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A nuclear protein quality control system for elimination of nucleolus-related inclusions

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  • Additional Information
    • Contributors:
      Centre de recherche en Biologie cellulaire de Montpellier (CRBM); Centre National de la Recherche Scientifique (CNRS)-Université de Montpellier (UM); BioCampus (BCM); Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université de Montpellier (UM); Unité de biologie Moléculaire, Cellulaire et du Développement (MCD); Centre de Biologie Intégrative (CBI); Université Toulouse III - Paul Sabatier (UT3); Université de Toulouse (UT)-Université de Toulouse (UT)-Centre National de la Recherche Scientifique (CNRS)-Université Toulouse III - Paul Sabatier (UT3); Université de Toulouse (UT)-Université de Toulouse (UT)-Centre National de la Recherche Scientifique (CNRS); Institut de pharmacologie et de biologie structurale (IPBS); The study was financially supported by the Labex EpiGenMed, an Investissements d’avenir program, reference ANR-10-LABX-12-0, the Fondation pour la Recherche Médicale (FDT202012010454) awarded to LB and the ANR-AAPG2021-PROCONUC. We are grateful to the imaging facility MRI, a member of the national infrastructure France-BioImaging infrastructure supported by the French National Research Agency (ANR-10-INBS-04, Investments for the future).; ANR-21-CE44-0025,PROCONUC,Contrôle de la qualité des protéines dans le noyau(2021); ANR-10-LABX-0012,EpiGenMed,From Genome and Epigenome to Molecular Medicine: turning new paradigms in biology into the therapeutic strategies of tomorrow(2010)
    • Publication Information:
      CCSD
      EMBO Press
    • Publication Date:
      2024
    • Abstract:
      The raw data regarding the SILAC-based proteomic analysis aresubmitted to ProteomeXchange via the PRIDE database (https://www.ebi.ac.uk/pride/) with the accession number: PXD054637.The source data of this paper are collected in the followingdatabase record: biostudies:S-SCDT-10_1038-S44318-024-00333-9. ; International audience ; The identification of pathways that control elimination of protein inclusions is essential to understand the cellular response to proteotoxicity, particularly in the nuclear compartment, for which our knowledge is limited. We report that stress-induced nuclear inclusions related to the nucleolus are eliminated upon stress alleviation during the recovery period. This process is independent of autophagy/lysosome and CRM1-mediated nuclear export pathways, but strictly depends on the ubiquitin-activating E1 enzyme, UBA1, and on nuclear proteasomes that are recruited into the formed inclusions. UBA1 activity is essential only for the recovery process but dispensable for nuclear inclusion formation. Furthermore, the E3 ligase HUWE1 and HSP70 are components of the ubiquitin/chaperone systems that promote inclusion elimination. The recovery process also requires RNA Pol I-dependent production of the lncRNA IGS 42 during stress. IGS 42 localises within the formed inclusions and promotes their elimination by preserving the mobility of resident proteins. These findings reveal a protein quality control system that operates within the nucleus for the elimination of stress-induced nucleolus-related inclusions.
    • Relation:
      https://doi.org/10.1038/s44318-024-00333-9; info:eu-repo/semantics/altIdentifier/pmid/39690241; PUBMED: 39690241; PUBMEDCENTRAL: PMC11791210
    • Accession Number:
      10.1038/s44318-024-00333-9
    • Online Access:
      https://hal.science/hal-05087097
      https://hal.science/hal-05087097v1/document
      https://hal.science/hal-05087097v1/file/brunello-et-al-a-nuclear-protein-quality-control-system-for-elimination-of-nucleolus-related-inclusions.pdf
      https://doi.org/10.1038/s44318-024-00333-9
    • Rights:
      http://creativecommons.org/licenses/by/ ; info:eu-repo/semantics/OpenAccess
    • Accession Number:
      edsbas.25E0137D