دورية أكاديمية
أعرض في EDS

Immunoproteasome-specific subunit PSMB9 induction is required to regulate cellular proteostasis upon mitochondrial dysfunction.

التفاصيل البيبلوغرافية
العنوان: Immunoproteasome-specific subunit PSMB9 induction is required to regulate cellular proteostasis upon mitochondrial dysfunction.
المؤلفون: Kim M; IMol Polish Academy of Sciences, Warsaw, Poland., Serwa RA; IMol Polish Academy of Sciences, Warsaw, Poland.; ReMedy International Research Agenda Unit, IMol Polish Academy of Sciences, Warsaw, Poland., Samluk L; Centre of New Technologies, University of Warsaw, Warsaw, Poland., Suppanz I; CIBSS Centre for Integrative Biological Signalling Studies, University of Freiburg, Freiburg, Germany.; Max Planck Institute of Immunobiology and Epigenetics, Freiburg, Germany., Kodroń A; IMol Polish Academy of Sciences, Warsaw, Poland.; ReMedy International Research Agenda Unit, IMol Polish Academy of Sciences, Warsaw, Poland., Stępkowski TM; IMol Polish Academy of Sciences, Warsaw, Poland.; ReMedy International Research Agenda Unit, IMol Polish Academy of Sciences, Warsaw, Poland., Elancheliyan P; IMol Polish Academy of Sciences, Warsaw, Poland., Tsegaye B; IMol Polish Academy of Sciences, Warsaw, Poland., Oeljeklaus S; Department of Biochemistry, Theodor Boveri-Institute, Biocenter, University of Würzburg, Würzburg, Germany., Wasilewski M; IMol Polish Academy of Sciences, Warsaw, Poland., Warscheid B; CIBSS Centre for Integrative Biological Signalling Studies, University of Freiburg, Freiburg, Germany.; Department of Biochemistry, Theodor Boveri-Institute, Biocenter, University of Würzburg, Würzburg, Germany., Chacinska A; IMol Polish Academy of Sciences, Warsaw, Poland. a.chacinska@imol.institute.; ReMedy International Research Agenda Unit, IMol Polish Academy of Sciences, Warsaw, Poland. a.chacinska@imol.institute.
المصدر: Nature communications [Nat Commun] 2023 Jul 11; Vol. 14 (1), pp. 4092. Date of Electronic Publication: 2023 Jul 11.
نوع المنشور: Journal Article; Research Support, Non-U.S. Gov't
اللغة: English
بيانات الدورية: Publisher: Nature Pub. Group Country of Publication: England NLM ID: 101528555 Publication Model: Electronic Cited Medium: Internet ISSN: 2041-1723 (Electronic) Linking ISSN: 20411723 NLM ISO Abbreviation: Nat Commun Subsets: MEDLINE
أسماء مطبوعة: Original Publication: [London] : Nature Pub. Group
مواضيع طبية MeSH: Proteasome Endopeptidase Complex* , Proteostasis* , Cysteine Endopeptidases*/metabolism, Humans ; Cytoplasm ; Mitochondria ; Peptide Elongation Factor 1
مستخلص: Perturbed cellular protein homeostasis (proteostasis) and mitochondrial dysfunction play an important role in neurodegenerative diseases, however, the interplay between these two phenomena remains unclear. Mitochondrial dysfunction leads to a delay in mitochondrial protein import, causing accumulation of non-imported mitochondrial proteins in the cytosol and challenging proteostasis. Cells respond by increasing proteasome activity and molecular chaperones in yeast and C. elegans. Here, we demonstrate that in human cells mitochondrial dysfunction leads to the upregulation of a chaperone HSPB1 and, interestingly, an immunoproteasome-specific subunit PSMB9. Moreover, PSMB9 expression is dependent on the translation elongation factor EEF1A2. These mechanisms constitute a defense response to preserve cellular proteostasis under mitochondrial stress. Our findings define a mode of proteasomal activation through the change in proteasome composition driven by EEF1A2 and its spatial regulation, and are useful to formulate therapies to prevent neurodegenerative diseases.
(© 2023. The Author(s).)
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المشرفين على المادة: 0 (EEF1A2 protein, human)
0 (Peptide Elongation Factor 1)
EC 3.4.25.1 (Proteasome Endopeptidase Complex)
144416-78-4 (LMP-2 protein)
EC 3.4.22.- (Cysteine Endopeptidases)
تواريخ الأحداث: Date Created: 20230711 Date Completed: 20230713 Latest Revision: 20230718
رمز التحديث: 20230718
مُعرف محوري في PubMed: PMC10336106
DOI: 10.1038/s41467-023-39642-8
PMID: 37433777
قاعدة البيانات: MEDLINE
الوصف
تدمد:2041-1723
DOI:10.1038/s41467-023-39642-8