Evidence map›Paper›PMID 26713495›Full record

ArticleCell cycle (Georgetown, Tex.)2016

Aurora A phosphorylation of WD40-repeat protein 62 in mitotic spindle regulation.

Nicholas R Lim, Yvonne Y C Yeap, Ching-Seng Ang, Nicholas A Williamson, Marie A Bogoyevitch, Leonie M Quinn, Dominic C H Ng

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 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.6field-weighted citation impact, top 18% 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, 29 citations in OpenAlex.

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  15. Aurora A activation in mitosis promoted by BuGZ.The Journal of cell biology · 2018
    Article
  16. Article
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  18. Driving WDR62 to the pole.Cell cycle (Georgetown, Tex.) · 2016
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  19. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors at 2 institutions in 1 country.

Nicholas R Lima Department of Biochemistry and Molecular Biology , University of Melbourne , Victoria , Australia.
Yvonne Y C Yeapa Department of Biochemistry and Molecular Biology , University of Melbourne , Victoria , Australia.
Ching-Seng Angb Bio21 Molecular Science and Biotechnology Institute, University of Melbourne , Victoria , Australia.
Nicholas A Williamsonb Bio21 Molecular Science and Biotechnology Institute, University of Melbourne , Victoria , Australia.
Marie A Bogoyevitcha Department of Biochemistry and Molecular Biology , University of Melbourne , Victoria , Australia.
Leonie M Quinnc Department of Anatomy and Neuroscience , University of Melbourne , Victoria , Australia.
Dominic C H Nga Department of Biochemistry and Molecular Biology , University of Melbourne , Victoria , Australia.
University of Melbourne · AUUniversity of Queensland · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Mitotic spindle organization is regulated by centrosomal kinases that potentiate recruitment of spindle-associated proteins required for normal mitotic progress including the microcephaly protein WD40-repeat protein 62 (WDR62). WDR62 functions underlie normal brain development as autosomal recessive mutations and wdr62 loss cause microcephaly. Here we investigate the signaling interactions between WDR62 and the mitotic kinase Aurora A (AURKA) that has been recently shown to cooperate to control brain size in mice. The spindle recruitment of WDR62 is closely correlated with increased levels of AURKA following mitotic entry. We showed that depletion of TPX2 attenuated WDR62 localization at spindle poles indicating that TPX2 co-activation of AURKA is required to recruit WDR62 to the spindle. We demonstrated that AURKA activity contributed to the mitotic phosphorylation of WDR62 residues Ser49 and Thr50 and phosphorylation of WDR62 N-terminal residues was required for spindle organization and metaphase chromosome alignment. Our analysis of several MCPH-associated WDR62 mutants (V65M, R438H and V1314RfsX18) that are mislocalized in mitosis revealed that their interactions and phosphorylation by AURKA was substantially reduced consistent with the notion that AURKA is a key determinant of WDR62 spindle recruitment. Thus, our study highlights the role of AURKA signaling in the spatiotemporal control of WDR62 at spindle poles where it maintains spindle organization.

Indexed as

AnimalsAurora Kinase ACell Cycle ProteinsCell LineChromosome SegregationCRISPR-Cas SystemsHeLa CellsHumansMetaphaseMiceMicroscopy, FluorescenceMicrotubule-Associated ProteinsNerve Tissue ProteinsNuclear ProteinsPhosphorylationRNA InterferenceAurora Kinase ACell Cycle ProteinsMicrotubule-Associated ProteinsNerve Tissue ProteinsNuclear ProteinsRNA, Small InterferingTPX2 protein, humanWDR62 protein, humanaurora Ac-jun N-terminal kinasemitosisphosphorylationprimary microcephaly

Identifiers

PMID26713495
PMCPMC4943692
OpenAlexW2207624337

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.