Evidence map›Paper›PMID 24013921›Full record

ArticlePLoS biology2013

The CK2 kinase stabilizes CLOCK and represses its activity in the Drosophila circadian oscillator.

Aron Szabó, Christian Papin, Daniela Zorn, Prishila Ponien, Frank Weber, Thomas Raabe, François Rouyer

Open access · goldAbstract read
In one paragraph

Article in PLoS biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
2.9field-weighted citation impact, top 10% 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

27 citing papers in PubMed, 51 citations in OpenAlex.

  1. Post-Translational Modifications in Animal Circadian Clocks.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Review
  2. Circadian Control of Protein Synthesis.BioEssays : news and reviews in molecular, cellular and developmental biology · 2025
    Review
  3. Review
  4. Alternative splicing ofProceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  5. Alternative splicing ofbioRxiv : the preprint server for biology · 2024
    Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. AMP-Activated Protein Kinase Regulates Circadian Rhythm by Affecting CLOCK inThe Journal of neuroscience : the official journal of the Society for Neuroscience · 2019
    Article
  16. Article
  17. CK1α Collaborates with DOUBLETIME to Regulate PERIOD Function in theThe Journal of neuroscience : the official journal of the Society for Neuroscience · 2018
    Article
  18. Review
  19. Article
  20. Molecular modulators of the circadian clock: lessons from flies and mice.Cellular and molecular life sciences : CMLS · 2017
    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

7 authors at 5 institutions in 2 countries.

Aron SzabóInstitut de Neurobiologie Alfred Fessard, Centre National de la Recherche Scientifique Unité Propre de Recherche 3294, Gif-sur-Yvette, France ; Département de Biologie, Université Paris Sud, Orsay, France.
Christian Papin
Daniela Zorn
Prishila Ponien
Frank Weber
Thomas Raabe
François Rouyer
Heidelberg University · DELaboratoire de Neurobiologie Cellulaire et Moléculaire · FRInstitut de Chimie des Substances Naturelles · FRUniversité Paris-Sud · FRUniversity of Würzburg · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Phosphorylation is a pivotal regulatory mechanism for protein stability and activity in circadian clocks regardless of their evolutionary origin. It determines the speed and strength of molecular oscillations by acting on transcriptional activators and their repressors, which form negative feedback loops. In Drosophila, the CK2 kinase phosphorylates and destabilizes the PERIOD (PER) and TIMELESS (TIM) proteins, which inhibit CLOCK (CLK) transcriptional activity. Here we show that CK2 also targets the CLK activator directly. Downregulating the activity of the catalytic α subunit of CK2 induces CLK degradation, even in the absence of PER and TIM. Unexpectedly, the regulatory β subunit of the CK2 holoenzyme is not required for the regulation of CLK stability. In addition, downregulation of CK2α activity decreases CLK phosphorylation and increases per and tim transcription. These results indicate that CK2 inhibits CLK degradation while reducing its activity. Since the CK1 kinase promotes CLK degradation, we suggest that CLK stability and transcriptional activity result from counteracting effects of CK1 and CK2.

Indexed as

AnimalsCircadian RhythmCLOCK ProteinsDrosophilaDrosophila ProteinsPhosphorylationCLOCK ProteinsDrosophila Proteinstim protein, Drosophila

Identifiers

PMID24013921
PMCPMC3754892
OpenAlexW2044288080

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.