Evidence map›Paper›PMID 23593009›Full record

ArticlePLoS genetics2013

Site-specific phosphorylation of the DNA damage response mediator rad9 by cyclin-dependent kinases regulates activation of checkpoint kinase 1.

Carla Manuela Abreu, Ramesh Kumar, Danielle Hamilton, Andrew William Dawdy, Kevin Creavin, Sarah Eivers, Karen Finn, Jeremy Lynn Balsbaugh, Rosemary O'Connor, Patrick A Kiely and 4 more

Open access · goldAbstract read
In one paragraph

Article in PLoS genetics, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.5field-weighted citation impact, top 18% 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

18 citing papers in PubMed, 27 citations in OpenAlex.

  1. Review
  2. DNA Damage and Replication Stress Checkpoints.Annual review of biochemistry · 2025
    Review
  3. Article
  4. Article
  5. Review
  6. Checkpoint Responses to DNA Double-Strand Breaks.Annual review of biochemistry · 2020
    Review
  7. Article
  8. Article
  9. Review
  10. Article
  11. Mechanisms and regulation of DNA replication initiation in eukaryotes.Critical reviews in biochemistry and molecular biology · 2017
    Review
  12. TOPBP1The Journal of cell biology · 2017
    Article
  13. Review
  14. Article
  15. Review
  16. Regulation of Elg1 activity by phosphorylation.Cell cycle (Georgetown, Tex.) · 2015
    Article
  17. Review
  18. Review
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

14 authors at 4 institutions in 2 countries.

Carla Manuela AbreuCentre for Chromosome Biology, School of Natural Science, National University of Ireland Galway, Galway, Ireland.
Ramesh Kumar
Danielle Hamilton
Andrew William Dawdy
Kevin Creavin
Sarah Eivers
Karen Finn
Jeremy Lynn Balsbaugh
Rosemary O'Connor
Patrick A Kiely
Jeffrey Shabanowitz
Donald F Hunt
Muriel Grenon
Noel Francis Lowndes
Ollscoil na Gaillimhe – University of Galway · IEUniversity of Virginia · USUniversity College Cork · IEUniversity of Limerick · IE

Funding

PROTEIN SEQUENCING BY TANDEM MASS SPECTROMETRYR01GM037537 · NIGMS · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI HUNT, DONALD F · 1987 to 2023
$17.8M
NIGMS NIH HHS GM037537NIGMS NIH HHS R01 GM037537
6 · The paper itself

Abstract

The mediators of the DNA damage response (DDR) are highly phosphorylated by kinases that control cell proliferation, but little is known about the role of this regulation. Here we show that cell cycle phosphorylation of the prototypical DDR mediator Saccharomyces cerevisiae Rad9 depends on cyclin-dependent kinase (CDK) complexes. We find that a specific G2/M form of Cdc28 can phosphorylate in vitro the N-terminal region of Rad9 on nine consensus CDK phosphorylation sites. We show that the integrity of CDK consensus sites and the activity of Cdc28 are required for both the activation of the Chk1 checkpoint kinase and its interaction with Rad9. We have identified T125 and T143 as important residues in Rad9 for this Rad9/Chk1 interaction. Phosphorylation of T143 is the most important feature promoting Rad9/Chk1 interaction, while the much more abundant phosphorylation of the neighbouring T125 residue impedes the Rad9/Chk1 interaction. We suggest a novel model for Chk1 activation where Cdc28 regulates the constitutive interaction of Rad9 and Chk1. The Rad9/Chk1 complex is then recruited at sites of DNA damage where activation of Chk1 requires additional DDR-specific protein kinases.

Indexed as

DNA DamageCDC28 Protein Kinase, S cerevisiaeCell Cycle CheckpointsCell Cycle ProteinsCell ProliferationCheckpoint Kinase 1Enzyme ActivationMutationPhosphorylationProtein BindingProtein KinasesSaccharomyces cerevisiaeS PhaseCDC28 Protein Kinase, S cerevisiaeCell Cycle ProteinsCheckpoint Kinase 1Protein Kinasesrad9 protein

Identifiers

PMID23593009
PMCPMC3616908
OpenAlexW2082048987

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.