Evidence map›Paper›PMID 32296067›Full record

ArticleNature communications2020

A processive phosphorylation circuit with multiple kinase inputs and mutually diversional routes controls G1/S decision.

Rainis Venta, Ervin Valk, Mihkel Örd, Oleg Košik, Kaur Pääbo, Artemi Maljavin, Rait Kivi, Ilona Faustova, Nastassia Shtaida, Martin Lepiku and 4 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.7field-weighted citation impact, top 18% 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

13 citing papers in PubMed, 23 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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  5. Article
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  7. Review
  8. TOR Complex 1: Orchestrating Nutrient Signaling and Cell Cycle Progression.International journal of molecular sciences · 2023
    Review
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  10. Article
  11. Article
  12. Review
  13. 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

14 authors at 2 institutions in 2 countries.

Rainis VentaInstitute of Technology, University of Tartu, Tartu, 50411, Estonia.
Ervin ValkInstitute of Technology, University of Tartu, Tartu, 50411, Estonia.
Mihkel ÖrdInstitute of Technology, University of Tartu, Tartu, 50411, Estonia.ORCID http://orcid.org/0000-0003-0454-7241
Oleg KošikInstitute of Technology, University of Tartu, Tartu, 50411, Estonia.
Kaur PääboInstitute of Technology, University of Tartu, Tartu, 50411, Estonia.
Artemi MaljavinInstitute of Technology, University of Tartu, Tartu, 50411, Estonia.
Rait KiviInstitute of Technology, University of Tartu, Tartu, 50411, Estonia.
Ilona FaustovaInstitute of Technology, University of Tartu, Tartu, 50411, Estonia.
Nastassia ShtaidaInstitute of Technology, University of Tartu, Tartu, 50411, Estonia.
Martin LepikuInstitute of Technology, University of Tartu, Tartu, 50411, Estonia.
Kaidi MöllInstitute of Technology, University of Tartu, Tartu, 50411, Estonia.
Andreas DoncicDepartment of Biology, Stanford University, Stanford, CA, 94305, USA.
Mardo KõivomägiInstitute of Technology, University of Tartu, Tartu, 50411, Estonia.
Mart LoogInstitute of Technology, University of Tartu, Tartu, 50411, Estonia. mart.loog@ut.ee.ORCID http://orcid.org/0000-0003-1330-8453
University of Tartu · EEStanford University · US

Funding

Mechanisms of restriction point response to dynamic growth factor signalsR01GM092925 · NIGMS · STANFORD UNIVERSITY · PI SKOTHEIM, JAN M · 2010 to 2018
$2.8M
NIGMS NIH HHS R01 GM092925
6 · The paper itself

Abstract

Studies on multisite phosphorylation networks of cyclin-dependent kinase (CDK) targets have opened a new level of signaling complexity by revealing signal processing routes encoded into disordered proteins. A model target, the CDK inhibitor Sic1, contains linear phosphorylation motifs, docking sites, and phosphodegrons to empower an N-to-C terminally directed phosphorylation process. Here, we uncover a signal processing mechanism involving multi-step competition between mutually diversional phosphorylation routes within the S-CDK-Sic1 inhibitory complex. Intracomplex phosphorylation plays a direct role in controlling Sic1 degradation, and provides a mechanism to sequentially integrate both the G1- and S-CDK activities while keeping S-CDK inhibited towards other targets. The competing phosphorylation routes prevent premature Sic1 degradation and demonstrate how integration of MAPK from the pheromone pathway allows one to tune the competition of alternative phosphorylation paths. The mutually diversional phosphorylation circuits may be a general way for processing multiple kinase signals to coordinate cellular decisions in eukaryotes.

Indexed as

Blotting, WesternCell DivisionCyclin-Dependent KinasesEscherichia coliG1 PhaseImmunoprecipitationMass SpectrometryPhosphorylationSignal TransductionS PhaseCyclin-Dependent Kinases

Identifiers

PMID32296067
PMCPMC7160111
OpenAlexW3016794476

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.