Evidence map›Paper›PMID 41914023›Full record

ArticleFEBS letters2026

Hyperosmotic stress induces PARP1-mediated HPF1-dependent mono(ADP-ribosyl)ation.

Anna Georgina Kopasz, Mihály Mérey, Rebeka Vásárhelyi, Ramóna Pék, Victor Imburchia, László Henn, Adrián Kószó, Nicholas D Lakin, Ivan Ahel, Sébastien Huet and 2 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in FEBS letters, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

12 authors.

Anna Georgina KopaszLaboratory of DNA Damage and Nuclear Dynamics, Institute of Genetics, HUN-REN Biological Research Centre, Szeged, Hungary.
Mihály MéreyLaboratory of DNA Damage and Nuclear Dynamics, Institute of Genetics, HUN-REN Biological Research Centre, Szeged, Hungary.
Rebeka VásárhelyiLaboratory of DNA Damage and Nuclear Dynamics, Institute of Genetics, HUN-REN Biological Research Centre, Szeged, Hungary.
Ramóna PékUniv Rennes, CNRS, IGDR (Institut de Génétique et Développement de Rennes) - UMR 6290, BIOSIT (Biologie, Santé, Innovation Technologique de Rennes) - UMS 3480, France.
Victor ImburchiaUniv Rennes, CNRS, IGDR (Institut de Génétique et Développement de Rennes) - UMR 6290, BIOSIT (Biologie, Santé, Innovation Technologique de Rennes) - UMS 3480, France.
László HennLaboratory of DNA Damage and Nuclear Dynamics, Institute of Genetics, HUN-REN Biological Research Centre, Szeged, Hungary.
Adrián KószóLaboratory of DNA Damage and Nuclear Dynamics, Institute of Genetics, HUN-REN Biological Research Centre, Szeged, Hungary.
Nicholas D LakinDepartment of Biochemistry, University of Oxford, UK.
Ivan AhelSir William Dunn School of Pathology, University of Oxford, UK.ORCID https://orcid.org/0000-0002-9446-3756
Sébastien HuetUniv Rennes, CNRS, IGDR (Institut de Génétique et Développement de Rennes) - UMR 6290, BIOSIT (Biologie, Santé, Innovation Technologique de Rennes) - UMS 3480, France.ORCID https://orcid.org/0000-0002-3978-0003
Ágnes CzibulaLaboratory of DNA Damage and Nuclear Dynamics, Institute of Genetics, HUN-REN Biological Research Centre, Szeged, Hungary.
Gyula TiminszkyLaboratory of DNA Damage and Nuclear Dynamics, Institute of Genetics, HUN-REN Biological Research Centre, Szeged, Hungary.ORCID https://orcid.org/0000-0001-6342-8985

Funding

Agence Nationale de la Recherche ANR-22-CE12-0039 AROSEBiotechnology and Biological Sciences Research Council BB/R007195/1Biotechnology and Biological Sciences Research Council BB/W016613/1Cancer Research UK C35050/A22284Fondation pour la Recherche Médicale ECO202406019133Nemzeti Kutatási Fejlesztési és Innovációs Hivatal K143248Nemzeti Kutatási Fejlesztési és Innovációs Hivatal K151375Wellcome TrustWellcome Trust 223107Wellcome Trust 302632
6 · The paper itself

Abstract

While the downstream effectors of the hyperosmotic stress response are relatively well characterized, the primary molecular sensors responsible for initial stress detection remain poorly defined. In this study, we demonstrate that hyperosmotic stress triggers a rapid and transient mono(ADP-ribosyl)ation (MARylation). Beside MARylation, signs of acute genotoxicity are missing and CHK1 activation is observed only upon recovery from osmotic stress. Our data indicate that PARP1 catalyzes its own MARylation in an HPF1 co-factor dependent manner. Biochemical assays further demonstrate that the mono-ADP-ribose moiety is resistant to hydroxylamine treatment, which is a feature of HPF1-directed O-glycosidic bonds. Together, these findings support a model in which PARP1 acts as a sensor of chromatin structure changes induced by hyperosmotic stress leading to its autoMARylation.

Indexed as

Adenosine Diphosphate RiboseADP-RibosylationNuclear ProteinsOsmotic PressurePoly(ADP-ribose) PolymerasesCarrier ProteinsCheckpoint Kinase 1HumansHydroxylaminePoly (ADP-Ribose) Polymerase-1Adenosine Diphosphate RiboseCarrier ProteinsCheckpoint Kinase 1HPF1 protein, humanHydroxylamineNuclear ProteinsPARP1 protein, humanPoly (ADP-Ribose) Polymerase-1Poly(ADP-ribose) PolymerasesHPF1hyperosmotic stressmono(ADP‐ribosyl)ationPARP1

Identifiers

PMID41914023
PMCPMC13618299

What OpenQuestion holds

Textmetadata
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.