Evidence map›Paper›PMID 31045206›Full record

ArticleNucleic acids research2019

De novo phosphorylation of H2AX by WSTF regulates transcription-coupled homologous recombination repair.

Jae-Hoon Ji, Sunwoo Min, Sunyoung Chae, Geun-Hyoung Ha, Yonghyeon Kim, Yeon-Ji Park, Chang-Woo Lee, Hyeseong Cho

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 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.0field-weighted citation impact, top 24% 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

19 citing papers in PubMed, 39 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Epigenetic alterations in Myeloid Malignancies.Advances in experimental medicine and biology · 2026
    Review
  5. MOF promotes cisplatin resistance in lung cancer cells by enhancing WSTF acetylation.In vitro cellular & developmental biology. Animal · 2025
    Article
  6. Article
  7. Review
  8. Review
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Long non-coding RNAs: the tentacles of chromatin remodeler complexes.Cellular and molecular life sciences : CMLS · 2021
    Review
  16. The multi-functional eyes absent proteins.Critical reviews in biochemistry and molecular biology · 2020
    Review
  17. Screen identifies DYRK1B network as mediator of transcription repression on damaged chromatin.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  18. Article
  19. Article
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 1 country.

Jae-Hoon JiGenomic Instability Research Center, Ajou University School of Medicine, Suwon, South Korea.
Sunwoo MinDepartment of Biochemistry and Molecular Biology, Ajou University School of Medicine, Suwon, South Korea.
Sunyoung ChaeInstitute of Medical Science, Ajou University School of Medicine, Suwon, South Korea.
Geun-Hyoung HaDepartment of Molecular Cell Biology, Sungkyunkwan University School of Medicine, Suwon, South Korea.
Yonghyeon KimDepartment of Biochemistry and Molecular Biology, Ajou University School of Medicine, Suwon, South Korea.
Yeon-Ji ParkDepartment of Biochemistry and Molecular Biology, Ajou University School of Medicine, Suwon, South Korea.
Chang-Woo LeeDepartment of Molecular Cell Biology, Sungkyunkwan University School of Medicine, Suwon, South Korea.
Hyeseong ChoGenomic Instability Research Center, Ajou University School of Medicine, Suwon, South Korea.
Ajou University · KRSungkyunkwan University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Histone H2AX undergoes a phosphorylation switch from pTyr142 (H2AX-pY142) to pSer139 (γH2AX) in the DNA damage response (DDR); however, the functional role of H2AX-pY142 remains elusive. Here, we report a new layer of regulation involving transcription-coupled H2AX-pY142 in the DDR. We found that constitutive H2AX-pY142 generated by Williams-Beuren syndrome transcription factor (WSTF) interacts with RNA polymerase II (RNAPII) and is associated with RNAPII-mediated active transcription in proliferating cells. Also, removal of pre-existing H2AX-pY142 by ATM-dependent EYA1/3 phosphatases disrupts this association and requires for transcriptional silencing at transcribed active damage sites. The following recovery of H2AX-pY142 via translocation of WSTF to DNA lesions facilitates transcription-coupled homologous recombination (TC-HR) in the G1 phase, whereby RAD51 loading, but not RPA32, utilizes RNAPII-dependent active RNA transcripts as donor templates. We propose that the WSTF-H2AX-RNAPII axis regulates transcription and TC-HR repair to maintain genome integrity.

Indexed as

Recombinational DNA RepairTranscription, GeneticBromodomain Containing ProteinsCell Line, TumorDNA-Binding ProteinsG1 PhaseHEK293 CellsHeLa CellsHistonesHumansIntracellular Signaling Peptides and ProteinsNuclear ProteinsPhosphorylationProtein Tyrosine PhosphatasesRNA Polymerase IITranscription FactorsBAZ1B protein, humanBromodomain Containing ProteinsDNA-Binding ProteinsEYA1 protein, humanEYA3 protein, humanH2AX protein, humanHistonesIntracellular Signaling Peptides and ProteinsNuclear ProteinsProtein Tyrosine PhosphatasesRNA Polymerase IITranscription FactorsTyrosine

Identifiers

PMID31045206
PMCPMC6614800
OpenAlexW2942587013

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.