Evidence map›Paper›PMID 33961796›Full record

ArticleMolecular cell2021

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

Indrajeet Ghodke, Michaela Remisova, Audrey Furst, Sinan Kilic, Bernardo Reina-San-Martin, Anna R Poetsch, Matthias Altmeyer, Evi Soutoglou

Open access · bronzeAbstract read
In one paragraph

Article in Molecular cell, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing papers in PubMed
5.5field-weighted citation impact, top 3% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

53 citing papers in PubMed, 81 citations in OpenAlex.

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  3. Genetic alterations in SUPT6H are associated with neurodevelopmental disorders.Biochimica et biophysica acta. Molecular basis of disease · 2026
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors at 3 institutions in 3 countries.

Indrajeet GhodkeInstitut 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 RemisovaDepartment of Molecular Mechanisms of Disease, University of Zurich, 8057 Zurich, Switzerland.
Audrey FurstInstitut 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 KilicDepartment of Molecular Mechanisms of Disease, University of Zurich, 8057 Zurich, Switzerland.
Bernardo Reina-San-MartinInstitut 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 PoetschBiotechnology Center, TU Dresden and National Center for Tumor Diseases (NCT), Dresden, Germany.
Matthias AltmeyerDepartment of Molecular Mechanisms of Disease, University of Zurich, 8057 Zurich, Switzerland.
Evi SoutoglouInstitut 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.
Inserm · FRUniversity of Zurich · CHNational Center for Tumor Diseases · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

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.

Indexed as

Cell Line, TumorChromatinDNADNA Breaks, Double-StrandedDNA RepairG1 PhaseHistonesHumansMCF-7 CellsMembrane ProteinsNeoplasm ProteinsSignal TransductionTumor Suppressor p53-Binding Protein 1Tumor Suppressor Protein p53AHNAK protein, humanChromatinDNAHistonesMembrane ProteinsNeoplasm ProteinsTP53BP1 protein, humanTumor Suppressor p53-Binding Protein 1Tumor Suppressor Protein p5353BP1AHNAKapoptosiscancercell-cycle progressionDNA repairp21p53phase-separationsenescence

Identifiers

PMID33961796
PMCPMC8221568
OpenAlexW3159918861

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.