دورية أكاديمية
أعرض في EDS

RNF14-dependent atypical ubiquitylation promotes translation-coupled resolution of RNA-protein crosslinks.

التفاصيل البيبلوغرافية
العنوان: RNF14-dependent atypical ubiquitylation promotes translation-coupled resolution of RNA-protein crosslinks.
المؤلفون: Zhao S; Department of Biochemistry, Ludwig-Maximilians-Universität München, Munich, Germany; Gene Center, Ludwig-Maximilians-Universität München, Munich, Germany., Cordes J; Department of Biochemistry, Ludwig-Maximilians-Universität München, Munich, Germany; Gene Center, Ludwig-Maximilians-Universität München, Munich, Germany., Caban KM; Gene Center, Ludwig-Maximilians-Universität München, Munich, Germany., Götz MJ; Department of Biochemistry, Ludwig-Maximilians-Universität München, Munich, Germany; Gene Center, Ludwig-Maximilians-Universität München, Munich, Germany., Mackens-Kiani T; Department of Biochemistry, Ludwig-Maximilians-Universität München, Munich, Germany; Gene Center, Ludwig-Maximilians-Universität München, Munich, Germany., Veltri AJ; Department of Molecular Biology and Genetics, Johns Hopkins University School of Medicine, Baltimore, USA., Sinha NK; Department of Molecular Biology and Genetics, Johns Hopkins University School of Medicine, Baltimore, USA., Weickert P; Department of Biochemistry, Ludwig-Maximilians-Universität München, Munich, Germany; Gene Center, Ludwig-Maximilians-Universität München, Munich, Germany., Kaya S; Max Planck Institute of Biochemistry, Martinsried, Germany., Hewitt G; King's College London School of Cancer & Pharmaceutical Sciences, London, UK., Nedialkova DD; Max Planck Institute of Biochemistry, Martinsried, Germany; Technical University of Munich, TUM School of Natural Sciences, Department of Bioscience, Garching, Germany., Fröhlich T; Gene Center, Ludwig-Maximilians-Universität München, Munich, Germany., Beckmann R; Department of Biochemistry, Ludwig-Maximilians-Universität München, Munich, Germany; Gene Center, Ludwig-Maximilians-Universität München, Munich, Germany., Buskirk AR; Department of Molecular Biology and Genetics, Johns Hopkins University School of Medicine, Baltimore, USA., Green R; Department of Molecular Biology and Genetics, Johns Hopkins University School of Medicine, Baltimore, USA; Howard Hughes Medical Institute, Johns Hopkins University School of Medicine, Baltimore, USA., Stingele J; Department of Biochemistry, Ludwig-Maximilians-Universität München, Munich, Germany; Gene Center, Ludwig-Maximilians-Universität München, Munich, Germany. Electronic address: stingele@genzentrum.lmu.de.
المصدر: Molecular cell [Mol Cell] 2023 Dec 07; Vol. 83 (23), pp. 4290-4303.e9. Date of Electronic Publication: 2023 Nov 10.
نوع المنشور: Journal Article
اللغة: English
بيانات الدورية: Publisher: Cell Press Country of Publication: United States NLM ID: 9802571 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1097-4164 (Electronic) Linking ISSN: 10972765 NLM ISO Abbreviation: Mol Cell Subsets: MEDLINE
أسماء مطبوعة: Publication: Cambridge Ma : Cell Press
Original Publication: Cambridge, Mass. : Cell Press, c1997-
مواضيع طبية MeSH: RNA*/metabolism , Ubiquitin*/metabolism, Humans ; Ubiquitination ; Ribosomes/metabolism ; Ubiquitin-Protein Ligases/genetics ; Ubiquitin-Protein Ligases/metabolism ; Aldehydes ; Protein Biosynthesis
مستخلص: Reactive aldehydes are abundant endogenous metabolites that challenge homeostasis by crosslinking cellular macromolecules. Aldehyde-induced DNA damage requires repair to prevent cancer and premature aging, but it is unknown whether cells also possess mechanisms that resolve aldehyde-induced RNA lesions. Here, we establish photoactivatable ribonucleoside-enhanced crosslinking (PAR-CL) as a model system to study RNA crosslinking damage in the absence of confounding DNA damage in human cells. We find that such RNA damage causes translation stress by stalling elongating ribosomes, which leads to collisions with trailing ribosomes and activation of multiple stress response pathways. Moreover, we discovered a translation-coupled quality control mechanism that resolves covalent RNA-protein crosslinks. Collisions between translating ribosomes and crosslinked mRNA-binding proteins trigger their modification with atypical K6- and K48-linked ubiquitin chains. Ubiquitylation requires the E3 ligase RNF14 and leads to proteasomal degradation of the protein adduct. Our findings identify RNA lesion-induced translational stress as a central component of crosslinking damage.
Competing Interests: Declaration of interests R.G. is a member of the scientific advisory board at the journal Molecular Cell.
(Copyright © 2023 The Author(s). Published by Elsevier Inc. All rights reserved.)
التعليقات: Comment in: Mol Cell. 2023 Dec 7;83(23):4197-4199. (PMID: 38065058)
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معلومات مُعتمدة: R01 GM136960 United States GM NIGMS NIH HHS
فهرسة مساهمة: Keywords: GCN1; K6-linked ubiquitin chains; RNA damage; RNA-protein crosslinks; RNF14; RNF25; atypical ubiquitylation; formaldehyde; ribosome; translation
المشرفين على المادة: 63231-63-0 (RNA)
0 (Ubiquitin)
EC 2.3.2.27 (Ubiquitin-Protein Ligases)
0 (Aldehydes)
تواريخ الأحداث: Date Created: 20231111 Date Completed: 20231216 Latest Revision: 20240308
رمز التحديث: 20240309
مُعرف محوري في PubMed: PMC10783637
DOI: 10.1016/j.molcel.2023.10.012
PMID: 37951216
قاعدة البيانات: MEDLINE
الوصف
تدمد:1097-4164
DOI:10.1016/j.molcel.2023.10.012