Evidence map›Paper›PMID 21658602›Full record

ArticleMolecular cell2011

Dynamics of Cdk1 substrate specificity during the cell cycle.

Mardo Kõivomägi, Ervin Valk, Rainis Venta, Anna Iofik, Martin Lepiku, David O Morgan, Mart Loog

Open access · hybridAbstract read
In one paragraph

Article in Molecular cell, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 110 papers.

0numbers the graph read from it
0cells of the map it votes in
110citing papers in PubMed
4.8field-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

110 citing papers in PubMed, 162 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. 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
  5. Article
  6. Article
  7. Article
  8. Article
  9. SHARK-capture identifies functional motifs in intrinsically disordered protein regions.Protein science : a publication of the Protein Society · 2025
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. TOR Complex 1: Orchestrating Nutrient Signaling and Cell Cycle Progression.International journal of molecular sciences · 2023
    Review
  17. Article
  18. Article
  19. Article
  20. Article

50 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

7 authors at 2 institutions in 2 countries.

Mardo KõivomägiInstitute of Technology, University of Tartu, Tartu 50411, Estonia. mart.loog@ut.ee
Ervin Valk
Rainis Venta
Anna Iofik
Martin Lepiku
David O Morgan
Mart Loog
University of Tartu · EEUniversity of California, San Francisco · US

Funding

Cell Cycle Control by Cyclin-Dependent KinasesR01GM069901 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI MORGAN, DAVID OWEN · 2004 to 2015
$3.6M
Howard Hughes Medical InstituteNIGMS NIH HHS R01 GM069901Wellcome Trust 079014/Z/06/Z
6 · The paper itself

Abstract

Cdk specificity is determined by the intrinsic selectivity of the active site and by substrate docking sites on the cyclin subunit. There is a long-standing debate about the relative importance of these factors in the timing of Cdk1 substrate phosphorylation. We analyzed major budding yeast cyclins (the G1/S-cyclin Cln2, S-cyclin Clb5, G2/M-cyclin Clb3, and M-cyclin Clb2) and found that the activity of Cdk1 toward the consensus motif increased gradually in the sequence Cln2-Clb5-Clb3-Clb2, in parallel with cell cycle progression. Further, we identified a docking element that compensates for the weak intrinsic specificity of Cln2 toward G1-specific targets. In addition, Cln2-Cdk1 showed distinct consensus site specificity, suggesting that cyclins do not merely activate Cdk1 but also modulate its active-site specificity. Finally, we identified several Cln2-, Clb3-, and Clb2-specific Cdk1 targets. We propose that robust timing and ordering of cell cycle events depend on gradual changes in the substrate specificity of Cdk1.

Indexed as

Cell CycleAmino Acid MotifsBinding SitesCDC2 Protein KinaseConsensus SequenceHydrophobic and Hydrophilic InteractionsModels, BiologicalSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSubstrate SpecificityCDC2 Protein KinaseSaccharomyces cerevisiae Proteins

Identifiers

PMID21658602
PMCPMC3115021
OpenAlexW2092062544

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.