Evidence map›Paper›PMID 38542224›Full record

ArticleInternational journal of molecular sciences2024

Mitochondrial Ribosomal Protein MRPS15 Is a Component of Cytosolic Ribosomes and Regulates Translation in Stressed Cardiomyocytes.

Florian David, Emilie Roussel, Carine Froment, Tangra Draia-Nicolau, Françoise Pujol, Odile Burlet-Schiltz, Anthony K Henras, Eric Lacazette, Florent Morfoisse, Florence Tatin and 4 more

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
1.4field-weighted citation impact, top 20% 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

3 citing papers in PubMed, 6 citations in OpenAlex.

  1. Article
  2. Article
  3. 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

14 authors at 3 institutions in 1 country.

Florian DavidInstitut des Maladies Métaboliques et Cardiovasculaires (I2MC), Unité Mixte de Recherche (UMR) 1297, Institut National de la Santé et de la Recherche Médicale (Inserm), Université de Toulouse, 31432 Toulouse, France.
Emilie RousselInstitut des Maladies Métaboliques et Cardiovasculaires (I2MC), Unité Mixte de Recherche (UMR) 1297, Institut National de la Santé et de la Recherche Médicale (Inserm), Université de Toulouse, 31432 Toulouse, France.
Carine FromentInstitut de Pharmacologie et Biologie Structurale (IPBS), Centre National de la Recherche Scientifique (CNRS), Université de Toulouse, 31077 Toulouse, France.ORCID 0000-0003-3688-5560
Tangra Draia-NicolauInstitut des Maladies Métaboliques et Cardiovasculaires (I2MC), Unité Mixte de Recherche (UMR) 1297, Institut National de la Santé et de la Recherche Médicale (Inserm), Université de Toulouse, 31432 Toulouse, France.
Françoise PujolInstitut des Maladies Métaboliques et Cardiovasculaires (I2MC), Unité Mixte de Recherche (UMR) 1297, Institut National de la Santé et de la Recherche Médicale (Inserm), Université de Toulouse, 31432 Toulouse, France.
Odile Burlet-SchiltzInstitut de Pharmacologie et Biologie Structurale (IPBS), Centre National de la Recherche Scientifique (CNRS), Université de Toulouse, 31077 Toulouse, France.ORCID 0000-0002-3606-2356
Anthony K HenrasUMR 5077 Molecular, Cellular and Developmental Biology (MCD), Centre de Biologie Intégrative (CBI), CNRS, Université de Toulouse, 31062 Toulouse, France.ORCID 0000-0001-7785-9938
Eric LacazetteInstitut des Maladies Métaboliques et Cardiovasculaires (I2MC), Unité Mixte de Recherche (UMR) 1297, Institut National de la Santé et de la Recherche Médicale (Inserm), Université de Toulouse, 31432 Toulouse, France.ORCID 0000-0003-1234-5260
Florent MorfoisseInstitut des Maladies Métaboliques et Cardiovasculaires (I2MC), Unité Mixte de Recherche (UMR) 1297, Institut National de la Santé et de la Recherche Médicale (Inserm), Université de Toulouse, 31432 Toulouse, France.ORCID 0000-0003-1532-3665
Florence TatinInstitut des Maladies Métaboliques et Cardiovasculaires (I2MC), Unité Mixte de Recherche (UMR) 1297, Institut National de la Santé et de la Recherche Médicale (Inserm), Université de Toulouse, 31432 Toulouse, France.
Jean-Jacques DiazCentre de Recherche en Cancerologie de Lyon (CRCL), UMR 1052, Inserm, UMR 5286, CNRS, Centre Léon Bérard, Université de Lyon, 69008 Lyon, France.ORCID 0000-0002-7914-4319
Frédéric CatezCentre de Recherche en Cancerologie de Lyon (CRCL), UMR 1052, Inserm, UMR 5286, CNRS, Centre Léon Bérard, Université de Lyon, 69008 Lyon, France.ORCID 0000-0001-8255-9091
Barbara Garmy-SusiniInstitut des Maladies Métaboliques et Cardiovasculaires (I2MC), Unité Mixte de Recherche (UMR) 1297, Institut National de la Santé et de la Recherche Médicale (Inserm), Université de Toulouse, 31432 Toulouse, France.ORCID 0000-0001-6100-2294
Anne-Catherine PratsInstitut des Maladies Métaboliques et Cardiovasculaires (I2MC), Unité Mixte de Recherche (UMR) 1297, Institut National de la Santé et de la Recherche Médicale (Inserm), Université de Toulouse, 31432 Toulouse, France.ORCID 0000-0002-5282-3776
Inserm · FRCentre National de la Recherche Scientifique · FRUniversité Claude Bernard Lyon 1 · FR

Funding

Agence Nationale de la Recherche ANR-18-CE11-0020-RIBOCARDFondation pour la Recherche Médicale 2022 labellisationFondation Toulouse Cancer Santé 2022Ligue Nationale Contre le Cancer PhD fellowship
6 · The paper itself

Abstract

Regulation of mRNA translation is a crucial step in controlling gene expression in stressed cells, impacting many pathologies, including heart ischemia. In recent years, ribosome heterogeneity has emerged as a key control mechanism driving the translation of subsets of mRNAs. In this study, we investigated variations in ribosome composition in human cardiomyocytes subjected to endoplasmic reticulum stress induced by tunicamycin treatment. Our findings demonstrate that this stress inhibits global translation in cardiomyocytes while activating internal ribosome entry site (IRES)-dependent translation. Analysis of translating ribosome composition in stressed and unstressed cardiomyocytes was conducted using mass spectrometry. We observed no significant changes in ribosomal protein composition, but several mitochondrial ribosomal proteins (MRPs) were identified in cytosolic polysomes, showing drastic variations between stressed and unstressed cells. The most notable increase in polysomes of stressed cells was observed in MRPS15. Its interaction with ribosomal proteins was confirmed by proximity ligation assay (PLA) and immunoprecipitation, suggesting its intrinsic role as a ribosomal component during stress. Knock-down or overexpression experiments of MRPS15 revealed its role as an activator of IRES-dependent translation. Furthermore, polysome profiling after immunoprecipitation with anti-MRPS15 antibody revealed that the "MRPS15 ribosome" is specialized in translating mRNAs involved in the unfolded protein response.

Indexed as

Myocytes, CardiacRibosomal ProteinsCytosolHumansInternal Ribosome Entry SitesPolyribosomesProtein BiosynthesisRibosomesRNA, MessengerInternal Ribosome Entry SitesRibosomal ProteinsRNA, Messengercardiomyocyteendoplasmic reticulum stressIRESmitochondrial ribosomal proteinproteomicsribosome heterogeneitytranslational control

Identifiers

PMID38542224
PMCPMC10970015
OpenAlexW4392747779

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.