Evidence map›Paper›PMID 24186061›Full record

ArticleNature structural & molecular biology2013

Multisite phosphorylation networks as signal processors for Cdk1.

Mardo Kõivomägi, Mihkel Ord, Anna Iofik, Ervin Valk, Rainis Venta, Ilona Faustova, Rait Kivi, Eva Rose M Balog, Seth M Rubin, Mart Loog

Open access · greenAbstract read
In one paragraph

Article in Nature structural & molecular biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 92 papers.

0numbers the graph read from it
0cells of the map it votes in
92citing papers in PubMed
5.4field-weighted citation impact, top 4% 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

92 citing papers in PubMed, 134 citations in OpenAlex.

  1. Review
  2. Article
  3. Decoding Cdk1 control: from mitotic thresholds to meiotic specificity.Chromosome research : an international journal on the molecular, supramolecular and evolutionary aspects of chromosome biology · 2026
    Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Dynamic phosphorylation of Hcm1 promotes fitness in chronic stress.bioRxiv : the preprint server for biology · 2025
    Article
  11. SHARK-capture identifies functional motifs in intrinsically disordered protein regions.Protein science : a publication of the Protein Society · 2025
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Review
  19. Article
  20. Article

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

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.

Mardo KõivomägiInstitute of Technology, University of Tartu, Tartu, Estonia.
Mihkel Ord
Anna Iofik
Ervin Valk
Rainis Venta
Ilona Faustova
Rait Kivi
Eva Rose M Balog
Seth M Rubin
Mart Loog
University of Tartu · EEUniversity of California, Santa Cruz · US

Funding

Training Program/Molecular/Cell/Developmental BiologyT32GM008646 · NIGMS · UNIVERSITY OF CALIFORNIA SANTA CRUZ · PI STROME, SUSAN · 1999 to 2018
$3.7M
Howard Hughes Medical Institute 1253Wellcome Trust 079014Wellcome Trust 079014/Z/06/Z
6 · The paper itself

Abstract

The order and timing of cell-cycle events is controlled by changing substrate specificity and different activity thresholds of cyclin-dependent kinases (CDKs). However, it is not understood how a single protein kinase can trigger hundreds of switches in a sufficiently time-resolved fashion. We show that cyclin-Cdk1-Cks1-dependent phosphorylation of multisite targets in Saccharomyces cerevisiae is controlled by key substrate parameters including distances between phosphorylation sites, distribution of serines and threonines as phosphoacceptors and positioning of cyclin-docking motifs. The component mediating the key interactions in this process is Cks1, the phosphoadaptor subunit of the cyclin-Cdk1-Cks1 complex. We propose that variation of these parameters within networks of phosphorylation sites in different targets provides a wide range of possibilities for differential amplification of Cdk1 signals, thus providing a mechanism to generate a wide range of thresholds in the cell cycle.

Indexed as

Adaptor Proteins, Signal TransducingCDC2 Protein KinaseCell Cycle ProteinsCyclin BCyclinsPhosphorylationPhosphoserinePhosphothreonineSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSignal TransductionAdaptor Proteins, Signal TransducingCDC2 Protein KinaseCell Cycle ProteinsCKS1 protein, S cerevisiaeCLB5 protein, S cerevisiaeCLN2 protein, S cerevisiaeCyclin BCyclinsPhosphoserinePhosphothreonineSaccharomyces cerevisiae Proteins

Identifiers

PMID24186061
PMCPMC3855452
OpenAlexW2056658675

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.