Evidence map›Paper›PMID 36522328›Full record

ArticleCell death & disease2022

Filamentous nuclear actin regulation of PML NBs during the DNA damage response is deregulated by prelamin A.

Andrew M Cobb, Shanelle A De Silva, Robert Hayward, Karolina Sek, Svenja Ulferts, Robert Grosse, Catherine M Shanahan

Open access · goldAbstract read
In one paragraph

Article in Cell death & disease, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
1.4field-weighted citation impact, top 19% 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

10 citing papers in PubMed, 16 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Recent advances in nuclear actin research.Nucleus (Austin, Tex.) · 2025
    Review
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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

7 authors at 2 institutions in 2 countries.

Andrew M CobbBHF Centre of Research Excellence, School of Cardiovascular Medicine and Sciences, King's College London, The James Black Centre, 125 Coldharbour Lane, London, SE5 9NU, United Kingdom. andrew.cobb@kcl.ac.uk.ORCID 0000-0003-2163-5999
Shanelle A De SilvaBHF Centre of Research Excellence, School of Cardiovascular Medicine and Sciences, King's College London, The James Black Centre, 125 Coldharbour Lane, London, SE5 9NU, United Kingdom.
Robert HaywardBHF Centre of Research Excellence, School of Cardiovascular Medicine and Sciences, King's College London, The James Black Centre, 125 Coldharbour Lane, London, SE5 9NU, United Kingdom.
Karolina SekBHF Centre of Research Excellence, School of Cardiovascular Medicine and Sciences, King's College London, The James Black Centre, 125 Coldharbour Lane, London, SE5 9NU, United Kingdom.
Svenja UlfertsInstitute of Experimental and Clinical Pharmacology and Toxicology, Medical Faculty, University of Freiburg, Albertstraße 25, 79104, Freiburg, Germany.ORCID 0000-0002-6605-8163
Robert GrosseInstitute of Experimental and Clinical Pharmacology and Toxicology, Medical Faculty, University of Freiburg, Albertstraße 25, 79104, Freiburg, Germany.ORCID 0000-0002-3380-5273
Catherine M ShanahanBHF Centre of Research Excellence, School of Cardiovascular Medicine and Sciences, King's College London, The James Black Centre, 125 Coldharbour Lane, London, SE5 9NU, United Kingdom.
King's College London · GBUniversity of Freiburg · DE

Funding

British Heart Foundation (BHF) RG/17/2/32808
6 · The paper itself

Abstract

Nuclear actin participates in a continuously expanding list of core processes within eukaryotic nuclei, including the maintenance of genomic integrity. In response to DNA damage, nuclear actin polymerises into filaments that are involved in the repair of damaged DNA through incompletely defined mechanisms. We present data to show that the formation of nuclear F-actin in response to genotoxic stress acts as a scaffold for PML NBs and that these filamentous networks are essential for PML NB fission and recruitment of microbodies to DNA lesions. Further to this, we demonstrate that the accumulation of the toxic lamin A precursor prelamin A induces mislocalisation of nuclear actin to the nuclear envelope and prevents the establishment of nucleoplasmic F-actin networks in response to stress. Consequently, PML NB dynamics and recruitment to DNA lesions is ablated, resulting in impaired DNA damage repair. Inhibition of nuclear export of formin mDia2 restores nuclear F-actin formation by augmenting polymerisation of nuclear actin in response to stress and rescues PML NB localisation to sites of DNA repair, leading to reduced levels of DNA damage.

Indexed as

ActinsNuclear ProteinsCell NucleusDNADNA DamageLamin Type APromyelocytic Leukemia Nuclear BodiesPromyelocytic Leukemia ProteinActinsDNALamin Type ANuclear Proteinsprelamin APromyelocytic Leukemia Protein

Identifiers

PMID36522328
PMCPMC9755150
OpenAlexW4311744542

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.