Evidence map›Paper›PMID 29263250›Full record

ArticleOpen biology2017

Two-step phosphorylation of Ana2 by Plk4 is required for the sequential loading of Ana2 and Sas6 to initiate procentriole formation.

Nikola S Dzhindzhev, George Tzolovsky, Zoltan Lipinszki, Mohammed Abdelaziz, Janus Debski, Michal Dadlez, David M Glover

Open access · goldAbstract read
In one paragraph

Article in Open biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.

0numbers the graph read from it
0cells of the map it votes in
47citing papers in PubMed
5.8field-weighted citation impact, top 3% 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

47 citing papers in PubMed, 76 citations in OpenAlex.

  1. Article
  2. Review
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  6. Article
  7. Article
  8. Article
  9. Article
  10. Plk4 Is a Novel Substrate of Protein Phosphatase 5.International journal of molecular sciences · 2023
    Article
  11. Article
  12. Article
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  15. Review
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  18. Article
  19. Phospho-regulation of mitotic spindle assembly.Cytoskeleton (Hoboken, N.J.) · 2020
    Review
  20. 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

7 authors at 3 institutions in 3 countries.

Nikola S DzhindzhevDepartment of Genetics, University of Cambridge, Cambridge CB2 3EH, UK nsd23@cam.ac.uk.
George TzolovskyDepartment of Genetics, University of Cambridge, Cambridge CB2 3EH, UK.
Zoltan LipinszkiMTA SZBK Lendület Laboratory of Cell Cycle Regulation and Institute of Biochemistry, Biological Research Centre, Hungarian Academy of sciences, Szeged, Hungary.
Mohammed AbdelazizDepartment of Genetics, University of Cambridge, Cambridge CB2 3EH, UK.
Janus DebskiLaboratory of Mass Spectrometry, Institute of Biochemistry and Biophysics, Polish Academy of Sciences, 02-106 Warsaw, Poland.
Michal DadlezLaboratory of Mass Spectrometry, Institute of Biochemistry and Biophysics, Polish Academy of Sciences, 02-106 Warsaw, Poland.
David M GloverDepartment of Genetics, University of Cambridge, Cambridge CB2 3EH, UK dmg25@hermes.cam.ac.uk.ORCID 0000-0003-0956-0103
University of Cambridge · GBInstitute of Biochemistry and Biophysics, Polish Academy of Sciences · PLHUN-REN Szegedi Biológiai Kutatóközpont · HU

Funding

Cancer Research UK 18795Cancer Research UK C3/A18795Wellcome Trust 202855/Z/16/Z
6 · The paper itself

Abstract

The conserved process of centriole duplication requires Plk4 kinase to recruit and promote interactions between Sas6 and Sas5/Ana2/STIL (respective nomenclature of worms/flies/humans). Plk4-mediated phosphorylation of Ana2/STIL in its conserved STAN motif has been shown to promote its interaction with Sas6. However, STAN motif phosphorylation is not required for recruitment of Ana2 to the centriole. Here we show that in

Indexed as

Protein Processing, Post-TranslationalAnimalsCell Cycle ProteinsCell LineCentriolesDrosophila melanogasterDrosophila ProteinsMicrotubule-Associated ProteinsPhosphorylationProtein Serine-Threonine KinasesAna2 protein, DrosophilaCell Cycle ProteinsDrosophila ProteinsMicrotubule-Associated ProteinsProtein Serine-Threonine KinasesSak protein, DrosophilaSas-6 protein, DrosophilaAna2centriolecentrosomePlk4Sas6

Identifiers

PMID29263250
PMCPMC5746551
OpenAlexW2781466531

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.