up a correct cellular response to stress by orchestrating several effects. First, Galectin-3 constitutes a key post-transcriptional regulator of stress-related mRNA regulons coordinating the cell metabolism, the mTORC1 complex or the unfolded protein response (UPR). Moreover, we demonstrated the presence of Galectin-3 with mitochondria-associated membranes (MAM), and its interaction with proteins located at the ER or mitochondrial membranes. There Galectin-3 prevents the activation and recruitment at the mitochondria of the regulator of mitochondria fission DRP-1. Accordingly, loss of Galectin-3 impairs mitochondrial morphology, with more fragmented and round mitochondria, and dynamics both in normal and cancer epithelial cells in basal conditions. Importantly, Galectin-3 deficient cells also display changes of the activity of the mitochondrial respiratory chain complexes, of the mTORC1/S6RP/4EBP1 translation pathway and reactive oxygen species levels. Regarding the ER, Galectin-3 did not modify the activities of the 3 branches of the UPR in basal conditions. However, Galectin-3 favours an adaptative UPR following ER stress induction by Thapsigargin treatment. Altogether, at the ER-mitochondria interface, Galectin-3 coordinates the functioning of the ER and mitochondria, preserves the integrity of mitochondrial network and modulates the ER stress response.

Indexed as

ApoptosisBlood ProteinsEndoplasmic ReticulumEndoplasmic Reticulum StressEpithelial CellsGalectinsHumansMitochondriaMitochondrial MembranesReactive Oxygen SpeciesThapsigarginUnfolded Protein ResponseBlood ProteinsGalectinsLGALS3 protein, humanReactive Oxygen SpeciesThapsigargin

Identifiers

PMID32398681
PMCPMC7217954
OpenAlexW3024648022

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.