53BP1-mediated recruitment of RASSF1A to ribosomal DNA breaks promotes local ATM signaling.


Journal

EMBO reports
ISSN: 1469-3178
Titre abrégé: EMBO Rep
Pays: England
ID NLM: 100963049

Informations de publication

Date de publication:
03 08 2022
Historique:
revised: 30 05 2022
received: 09 12 2021
accepted: 03 06 2022
pubmed: 28 6 2022
medline: 5 8 2022
entrez: 27 6 2022
Statut: ppublish

Résumé

DNA lesions occur across the genome and constitute a threat to cell viability; however, damage at specific genomic loci has a relatively greater impact on overall genome stability. The ribosomal RNA gene repeats (rDNA) are emerging fragile sites. Recent progress in understanding how the rDNA damage response is organized has highlighted a key role of adaptor proteins. Here, we show that the scaffold tumor suppressor RASSF1A is recruited to rDNA breaks. RASSF1A recruitment to double-strand breaks is mediated by 53BP1 and depends on RASSF1A phosphorylation at Serine 131 by ATM kinase. Employing targeted rDNA damage, we uncover that RASSF1A recruitment promotes local ATM signaling. RASSF1A silencing, a common epigenetic event during malignant transformation, results in persistent breaks, rDNA copy number alterations and decreased cell viability. Overall, we identify a novel role for RASSF1A at rDNA break sites, provide mechanistic insight into how the DNA damage response is organized in a chromatin context, and provide further evidence for how silencing of the RASSF1A tumor suppressor contributes to genome instability.

Identifiants

pubmed: 35758159
doi: 10.15252/embr.202154483
pmc: PMC9346497
doi:

Substances chimiques

DNA, Ribosomal 0
DNA-Binding Proteins 0
Tumor Suppressor Proteins 0
Tumor Suppressor p53-Binding Protein 1 0
ATM protein, human EC 2.7.11.1
Ataxia Telangiectasia Mutated Proteins EC 2.7.11.1

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

e54483

Informations de copyright

© 2022 The Authors. Published under the terms of the CC BY NC ND 4.0 license.

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Auteurs

Stavroula Tsaridou (S)

Department of Biology, School of Medicine, University of Patras, Patras, Greece.

Georgia Velimezi (G)

Department of Biology, School of Medicine, University of Patras, Patras, Greece.
Biomedical Research Foundation of the Academy of Athens, Athens, Greece.

Frances Willenbrock (F)

Department of Oncology, University of Oxford, Oxford, UK.

Maria Chatzifrangkeskou (M)

Department of Oncology, University of Oxford, Oxford, UK.

Waheba Elsayed (W)

Institute of Molecular Biology (IMB), Mainz, Germany.

Andreas Panagopoulos (A)

Department of Biology, School of Medicine, University of Patras, Patras, Greece.

Dimitris Karamitros (D)

Department of Physiology, School of Medicine, University of Patras, Patras, Greece.

Vassilis Gorgoulis (V)

Biomedical Research Foundation of the Academy of Athens, Athens, Greece.
Laboratory of Histology and Embryology, Medical School, National and Kapodistrian University of Athens, Athens, Greece.
Faculty of Biology, Medicine and Health, Manchester Academic Health Centre, University of Manchester, Manchester, UK.
Ninewells Hospital and Medical School, University of Dundee, Dundee, UK.

Zoi Lygerou (Z)

Department of Biology, School of Medicine, University of Patras, Patras, Greece.

Vassilis Roukos (V)

Department of Biology, School of Medicine, University of Patras, Patras, Greece.
Institute of Molecular Biology (IMB), Mainz, Germany.

Eric O'Neill (E)

Department of Oncology, University of Oxford, Oxford, UK.

Dafni Eleftheria Pefani (DE)

Department of Biology, School of Medicine, University of Patras, Patras, Greece.

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Classifications MeSH