Evidence map›Paper›PMID 30349077›Full record

ArticleCell death and differentiation2019

Recruitment of LC3 to damaged Golgi apparatus.

Lígia C Gomes-da-Silva, Ana Joaquina Jimenez, Allan Sauvat, Wei Xie, Sylvie Souquere, Séverine Divoux, Marko Storch, Baldur Sveinbjørnsson, Øystein Rekdal, Luis G Arnaut and 3 more

Open access · bronzeAbstract read
In one paragraph

Article in Cell death and differentiation, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing 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

19 citing papers in PubMed, 25 citations in OpenAlex.

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  5. A role for CASM in the repair of damaged Golgi architecture.bioRxiv : the preprint server for biology · 2025
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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

13 authors at 5 institutions in 5 countries.

Lígia C Gomes-da-SilvaChemistry Department, University of Coimbra, Coimbra, Portugal.
Ana Joaquina JimenezCell Biology and Cancer, Institut Curie, PSL Research University, CNRS UMR144, Paris, France.
Allan SauvatFaculty of Medicine, University of Paris Sud, Kremlin-Bicêtre, France; 3Metabolomics and Cell Biology Platforms, Gustave Roussy Cancer Campus, Villejuif, France.
Wei XieFaculty of Medicine, University of Paris Sud, Kremlin-Bicêtre, France; 3Metabolomics and Cell Biology Platforms, Gustave Roussy Cancer Campus, Villejuif, France.
Sylvie SouquereGustave Roussy Comprehensive Cancer Center, Villejuif, France.
Séverine DivouxCell Biology and Cancer, Institut Curie, PSL Research University, CNRS UMR144, Paris, France.
Marko StorchDepartment of Life Sciences & Centre for Synthetic Biology & Innovation, Imperial College, South Kensington Campus, London, UK.
Baldur SveinbjørnssonLytix Biopharma AS, Oslo, Norway.
Øystein RekdalLytix Biopharma AS, Oslo, Norway.
Luis G ArnautChemistry Department, University of Coimbra, Coimbra, Portugal.
Oliver KeppFaculty of Medicine, University of Paris Sud, Kremlin-Bicêtre, France; 3Metabolomics and Cell Biology Platforms, Gustave Roussy Cancer Campus, Villejuif, France. captain.olsen@gmail.com.ORCID 0000-0002-6081-9558
Guido KroemerFaculty of Medicine, University of Paris Sud, Kremlin-Bicêtre, France; 3Metabolomics and Cell Biology Platforms, Gustave Roussy Cancer Campus, Villejuif, France. kroemer@orange.fr.ORCID 0000-0002-9129-9401
Franck PerezCell Biology and Cancer, Institut Curie, PSL Research University, CNRS UMR144, Paris, France. franck.perez@curie.fr.
Université Paris-Sud · FRCentre National de la Recherche Scientifique · FRLytix Biopharma (Norway) · NOImperial College London · GBUniversity of Coimbra · PT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

LC3 is a protein that can associate with autophagosomes, autolysosomes, and phagosomes. Here, we show that LC3 can also redistribute toward the damaged Golgi apparatus where it clusters with SQSTM1/p62 and lysosomes. This organelle-specific relocation, which did not involve the generation of double-membraned autophagosomes, could be observed after Golgi damage was induced by various strategies, namely (i) laser-induced localized cellular damage, (ii) local expression of peroxidase and exposure to peroxide and diaminobenzidine, (iii) treatment with the Golgi-tropic photosensitizer redaporfin and light, (iv) or exposure to the Golgi-tropic anticancer peptidomimetic LTX-401. Mechanistic exploration led to the conclusion that both reactive oxygen species-dependent and -independent Golgi damage induces a similar phenotype that depended on ATG5 yet did not depend on phosphatidylinositol-3-kinase catalytic subunit type 3 and Beclin-1. Interestingly, knockout of ATG5 sensitized cells to Golgi damage-induced cell death, suggesting that the pathway culminating in the relocation of LC3 to the damaged Golgi may have a cytoprotective function.

Indexed as

Antineoplastic Agentsbeta-AlanineCell DeathGolgi ApparatusGreen Fluorescent ProteinsHeLa CellsHumansMicrotubule-Associated ProteinsTumor Cells, CulturedAntineoplastic Agentsbeta-AlanineGreen Fluorescent ProteinsLTX-401MAP1LC3A protein, humanMicrotubule-Associated Proteins

Identifiers

PMID30349077
PMCPMC6748261
OpenAlexW2897066615

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.