Evidence map›Paper›PMID 18845678›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2008

Temporal control of the dephosphorylation of Cdk substrates by mitotic exit pathways in budding yeast.

Fengzhi Jin, Hong Liu, Fengshan Liang, Raed Rizkallah, Myra M Hurt, Yanchang Wang

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
2.4field-weighted citation impact, top 12% 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

25 citing papers in PubMed, 39 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. The Multiple Roles of the Cdc14 Phosphatase in Cell Cycle Control.International journal of molecular sciences · 2020
    Review
  6. Review
  7. How the cell cycle clock ticks.Molecular biology of the cell · 2019
    Article
  8. Article
  9. Article
  10. A Clb/Cdk1-mediated regulation of Fkh2 synchronizesNPJ systems biology and applications · 2017
    Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. A quantitative model for cyclin-dependent kinase control of the cell cycle: revisited.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2011
    Review
  20. 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.

Fengzhi JinDepartment of Biomedical Sciences, College of Medicine, Florida State University, 1115 West Call Street, Tallahassee, FL 32306, USA.
Hong Liu
Fengshan Liang
Raed Rizkallah
Myra M Hurt
Yanchang Wang
Florida State University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The temporal phosphorylation of cell cycle-related proteins by cyclin-dependent kinases (Cdks) is critical for the correct order of cell cycle events. In budding yeast, CDC28 encodes the only Cdk and its association with various cyclins governs the temporal phosphorylation of Cdk substrates. S-phase Cdk substrates are phosphorylated earlier than mitotic Cdk substrates, which ensures the sequential order of DNA synthesis and mitosis. However, it remains unclear whether Cdk substrates are dephosphorylated in temporally distinct windows. Cdc14 is a conserved protein phosphatase responsible for the dephosphorylation of Cdk substrates. In budding yeast, FEAR (Cdc14 early anaphase release) and MEN (mitotic exit network) activate phosphatase Cdc14 by promoting its release from the nucleolus in early and late anaphase, respectively. Here, we show that the sequential Cdc14 release and the distinct degradation timing of different cyclins provides the molecular basis for the differential dephosphorylation windows of S-phase and mitotic cyclin substrates. Our data also indicate that FEAR-induced dephosphorylation of S-phase Cdk substrates facilitates anaphase progression, revealing an extra layer of mitotic regulation.

Indexed as

MitosisCell Cycle ProteinsCyclin-Dependent KinasesCyclinsMutationPhosphoprotein PhosphatasesPhosphorylationProtein Tyrosine PhosphatasesSaccharomycetalesSubstrate SpecificityTime FactorsCell Cycle ProteinsCyclin-Dependent KinasesCyclinsPhosphoprotein PhosphatasesProtein Tyrosine Phosphatases

Identifiers

PMID18845678
PMCPMC2570984
OpenAlexW2048054554

What OpenQuestion holds

Textmetadata
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.