Evidence map›Paper›PMID 27580187›Full record

ArticleCell cycle (Georgetown, Tex.)2016

Phosphorylation of CDC25A on SER283 in late S/G2 by CDK/cyclin complexes accelerates mitotic entry.

Laurent Mazzolini, Anaïs Broban, Carine Froment, Odile Burlet-Schiltz, Arnaud Besson, Stéphane Manenti, Christine Dozier

Open access · bronzeAbstract read
In one paragraph

Article in Cell cycle (Georgetown, Tex.), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
0.8field-weighted citation impact, top 28% 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

9 citing papers in PubMed, 38 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. SRSF10 stabilizes CDC25A by triggering exon 6 skipping to promote hepatocarcinogenesis.Journal of experimental & clinical cancer research : CR · 2022
    Article
  5. Article
  6. Article
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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 4 institutions in 1 country.

Laurent Mazzolinia Centre de Recherche en Cancérologie de Toulouse, INSERM UMR1037, CNRS ERL5294 , Université Toulouse III Paul Sabatier , Toulouse , France.
Anaïs Brobana Centre de Recherche en Cancérologie de Toulouse, INSERM UMR1037, CNRS ERL5294 , Université Toulouse III Paul Sabatier , Toulouse , France.
Carine Fromentc Institut de Pharmacologie et de Biologie Structurale , Université Toulouse III Paul Sabatier Toulouse , CNRS UMR5089 , Toulouse , France.
Odile Burlet-Schiltzc Institut de Pharmacologie et de Biologie Structurale , Université Toulouse III Paul Sabatier Toulouse , CNRS UMR5089 , Toulouse , France.
Arnaud Bessona Centre de Recherche en Cancérologie de Toulouse, INSERM UMR1037, CNRS ERL5294 , Université Toulouse III Paul Sabatier , Toulouse , France.
Stéphane Manentia Centre de Recherche en Cancérologie de Toulouse, INSERM UMR1037, CNRS ERL5294 , Université Toulouse III Paul Sabatier , Toulouse , France.
Christine Doziera Centre de Recherche en Cancérologie de Toulouse, INSERM UMR1037, CNRS ERL5294 , Université Toulouse III Paul Sabatier , Toulouse , France.
Centre National de la Recherche Scientifique · FRInserm · FRCentre de Recherche en Cancérologie de Toulouse · FRUniversité Toulouse III - Paul Sabatier · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The Cdc25A phosphatase is an essential activator of CDK-cyclin complexes at all steps of the eukaryotic cell cycle. The activity of Cdc25A is itself regulated in part by positive and negative feedback regulatory loops performed by its CDK-cyclin substrates that occur in G1 as well as during the G1/S and G2/M transitions. However, the regulation of Cdc25A during G2 phase progression before mitotic entry has not been intensively characterized. Here, we identify by mass spectrometry analysis a new phosphorylation event of Cdc25A on Serine283. Phospho-specific antibodies revealed that the phosphorylation of this residue appears in late S/G2 phase of an unperturbed cell cycle and is performed by CDK-cyclin complexes. Overexpression studies of wild-type and non-phosphorylatable mutant forms of Cdc25A indicated that Ser283 phosphorylation increases the G2/M-promoting activity of the phosphatase without impacting its stability or subcellular localization. Our results therefore identify a new positive regulatory loop between Cdc25A and its CDK-cyclin substrates which contributes to accelerate entry into mitosis through the regulation of Cdc25A activity in G2.

Indexed as

G2 PhaseMitosisS PhaseAmino Acid Sequencecdc25 PhosphatasesCell Line, TumorCyclin-Dependent KinasesCyclinsHumansIntracellular SpaceMass SpectrometryMutationPhosphorylationProtein StabilitySerineCDC25A protein, humancdc25 PhosphatasesCyclin-Dependent KinasesCyclinsSerineactivating phosphorylationCdc25ACDK-cyclincell cycleG2/M transition

Identifiers

PMID27580187
PMCPMC5053558
OpenAlexW2507489293

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.