Evidence map›Paper›PMID 26761639›Full record

ArticleCell cycle (Georgetown, Tex.)2016

Spatial regulation of greatwall by Cdk1 and PP2A-Tws in the cell cycle.

Peng Wang, Myreille Larouche, Karine Normandin, David Kachaner, Haytham Mehsen, Gregory Emery, Vincent Archambault

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 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
2.7field-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

17 citing papers in PubMed, 24 citations in OpenAlex.

  1. Review
  2. Article
  3. The ATM-E6AP-MASTL axis mediates DNA damage checkpoint recovery.bioRxiv : the preprint server for biology · 2023
    Article
  4. Article
  5. Article
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  7. Molecular Basis of the Mechanisms Controlling MASTL.Molecular & cellular proteomics : MCP · 2020
    Article
  8. Review
  9. Article
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  12. Review
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  17. 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

7 authors at 2 institutions in 1 country.

Peng Wanga Département de biochimie et médecine moléculaire ; Université de Montréal ; Québec , Canada.
Myreille Larouchea Département de biochimie et médecine moléculaire ; Université de Montréal ; Québec , Canada.
Karine Normandinb Institute for Research in Immunology and Cancer, Université de Montréal , Montréal , Québec , Canada.
David Kachanera Département de biochimie et médecine moléculaire ; Université de Montréal ; Québec , Canada.
Haytham Mehsenb Institute for Research in Immunology and Cancer, Université de Montréal , Montréal , Québec , Canada.
Gregory Emeryb Institute for Research in Immunology and Cancer, Université de Montréal , Montréal , Québec , Canada.
Vincent Archambaulta Département de biochimie et médecine moléculaire ; Université de Montréal ; Québec , Canada.
Université de Montréal · CAInstitute for Research in Immunology and Cancer · CA

Funding

Canadian Institutes of Health Research
6 · The paper itself

Abstract

Entry into mitosis requires the phosphorylation of multiple substrates by cyclin B-Cdk1, while exit from mitosis requires their dephosphorylation, which depends largely on the phosphatase PP2A in complex with its B55 regulatory subunit (Tws in Drosophila). At mitotic entry, cyclin B-Cdk1 activates the Greatwall kinase, which phosphorylates Endosulfine proteins, thereby activating their ability to inhibit PP2A-B55 competitively. The inhibition of PP2A-B55 at mitotic entry facilitates the accumulation of phosphorylated Cdk1 substrates. The coordination of these enzymes involves major changes in their localization. In interphase, Gwl is nuclear while PP2A-B55 is cytoplasmic. We recently showed that Gwl suddenly relocalizes from the nucleus to the cytoplasm in prophase, before nuclear envelope breakdown and that this controlled localization of Gwl is required for its function. We and others have shown that phosphorylation of Gwl by cyclin B-Cdk1 at multiple sites is required for its nuclear exclusion, but the precise mechanisms remained unclear. In addition, how Gwl returns to its nuclear localization was not explored. Here we show that cyclin B-Cdk1 directly inactivates a Nuclear Localization Signal in the central region of Gwl. This phosphorylation facilitates the cytoplasmic retention of Gwl, which is exported to the cytoplasm in a Crm1-dependent manner. In addition, we show that PP2A-Tws promotes the return of Gwl to its nuclear localization during cytokinesis. Our results indicate that the cyclic changes in Gwl localization at mitotic entry and exit are directly regulated by the antagonistic cyclin B-Cdk1 and PP2A-Tws enzymes.

Indexed as

AnimalsCDC2 Protein KinaseCell NucleusCyclin BCytoplasmDrosophilaDrosophila ProteinsExportin 1 ProteinGene Expression Regulation, DevelopmentalKaryopherinsMitosisPhosphoprotein PhosphatasesPhosphorylationProtein Serine-Threonine KinasesReceptors, Cytoplasmic and NuclearCDC2 Protein KinaseCyclin BDrosophila ProteinsExportin 1 ProteinGwl protein, DrosophilaKaryopherinsPhosphoprotein PhosphatasesProtein Serine-Threonine KinasesReceptors, Cytoplasmic and Nucleartws protein, DrosophilaCdk1Cell cycleGreatwallMitosisPP2A

Identifiers

PMID26761639
PMCPMC5056603
OpenAlexW2293219121

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.