Evidence map›Paper›PMID 30668775›Full record

ArticleNucleic acids research2019

Tyrosine kinase c-Abl couples RNA polymerase II transcription to DNA double-strand breaks.

Kaspar Burger, Margarita Schlackow, Monika Gullerova

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 61 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
61citing papers in PubMed, 1 pooled it
4.9field-weighted citation impact, top 4% 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

61 citing papers in PubMed, 1 synthesis or guideline pooled it, 95 citations in OpenAlex.

  1. Pooled it
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  13. Mechanisms underlining R-loop biology and implications for human disease.Frontiers in cell and developmental biology · 2025
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    Article
  17. Article
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  20. Article

1 more citing papers are in PubMed but not listed here.

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

3 authors at 1 institution in 1 country.

Kaspar BurgerSir William Dunn School of Pathology, University of Oxford, South Parks Road, Oxford OX1 3RE, UK.
Margarita SchlackowSir William Dunn School of Pathology, University of Oxford, South Parks Road, Oxford OX1 3RE, UK.
Monika GullerovaSir William Dunn School of Pathology, University of Oxford, South Parks Road, Oxford OX1 3RE, UK.
University of Oxford · GB

Funding

Cancer Research UK 24866Medical Research Council MR/K006606/1
6 · The paper itself

Abstract

DNA is constantly exposed to endogenous and exogenous damage. Various types of DNA repair counteract highly toxic DNA double-strand breaks (DSBs) to maintain genome stability. Recent findings suggest that the human DNA damage response (DDR) utilizes small RNA species, which are produced as long non-coding (nc)RNA precursors and promote recognition of DSBs. However, regulatory principles that control production of such transcripts remain largely elusive. Here we show that the Abelson tyrosine kinase c-Abl/ABL1 causes formation of RNA polymerase II (RNAPII) foci, predominantly phosphorylated at carboxy-terminal domain (CTD) residue Tyr1, at DSBs. CTD Tyr1-phosphorylated RNAPII (CTD Y1P) synthetizes strand-specific, damage-responsive transcripts (DARTs), which trigger formation of double-stranded (ds)RNA intermediates via DNA-RNA hybrid intermediates to promote recruitment of p53-binding protein 1 (53BP1) and Mediator of DNA damage checkpoint 1 (MDC1) to endogenous DSBs. Interference with transcription, c-Abl activity, DNA-RNA hybrid formation or dsRNA processing impairs CTD Y1P foci formation, attenuates DART synthesis and delays recruitment of DDR factors and DSB signalling. Collectively, our data provide novel insight in RNA-dependent DDR by coupling DSB-induced c-Abl activity on RNAPII to generate DARTs for consequent DSB recognition.

Indexed as

Adaptor Proteins, Signal TransducingCell Cycle ProteinsDNADNA-Binding ProteinsDNA Breaks, Double-StrandedDNA DamageDNA RepairDNA ReplicationGenomic InstabilityHumansNuclear ProteinsPhosphorylationProtein DomainsProto-Oncogene Proteins c-ablRNA, Long NoncodingRNA Polymerase IIABL1 protein, humanAdaptor Proteins, Signal TransducingCell Cycle ProteinsDNADNA-Binding ProteinsMDC1 protein, humanNuclear ProteinsProto-Oncogene Proteins c-ablRNA, Long NoncodingRNA Polymerase IITP53BP1 protein, humanTrans-ActivatorsTumor Suppressor p53-Binding Protein 1

Identifiers

PMID30668775
PMCPMC6468493
OpenAlexW2914064467

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.