Evidence map›Paper›PMID 36766713›Full record

ArticleCells2023

Aurora B SUMOylation Is Restricted to Centromeres in Early Mitosis and Requires RANBP2.

Erica Di Cesare, Sara Moroni, Jessica Bartoli, Michela Damizia, Maria Giubettini, Carolin Koerner, Veronica Krenn, Andrea Musacchio, Patrizia Lavia

Open access · goldAbstract read
In one paragraph

Article in Cells, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
1.5field-weighted citation impact, top 21% 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

5 citing papers in PubMed, 7 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Nuclear transport proteins: structure, function, and disease relevance.Signal transduction and targeted therapy · 2023
    Review
  5. 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

9 authors at 2 institutions in 2 countries.

Erica Di CesareInstitute of Molecular Biology and Pathology (IBPM), CNR National Research Council of Italy, 00185 Rome, Italy.
Sara MoroniInstitute of Molecular Biology and Pathology (IBPM), CNR National Research Council of Italy, 00185 Rome, Italy.
Jessica BartoliInstitute of Molecular Biology and Pathology (IBPM), CNR National Research Council of Italy, 00185 Rome, Italy.
Michela DamiziaInstitute of Molecular Biology and Pathology (IBPM), CNR National Research Council of Italy, 00185 Rome, Italy.
Maria GiubettiniCrestOptics, 00165 Rome, Italy.
Carolin KoernerMax Planck Institute of Molecular Physiology, 44227 Dortmund, Germany.ORCID 0000-0001-8132-1735
Veronica KrennMax Planck Institute of Molecular Physiology, 44227 Dortmund, Germany.ORCID 0000-0002-7416-3385
Andrea MusacchioMax Planck Institute of Molecular Physiology, 44227 Dortmund, Germany.ORCID 0000-0003-2362-8784
Patrizia LaviaInstitute of Molecular Biology and Pathology (IBPM), CNR National Research Council of Italy, 00185 Rome, Italy.ORCID 0000-0003-3310-6701
Institute of Molecular Biology and Pathology · ITMax Planck Institute of Molecular Physiology · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Conjugation with the small ubiquitin-like modifier (SUMO) modulates protein interactions and localisation. The kinase Aurora B, a key regulator of mitosis, was previously identified as a SUMOylation target in vitro and in assays with overexpressed components. However, where and when this modification genuinely occurs in human cells was not ascertained. Here, we have developed intramolecular Proximity Ligation Assays (PLA) to visualise SUMO-conjugated Aurora B in human cells in situ. We visualised Aurora B-SUMO products at centromeres in prometaphase and metaphase, which declined from anaphase onwards and became virtually undetectable at cytokinesis. In the mitotic window in which Aurora B/SUMO products are abundant, Aurora B co-localised and interacted with NUP358/RANBP2, a nucleoporin with SUMO ligase and SUMO-stabilising activity. Indeed, in addition to the requirement for the previously identified PIAS3 SUMO ligase, we found that NUP358/RANBP2 is also implicated in Aurora B-SUMO PLA product formation and centromere localisation. In summary, SUMOylation marks a distinctive window of Aurora B functions at centromeres in prometaphase and metaphase while being dispensable for functions exerted in cytokinesis, and RANBP2 contributes to this control, adding a novel layer to modulation of Aurora B functions during mitosis.

Indexed as

Nuclear Pore Complex ProteinsSumoylationAurora Kinase BCentromereHumansLigasesMitosisMolecular ChaperonesProtein Inhibitors of Activated STATAURKB protein, humanAurora Kinase BLigasesMolecular ChaperonesNuclear Pore Complex ProteinsPIAS3 protein, humanProtein Inhibitors of Activated STATran-binding protein 2Aurora Bin situ proximity ligation assay (isPLA)mitosisRANBP2SUMOylation

Identifiers

PMID36766713
PMCPMC9913629
OpenAlexW4317503514

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.