Evidence map›Paper›PMID 20956543›Full record

ArticleThe Journal of biological chemistry2010

Human Cdc14A phosphatase modulates the G2/M transition through Cdc25A and Cdc25B.

María D Vázquez-Novelle, Niels Mailand, Sara Ovejero, Avelino Bueno, María P Sacristán

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
2.0field-weighted citation impact, top 15% 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

17 citing papers in PubMed, 38 citations in OpenAlex.

  1. Article
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  8. Review
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  13. Functional redundancy between Cdc14 phosphatases in zebrafish ciliogenesis.Developmental dynamics : an official publication of the American Association of Anatomists · 2012
    Article
  14. Review
  15. The role of Cdc25A in the regulation of cell proliferation and apoptosis.Anti-cancer agents in medicinal chemistry · 2012
    Review
  16. Article
  17. 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

5 authors at 3 institutions in 2 countries.

María D Vázquez-NovelleCentro de Investigación del Cáncer, Universidad de Salamanca/CSIC, 37007 Salamanca, Spain.
Niels Mailand
Sara Ovejero
Avelino Bueno
María P Sacristán
Universidad de Salamanca · ESCentro de Investigación del Cáncer · ESDanish Cancer Society · DK

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The Cdc14 family of serine-threonine phosphatases antagonizes CDK activity by reversing CDK-dependent phosphorylation events. It is well established that the yeast members of this family bring about the M/G1 transition. Budding yeast Cdc14 is essential for CDK inactivation at the end of mitosis and fission yeast Cdc14 homologue Flp1/Clp1 down-regulates Cdc25 to ensure the inactivation of mitotic CDK complexes to trigger cell division. However, the functions of human Cdc14 homologues remain poorly understood. Here we have tested the hypothesis that Cdc14A might regulate Cdc25 mitotic inducers in human cells. We found that increasing levels of Cdc14A delay entry into mitosis by inhibiting Cdk1-cyclin B1 activity. By contrast, lowering the levels of Cdc14A accelerates mitotic entry. Biochemical analyses revealed that Cdc14A acts through key Cdk1-cyclin B1 regulators. We observed that Cdc14A directly bound to and dephosphorylated Cdc25B, inhibiting its catalytic activity. Cdc14A also regulated the activity of Cdc25A at the G2/M transition. Our results indicate that Cdc14A phosphatase prevents premature activation of Cdk1 regulating Cdc25A and Cdc25B at the entry into mitosis.

Indexed as

cdc25 PhosphatasesCDC2 Protein KinaseCell LineEnzyme ActivationG2 PhaseHumansMitosisPhosphoric Monoester HydrolasesProtein Tyrosine PhosphatasesSaccharomyces cerevisiaeCDC14A protein, humanCDC25A protein, humanCDC25B protein, humancdc25 PhosphatasesCDC2 Protein KinasePhosphoric Monoester HydrolasesProtein Tyrosine Phosphatases

Identifiers

PMID20956543
PMCPMC3003353
OpenAlexW2062776477

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.