Evidence map›Paper›PMID 30455435›Full record

ArticleNature structural & molecular biology2018

A PxL motif promotes timely cell cycle substrate dephosphorylation by the Cdc14 phosphatase.

Meghna Kataria, Stephane Mouilleron, Moon-Hyeong Seo, Carles Corbi-Verge, Philip M Kim, Frank Uhlmann

Abstract read
In one paragraph

Article in Nature structural & molecular biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
–field-weighted citation impact
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

26 citing papers in PubMed.

  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
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Docking to a Basic Helix Promotes Specific Phosphorylation by G1-Cdk1.International journal of molecular sciences · 2021
    Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. The Multiple Roles of the Cdc14 Phosphatase in Cell Cycle Control.International journal of molecular sciences · 2020
    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

6 authors.

Meghna KatariaChromosome Segregation Laboratory, The Francis Crick Institute, London, UK.ORCID http://orcid.org/0000-0001-7868-3786
Stephane MouilleronStructural Biology Science Technology Platform, The Francis Crick Institute, London, UK.ORCID http://orcid.org/0000-0001-7977-6298
Moon-Hyeong SeoTerrence Donnelly Centre for Cellular and Biomolecular Research, University of Toronto, Toronto, Ontario, Canada.
Carles Corbi-VergeTerrence Donnelly Centre for Cellular and Biomolecular Research, University of Toronto, Toronto, Ontario, Canada.
Philip M KimTerrence Donnelly Centre for Cellular and Biomolecular Research, University of Toronto, Toronto, Ontario, Canada.
Frank UhlmannChromosome Segregation Laboratory, The Francis Crick Institute, London, UK. frank.uhlmann@crick.ac.uk.ORCID http://orcid.org/0000-0002-3527-6619

Funding

Wellcome Trust FC001198
6 · The paper itself

Abstract

The cell division cycle consists of a series of temporally ordered events. Cell cycle kinases and phosphatases provide key regulatory input, but how the correct substrate phosphorylation and dephosphorylation timing is achieved is incompletely understood. Here we identify a PxL substrate recognition motif that instructs dephosphorylation by the budding yeast Cdc14 phosphatase during mitotic exit. The PxL motif was prevalent in Cdc14-binding peptides enriched in a phage display screen of native disordered protein regions. PxL motif removal from the Cdc14 substrate Cbk1 delays its dephosphorylation, whereas addition of the motif advances dephosphorylation of otherwise late Cdc14 substrates. Crystal structures of Cdc14 bound to three PxL motif substrate peptides provide a molecular explanation for PxL motif recognition on the phosphatase surface. Our results illustrate the sophistication of phosphatase-substrate interactions and identify them as an important determinant of ordered cell cycle progression.

Indexed as

Cell DivisionAmino Acid MotifsCell Cycle ProteinsMitosisModels, MolecularPhosphorylationProtein Tyrosine PhosphatasesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence Analysis, ProteinCDC14 protein, S cerevisiaeCell Cycle ProteinsProtein Tyrosine PhosphatasesSaccharomyces cerevisiae Proteins

Identifiers

PMID30455435
PMCPMC6292506

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.