Evidence map›Paper›PMID 24319056›Full record

ArticleMolecular & cellular proteomics : MCP2014

Global analysis of cdc14 dephosphorylation sites reveals essential regulatory role in mitosis and cytokinesis.

Li Kao, Yi-Ting Wang, Yu-Chen Chen, Shun-Fu Tseng, Jia-Cin Jhang, Yu-Ju Chen, Shu-Chun Teng

Open access · hybridAbstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
0.8field-weighted citation impact, top 30% 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

20 citing papers in PubMed, 27 citations in OpenAlex.

  1. Article
  2. Article
  3. Analog-sensitive Cdk1 as a tool to study mitotic exit: protein phosphatase 1 is required downstream from Cdk1 inactivation in budding yeast.Chromosome research : an international journal on the molecular, supramolecular and evolutionary aspects of chromosome biology · 2023
    Article
  4. Article
  5. GScience (New York, N.Y.) · 2021
    Article
  6. Review
  7. Hog1 activation delays mitotic exit via phosphorylation of Net1.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  8. The Multiple Roles of the Cdc14 Phosphatase in Cell Cycle Control.International journal of molecular sciences · 2020
    Review
  9. Review
  10. Article
  11. Article
  12. Review
  13. Article
  14. TheFrontiers in cellular and infection microbiology · 2018
    Article
  15. Article
  16. Article
  17. APC/CScientific reports · 2016
    Article
  18. Synthetic physical interactions map kinetochore regulators and regions sensitive to constitutive Cdc14 localization.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  19. Article
  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

7 authors at 2 institutions in 1 country.

Li KaoDepartment of Microbiology, College of Medicine, National Taiwan University, Taipei 10051, Taiwan;
Yi-Ting Wang
Yu-Chen Chen
Shun-Fu Tseng
Jia-Cin Jhang
Yu-Ju Chen
Shu-Chun Teng
National Taiwan University · TWInstitute of Molecular Biology, Academia Sinica · TW

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Degradation of the M phase cyclins triggers the exit from M phase. Cdc14 is the major phosphatase required for the exit from the M phase. One of the functions of Cdc14 is to dephosphorylate and activate the Cdh1/APC/C complex, resulting in the degradation of the M phase cyclins. However, other crucial targets of Cdc14 for mitosis and cytokinesis remain to be elucidated. Here we systematically analyzed the positions of dephosphorylation sites for Cdc14 in the budding yeast Saccharomyces cerevisiae. Quantitative mass spectrometry identified a total of 835 dephosphorylation sites on 455 potential Cdc14 substrates in vivo. We validated two events, and through functional studies we discovered that Cdc14-mediated dephosphorylation of Smc4 and Bud3 is essential for proper mitosis and cytokinesis, respectively. These results provide insight into the Cdc14-mediated pathways for exiting the M phase.

Indexed as

CytokinesisMitosisBinding SitesCell Cycle ProteinsChromosomal Proteins, Non-HistoneChromosome SegregationDNA PackagingPhosphoproteinsPhosphorylationProtein Processing, Post-TranslationalProtein Tyrosine PhosphatasesProteomeSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTandem Mass SpectrometryBUD3 protein, S cerevisiaeCDC14 protein, S cerevisiaeCell Cycle ProteinsChromosomal Proteins, Non-HistonePhosphoproteinsProtein Tyrosine PhosphatasesProteomeSaccharomyces cerevisiae ProteinsSMC4 protein, S cerevisiae

Identifiers

PMID24319056
PMCPMC3916656
OpenAlexW1973862928

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.