Evidence map›Paper›PMID 32772043›Full record

ArticleOncogene2020

USP13 controls the stability of Aurora B impacting progression through the cell cycle.

Mara Esposito, H Begum Akman, Philippe Giron, M Angeles Ceregido, Rogier Schepers, Luis C Ramos Paez, Esther La Monaca, Jacques De Greve, Olivier Coux, Carl De Trez and 2 more

Abstract read
PubMed Publisher
In one paragraph

Article in Oncogene, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.9field-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

19 citing papers in PubMed, 32 citations in OpenAlex.

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  16. Article
  17. Role of USP13 in physiology and diseases.Frontiers in molecular biosciences · 2022
    Review
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  19. 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

12 authors at 4 institutions in 3 countries.

Mara EspositoLaboratory of Pathophysiological Cell Signaling, Department of Biology, Faculty of Science and Bioengineering Sciences, Vrije Universiteit Brussel, Pleinlaan 2, 1050, Brussels, Belgium.
H Begum AkmanDepartment of Pharmacology, University of Cambridge, Tennis Court Road, Cambridge, CB2 1PD, UK.
Philippe GironLaboratory of Pathophysiological Cell Signaling, Department of Biology, Faculty of Science and Bioengineering Sciences, Vrije Universiteit Brussel, Pleinlaan 2, 1050, Brussels, Belgium.
M Angeles CeregidoLaboratory of Pathophysiological Cell Signaling, Department of Biology, Faculty of Science and Bioengineering Sciences, Vrije Universiteit Brussel, Pleinlaan 2, 1050, Brussels, Belgium.
Rogier SchepersLaboratory of Pathophysiological Cell Signaling, Department of Biology, Faculty of Science and Bioengineering Sciences, Vrije Universiteit Brussel, Pleinlaan 2, 1050, Brussels, Belgium.
Luis C Ramos PaezLaboratory of Pathophysiological Cell Signaling, Department of Biology, Faculty of Science and Bioengineering Sciences, Vrije Universiteit Brussel, Pleinlaan 2, 1050, Brussels, Belgium.
Esther La MonacaLaboratory of Pathophysiological Cell Signaling, Department of Biology, Faculty of Science and Bioengineering Sciences, Vrije Universiteit Brussel, Pleinlaan 2, 1050, Brussels, Belgium.
Jacques De GreveLaboratory of Molecular and Medical Oncology, Faculty of Medicine and Pharmacy, Vrije Universiteit Brussel, Laarbeeklaan 103, 1090, Brussels, Belgium.
Olivier CouxCNRS-CRBM, 1919 Route de Mende, 34293, Montpellier, France.ORCID http://orcid.org/0000-0001-8455-3849
Carl De TrezLaboratory of Cellular and Molecular Immunology, Department of Bioengineering, Faculty of Science and Bioengineering Sciences, Vrije Universiteit Brussel, Pleinlaan 2, 1050, Brussels, Belgium.
Catherine LindonDepartment of Pharmacology, University of Cambridge, Tennis Court Road, Cambridge, CB2 1PD, UK.
Gustavo J GutierrezLaboratory of Pathophysiological Cell Signaling, Department of Biology, Faculty of Science and Bioengineering Sciences, Vrije Universiteit Brussel, Pleinlaan 2, 1050, Brussels, Belgium. ggutierr@vub.be.ORCID http://orcid.org/0000-0001-8652-972X
Vrije Universiteit Brussel · BEUniversity of Cambridge · GBAblynx (Belgium) · BECentre National de la Recherche Scientifique · FR

Funding

Biotechnology and Biological Sciences Research Council BB/R004137/1Medical Research Council MR/M01102X/1
6 · The paper itself

Abstract

Aurora B kinase plays essential roles in mitosis. Its protein levels increase before the onset of mitosis and sharply decrease during mitosis exit. The latter decrease is due to a balance between the actions of the E3 ubiquitin ligase anaphase-promoting complex or cyclosome (activated by the Cdh1 adapter), and the deubiquitinating enzyme USP35. Aurora B also executes important functions in interphase. Abnormal modulation of Aurora B in interphase leads to cell cycle defects often linked to aberrant chromosomal condensation and segregation. Very little is however known about how Aurora B levels are regulated in interphase. Here we found that USP13-associates with and stabilizes Aurora B in cells, especially before their entry into mitosis. In order for USP13 to exert its stabilizing effect on Aurora B, their association is promoted by the Aurora B-mediated phosphorylation of USP13 at Serine 114. We also present evidence that USP13 instigates Aurora B deubiquitination and/or protect it from degradation in a non-catalytic manner. In addition, we report that genetic or chemical modulation of the cellular levels/activity of USP13 affects unperturbed cell-cycle progression. Overall our study unveils the molecular and cellular connections of the USP13-Aurora B axis, which potentially participates in the rewiring of the cell cycle happening in cancer cells.

Indexed as

Aurora Kinase BCell CycleCell Cycle CheckpointsCell Line, TumorDisease ProgressionEndopeptidasesEnzyme StabilityGene ExpressionGene Knockdown TechniquesHumansPhosphorylationProtein BindingSerineUbiquitin-Specific ProteasesAURKB protein, humanAurora Kinase BEndopeptidasesSerineUbiquitin-Specific ProteasesUSP13 protein, human

Identifiers

PMID32772043
OpenAlexW3047957138

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.