Evidence map›Paper›PMID 21680713›Full record

ArticleMolecular biology of the cell2011

Role for casein kinase 1 in the phosphorylation of Claspin on critical residues necessary for the activation of Chk1.

Zheng Meng, Luisa Capalbo, David M Glover, William G Dunphy

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
2.0field-weighted citation impact, top 14% 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

24 citing papers in PubMed, 42 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. The TIMELESS effort for timely DNA replication and protection.Cellular and molecular life sciences : CMLS · 2023
    Review
  5. Article
  6. Article
  7. Review
  8. Review
  9. Article
  10. Implications ofCancers · 2020
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Roles of Chk1 in cell biology and cancer therapy.International journal of cancer · 2014
    Review
  16. Review
  17. Article
  18. Article
  19. Article
  20. Nek1 kinase associates with ATR-ATRIP and primes ATR for efficient DNA damage signaling.Proceedings of the National Academy of Sciences of the United States of America · 2013
    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

4 authors at 2 institutions in 2 countries.

Zheng MengDivision of Biology 147-75, California Institute of Technology, Pasadena, CA 91125, USA.
Luisa Capalbo
David M Glover
William G Dunphy
California Institute of Technology · USUniversity of Cambridge · GB

Funding

Role of ATR in Cell Cycle CheckpointsR01GM070891 · NIGMS · CALIFORNIA INSTITUTE OF TECHNOLOGY · PI DUNPHY, WILLIAM G · 2004 to 2018
$5.7M
ENZYMOLOGY OF MITOSIS PROMOTING FACTOR (MPF)R01GM043974 · NIGMS · CALIFORNIA INSTITUTE OF TECHNOLOGY · PI DUNPHY, WILLIAM G · 1990 to 2022
$4.0M
Enzymology of Mitosis Promoting Factor (MPF)R37GM043974 · NIGMS · CALIFORNIA INSTITUTE OF TECHNOLOGY · PI DUNPHY, WILLIAM G · 2002 to 2011
$4.0M
Biotechnology and Biological Sciences Research CouncilCancer Research UK 11431NIGMS NIH HHS GM-043974NIGMS NIH HHS GM-070891NIGMS NIH HHS R01 GM043974NIGMS NIH HHS R01 GM070891NIGMS NIH HHS R37 GM043974
6 · The paper itself

Abstract

The mediator protein Claspin is critical for the activation of the checkpoint kinase Chk1 during checkpoint responses to stalled replication forks. This function involves the Chk1-activating domain (CKAD) of Claspin, which undergoes phosphorylation on multiple conserved sites. These phosphorylations promote binding of Chk1 to Claspin and ensuing activation of Chk1 by ATR. However, despite the importance of this regulatory process, the kinase responsible for these phosphorylations has remained unknown. By using a multifaceted approach, we have found that casein kinase 1 gamma 1 (CK1γ1) carries out this function. CK1γ1 phosphorylates the CKAD of Claspin efficiently in vitro, and depletion of CK1γ1 from human cells by small interfering RNA (siRNA) results in dramatically diminished phosphorylation of Claspin. Consequently, the siRNA-treated cells display impaired activation of Chk1 and resultant checkpoint defects. These results indicate that CK1γ1 is a novel component of checkpoint responses that controls the interaction of a key checkpoint effector kinase with its cognate mediator protein.

Indexed as

Enzyme ActivationAdaptor Proteins, Signal TransducingAnimalsCasein Kinase ICell Cycle CheckpointsCell LineCheckpoint Kinase 1DNA DamageDrosophila melanogasterDrosophila ProteinsGenes, cdcHumansIsoenzymesPhosphorylationProtein KinasesRNA InterferenceAdaptor Proteins, Signal TransducingCasein Kinase ICheckpoint Kinase 1CHEK1 protein, humanCLSPN protein, humanDrosophila Proteinsgish protein, DrosophilaIsoenzymesProtein Kinases

Identifiers

PMID21680713
PMCPMC3154880
OpenAlexW2005315465

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.