Evidence map›Paper›PMID 22424773›Full record

ArticleMolecular cell2012

Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.

Petra Beli, Natalia Lukashchuk, Sebastian A Wagner, Brian T Weinert, Jesper V Olsen, Linda Baskcomb, Matthias Mann, Stephen P Jackson, Chunaram Choudhary

Open access · bronzeAbstract read
In one paragraph

Article in Molecular cell, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 218 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
218citing papers in PubMed, 1 pooled it
13.0field-weighted citation impact, top 1% 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

218 citing papers in PubMed, 1 synthesis or guideline pooled it, 342 citations in OpenAlex.

  1. Pooled it
  2. SMARCD1 and Its Functional Relevance in SWI/SNF and Cancer.International journal of molecular sciences · 2026
    Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Phosphoregulation of RAD51AP1 function in homology-directed repair.bioRxiv : the preprint server for biology · 2025
    Article
  10. Review
  11. Article
  12. Posttranslational Regulation of Mammalian Sulfur Amino Acid Metabolism.International journal of molecular sciences · 2025
    Review
  13. Article
  14. Regulation of the microprocessor by post-translational modifications.Frontiers in cell and developmental biology · 2025
    Review
  15. Article
  16. Article
  17. Review
  18. Article
  19. DNA damage-induced proteasome phosphorylation controls substrate recognition and facilitates DNA repair.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  20. Article

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

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

9 authors at 2 institutions in 3 countries.

Petra BeliThe NNF Center for Protein Research, University of Copenhagen, Blegdamsvej 3B, DK-2200 Copenhagen, Denmark.
Natalia Lukashchuk
Sebastian A Wagner
Brian T Weinert
Jesper V Olsen
Linda Baskcomb
Matthias Mann
Stephen P Jackson
Chunaram Choudhary
University of Copenhagen · DKUniversity of Cambridge · GB

Funding

Cancer Research UK 11224Cancer Research UK A11224Cancer Research UK C11628/A6535Cancer Research UK C6/A11224Wellcome Trust 075661Wellcome Trust 092096
6 · The paper itself

Abstract

The regulatory networks of the DNA damage response (DDR) encompass many proteins and posttranslational modifications. Here, we use mass spectrometry-based proteomics to analyze the systems-wide response to DNA damage by parallel quantification of the DDR-regulated phosphoproteome, acetylome, and proteome. We show that phosphorylation-dependent signaling networks are regulated more strongly compared to acetylation. Among the phosphorylated proteins identified are many putative substrates of DNA-PK, ATM, and ATR kinases, but a majority of phosphorylated proteins do not share the ATM/ATR/DNA-PK target consensus motif, suggesting an important role of downstream kinases in amplifying DDR signals. We show that the splicing-regulator phosphatase PPM1G is recruited to sites of DNA damage, while the splicing-associated protein THRAP3 is excluded from these regions. Moreover, THRAP3 depletion causes cellular hypersensitivity to DNA-damaging agents. Collectively, these data broaden our knowledge of DNA damage signaling networks and highlight an important link between RNA metabolism and DNA repair.

Indexed as

DNA DamageDNA RepairCell Line, TumorDNA-Binding ProteinsHeLa CellsHumansPhosphoprotein PhosphatasesPhosphorylationProtein Phosphatase 2CProteomicsSignal TransductionTranscription FactorsTumor Necrosis Factor-alphaDNA-Binding ProteinsPhosphoprotein PhosphatasesPPM1G protein, humanProtein Phosphatase 2CTHRAP3 protein, humanTranscription FactorsTumor Necrosis Factor-alpha

Identifiers

PMID22424773
PMCPMC3565437
OpenAlexW1998163656

What OpenQuestion holds

Textmetadata
LicenceTDM
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.