Evidence map›Paper›PMID 24074952›Full record

ArticleMolecular cell2013

Phosphorylation-dependent assembly and coordination of the DNA damage checkpoint apparatus by Rad4(TopBP1).

Meng Qu, Mathieu Rappas, Christopher P Wardlaw, Valerie Garcia, Jing-Yi Ren, Matthew Day, Antony M Carr, Antony W Oliver, Li-Lin Du, Laurence H Pearl

Open access · bronzeAbstract read
In one paragraph

Article in Molecular cell, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.6field-weighted citation impact, top 16% 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

21 citing papers in PubMed, 31 citations in OpenAlex.

  1. Article
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  7. Structure and regulation of human epithelial cell transforming 2 protein.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  8. Article
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  10. Article
  11. A New BRCT Binding Mode in TopBP1-BLM Helicase Interaction.Structure (London, England : 1993) · 2017
    Article
  12. Structural Insight into BLM Recognition by TopBP1.Structure (London, England : 1993) · 2017
    Article
  13. Review
  14. Article
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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

10 authors at 2 institutions in 2 countries.

Meng Qu *National Institute of Biological Sciences, 7 Science Park Road, ZGC Life Science Park, Beijing 102206, China.
Mathieu Rappas *Cancer Research UK DNA Repair Enzymes Group, Genome Damage and Stability Centre, School of Life Sciences, University of Sussex, Falmer, BN1 9RQ, UK.
Christopher P Wardlaw *MRC Genome Damage and Stability Centre, School of Life Sciences, University of Sussex, Falmer, BN1 9RQ, UK.
Valerie GarciaMRC Genome Damage and Stability Centre, School of Life Sciences, University of Sussex, Falmer, BN1 9RQ, UK.
Jing-Yi RenNational Institute of Biological Sciences, 7 Science Park Road, ZGC Life Science Park, Beijing 102206, China.
Matthew DayCancer Research UK DNA Repair Enzymes Group, Genome Damage and Stability Centre, School of Life Sciences, University of Sussex, Falmer, BN1 9RQ, UK.
Antony M CarrMRC Genome Damage and Stability Centre, School of Life Sciences, University of Sussex, Falmer, BN1 9RQ, UK.
Antony W OliverCancer Research UK DNA Repair Enzymes Group, Genome Damage and Stability Centre, School of Life Sciences, University of Sussex, Falmer, BN1 9RQ, UK.
Li-Lin DuNational Institute of Biological Sciences, 7 Science Park Road, ZGC Life Science Park, Beijing 102206, China.
Laurence H PearlCancer Research UK DNA Repair Enzymes Group, Genome Damage and Stability Centre, School of Life Sciences, University of Sussex, Falmer, BN1 9RQ, UK.
Cancer Research UK · GBNational Institute of Biological Sciences, Beijing · CN

Funding

Cancer Research UK 14532Cancer Research UK A14532Cancer Research UK C302/A14532Cancer Research UK C5514/A10722Medical Research Council G1100074Wellcome Trust 092933
6 · The paper itself

Abstract

The BRCT-domain protein Rad4(TopBP1) facilitates activation of the DNA damage checkpoint in Schizosaccharomyces pombe by physically coupling the Rad9-Rad1-Hus1 clamp, the Rad3(ATR) -Rad26(ATRIP) kinase complex, and the Crb2(53BP1) mediator. We have now determined crystal structures of the BRCT repeats of Rad4(TopBP1), revealing a distinctive domain architecture, and characterized their phosphorylation-dependent interactions with Rad9 and Crb2(53BP1). We identify a cluster of phosphorylation sites in the N-terminal region of Crb2(53BP1) that mediate interaction with Rad4(TopBP1) and reveal a hierarchical phosphorylation mechanism in which phosphorylation of Crb2(53BP1) residues Thr215 and Thr235 promotes phosphorylation of the noncanonical Thr187 site by scaffolding cyclin-dependent kinase (CDK) recruitment. Finally, we show that the simultaneous interaction of a single Rad4(TopBP1) molecule with both Thr187 phosphorylation sites in a Crb2(53BP1) dimer is essential for establishing the DNA damage checkpoint.

Indexed as

DNA-Binding ProteinsTransglutaminasesBinding SitesCell Cycle ProteinsCrystallography, X-RayDNA DamageNuclear ProteinsPhosphorylationProtein BindingProtein Structure, TertiarySchizosaccharomycesSchizosaccharomyces pombe ProteinsCell Cycle ProteinsCrb2 protein, S pombeDNA-Binding ProteinsNuclear ProteinsRAD4 protein, S pomberad9 proteinSchizosaccharomyces pombe ProteinsTransglutaminases

Identifiers

PMID24074952
PMCPMC4944838
OpenAlexW2132345481

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.