Evidence map›Paper›PMID 38039132›Full record

ArticleCell reports2023

The phosphorylated trimeric SOSS1 complex and RNA polymerase II trigger liquid-liquid phase separation at double-strand breaks.

Qilin Long, Marek Sebesta, Katerina Sedova, Vojtech Haluza, Adele Alagia, Zhichao Liu, Richard Stefl, Monika Gullerova

Open access · goldAbstract read
In one paragraph

Article in Cell reports, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed, 1 pooled it
2.8field-weighted citation impact, top 9% 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

15 citing papers in PubMed, 1 synthesis or guideline pooled it, 18 citations in OpenAlex.

  1. Pooled it
  2. TRIM21 inhibition alleviates acute kidney injury by promoting INTS3-associated DNA damage repair.Apoptosis : an international journal on programmed cell death · 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 2 institutions in 2 countries.

Qilin LongSir William Dunn School of Pathology, University of Oxford, South Parks Road, Oxford OX1 3RE, UK.
Marek SebestaCentral European Institute of Technology (CEITEC), Masaryk University, 62500 Brno, Czech Republic. Electronic address: marek.sebesta@ceitec.muni.cz.
Katerina SedovaCentral European Institute of Technology (CEITEC), Masaryk University, 62500 Brno, Czech Republic.
Vojtech HaluzaCentral European Institute of Technology (CEITEC), Masaryk University, 62500 Brno, Czech Republic.
Adele AlagiaSir William Dunn School of Pathology, University of Oxford, South Parks Road, Oxford OX1 3RE, UK.
Zhichao LiuSir William Dunn School of Pathology, University of Oxford, South Parks Road, Oxford OX1 3RE, UK.
Richard SteflCentral European Institute of Technology (CEITEC), Masaryk University, 62500 Brno, Czech Republic; National Center for Biomolecular Research, Faculty of Science, Masaryk University, 62500 Brno, Czech Republic.
Monika GullerovaSir William Dunn School of Pathology, University of Oxford, South Parks Road, Oxford OX1 3RE, UK. Electronic address: monika.gullerova@path.ox.ac.uk.
Central European Institute of Technology · CZUniversity of Oxford · GB

Funding

Cancer Research UK 24866Cancer Research UK 26737
6 · The paper itself

Abstract

Double-strand breaks (DSBs) are the most severe type of DNA damage. Previously, we demonstrated that RNA polymerase II (RNAPII) phosphorylated at the tyrosine 1 (Y1P) residue of its C-terminal domain (CTD) generates RNAs at DSBs. However, the regulation of transcription at DSBs remains enigmatic. Here, we show that the damage-activated tyrosine kinase c-Abl phosphorylates hSSB1, enabling its interaction with Y1P RNAPII at DSBs. Furthermore, the trimeric SOSS1 complex, consisting of hSSB1, INTS3, and c9orf80, binds to Y1P RNAPII in response to DNA damage in an R-loop-dependent manner. Specifically, hSSB1, as a part of the trimeric SOSS1 complex, exhibits a strong affinity for R-loops, even in the presence of replication protein A (RPA). Our in vitro and in vivo data reveal that the SOSS1 complex and RNAPII form dynamic liquid-like repair compartments at DSBs. Depletion of the SOSS1 complex impairs DNA repair, underscoring its biological role in the R-loop-dependent DNA damage response.

Indexed as

DNA-Binding ProteinsRNA Polymerase IIDNA DamageDNA RepairPhase SeparationDNA-Binding ProteinsRNA Polymerase IIc-Abl kinaseCP: Molecular biologyDNA damageDNA:RNA hybridshSSB1LLPSphase-separationphosphorylationR-loopsRNA polymerase IISOSS1 complex

Identifiers

PMID38039132
PMCPMC7617797
OpenAlexW4389202163

What OpenQuestion holds

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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.