AHNAK controls 53BP1-mediated p53 response by restraining 53BP1 oligomerization and phase separation.


Journal

Molecular cell
ISSN: 1097-4164
Titre abrégé: Mol Cell
Pays: United States
ID NLM: 9802571

Informations de publication

Date de publication:
17 06 2021
Historique:
received: 27 08 2020
revised: 05 03 2021
accepted: 09 04 2021
pubmed: 8 5 2021
medline: 21 7 2021
entrez: 7 5 2021
Statut: ppublish

Résumé

p53-binding protein 1 (53BP1) regulates both the DNA damage response and p53 signaling. Although 53BP1's function is well established in DNA double-strand break repair, how its role in p53 signaling is modulated remains poorly understood. Here, we identify the scaffolding protein AHNAK as a G1 phase-enriched interactor of 53BP1. We demonstrate that AHNAK binds to the 53BP1 oligomerization domain and controls its multimerization potential. Loss of AHNAK results in hyper-accumulation of 53BP1 on chromatin and enhanced phase separation, culminating in an elevated p53 response, compromising cell survival in cancer cells but leading to senescence in non-transformed cells. Cancer transcriptome analyses indicate that AHNAK-53BP1 cooperation contributes to the suppression of p53 target gene networks in tumors and that loss of AHNAK sensitizes cells to combinatorial cancer treatments. These findings highlight AHNAK as a rheostat of 53BP1 function, which surveys cell proliferation by preventing an excessive p53 response.

Identifiants

pubmed: 33961796
pii: S1097-2765(21)00315-4
doi: 10.1016/j.molcel.2021.04.010
pmc: PMC8221568
pii:
doi:

Substances chimiques

AHNAK protein, human 0
Chromatin 0
Histones 0
Membrane Proteins 0
Neoplasm Proteins 0
TP53BP1 protein, human 0
Tumor Suppressor Protein p53 0
Tumor Suppressor p53-Binding Protein 1 0
DNA 9007-49-2

Types de publication

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

Langues

eng

Sous-ensembles de citation

IM

Pagination

2596-2610.e7

Informations de copyright

Copyright © 2021 The Authors. Published by Elsevier Inc. All rights reserved.

Déclaration de conflit d'intérêts

Declaration of interests The authors declare no competing interests.

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Auteurs

Indrajeet Ghodke (I)

Institut de Génétique et de Biologie Moléculaire et Cellulaire, 67404 Illkirch, France; Institut National de la Santé et de la Recherche Médicale, U964, 67404 Illkirch, France; Centre National de Recherche Scientifique, UMR7104, 67404 Illkirch, France; Université de Strasbourg, 67081 Strasbourg, France. Electronic address: ghodkei@igbmc.fr.

Michaela Remisova (M)

Department of Molecular Mechanisms of Disease, University of Zurich, 8057 Zurich, Switzerland.

Audrey Furst (A)

Institut de Génétique et de Biologie Moléculaire et Cellulaire, 67404 Illkirch, France; Institut National de la Santé et de la Recherche Médicale, U964, 67404 Illkirch, France; Centre National de Recherche Scientifique, UMR7104, 67404 Illkirch, France; Université de Strasbourg, 67081 Strasbourg, France.

Sinan Kilic (S)

Department of Molecular Mechanisms of Disease, University of Zurich, 8057 Zurich, Switzerland.

Bernardo Reina-San-Martin (B)

Institut de Génétique et de Biologie Moléculaire et Cellulaire, 67404 Illkirch, France; Institut National de la Santé et de la Recherche Médicale, U964, 67404 Illkirch, France; Centre National de Recherche Scientifique, UMR7104, 67404 Illkirch, France; Université de Strasbourg, 67081 Strasbourg, France.

Anna R Poetsch (AR)

Biotechnology Center, TU Dresden and National Center for Tumor Diseases (NCT), Dresden, Germany.

Matthias Altmeyer (M)

Department of Molecular Mechanisms of Disease, University of Zurich, 8057 Zurich, Switzerland.

Evi Soutoglou (E)

Institut de Génétique et de Biologie Moléculaire et Cellulaire, 67404 Illkirch, France; Institut National de la Santé et de la Recherche Médicale, U964, 67404 Illkirch, France; Centre National de Recherche Scientifique, UMR7104, 67404 Illkirch, France; Université de Strasbourg, 67081 Strasbourg, France. Electronic address: e.soutoglou@sussex.ac.uk.

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