Evidence map›Paper›PMID 33210757›Full record

ArticleThe EMBO journal2021

A new linear cyclin docking motif that mediates exclusively S-phase CDK-specific signaling.

Ilona Faustova, Luka Bulatovic, Frida Matiyevskaya, Ervin Valk, Mihkel Örd, Mart Loog

Open access · hybridAbstract read
In one paragraph

Article in The EMBO journal, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
4.0field-weighted citation impact, top 6% 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

22 citing papers in PubMed, 35 citations in OpenAlex.

  1. Article
  2. 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
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  17. Bipartite binding of the N terminus of Skp2 to cyclin A.Structure (London, England : 1993) · 2021
    Article
  18. Docking to a Basic Helix Promotes Specific Phosphorylation by G1-Cdk1.International journal of molecular sciences · 2021
    Article
  19. Article
  20. Budding yeast relies on GScience advances · 2021
    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

6 authors at 1 institution in 1 country.

Ilona FaustovaInstitute of Technology, University of Tartu, Tartu, Estonia.
Luka BulatovicInstitute of Technology, University of Tartu, Tartu, Estonia.
Frida MatiyevskayaInstitute of Technology, University of Tartu, Tartu, Estonia.
Ervin ValkInstitute of Technology, University of Tartu, Tartu, Estonia.
Mihkel ÖrdInstitute of Technology, University of Tartu, Tartu, Estonia.
Mart LoogInstitute of Technology, University of Tartu, Tartu, Estonia.ORCID 0000-0003-1330-8453
University of Tartu · EE

Funding

EC | H2020 | H2020 Priority Excellent Science | H2020 European Research Council (ERC) 649124Eesti Teadusagentuur PRG550Sihtasutus Archimedes (Archimedes Foundation) TK143
6 · The paper itself

Abstract

Cyclin-dependent kinases (CDKs), the master regulators of cell division, are activated by different cyclins at different cell cycle stages. In addition to being activators of CDKs, cyclins recognize various linear motifs to target CDK activity to specific proteins. We uncovered a cyclin docking motif, NLxxxL, that contributes to phosphorylation-dependent degradation of the CDK inhibitor Far1 at the G1/S stage in the yeast Saccharomyces cerevisiae. This motif is recognized exclusively by S-phase CDK (S-CDK) Clb5/6-Cdc28 and is considerably more potent than the conventional RxL docking motif. The NLxxxL and RxL motifs were found to overlap in some target proteins, suggesting that cyclin docking motifs can evolve to switch from one to another for fine-tuning of cell cycle events. Using time-lapse fluorescence microscopy, we show how different docking connections temporally control phosphorylation-driven target degradation. This also revealed a differential function of the phosphoadaptor protein Cks1, as Cks1 docking potentiated degron phosphorylation of RxL-containing but not of NLxxxL-containing substrates. The NLxxxL motif was found to govern S-cyclin-specificity in multiple yeast CDK targets including Fin1, Lif1, and Slx4, suggesting its wider importance.

Indexed as

Amino Acid SequenceCell Cycle ProteinsCyclin-Dependent KinasesCyclinsPhosphorylationSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSignal TransductionS PhaseCell Cycle ProteinsCyclin-Dependent KinasesCyclinsSaccharomyces cerevisiae Proteinscell cyclecyclin-dependent kinasecyclin dockingphosphorylationshort linear motifs

Identifiers

PMID33210757
PMCPMC7809796
OpenAlexW3105126735

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.