Evidence map›Paper›PMID 25264260›Full record

ArticleCurrent biology : CB2014

Plk4 phosphorylates Ana2 to trigger Sas6 recruitment and procentriole formation.

Nikola S Dzhindzhev, George Tzolovsky, Zoltan Lipinszki, Sandra Schneider, Ramona Lattao, Jingyan Fu, Janusz Debski, Michal Dadlez, David M Glover

Abstract read
In one paragraph

Article in Current biology : CB, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 126 papers.

0numbers the graph read from it
0cells of the map it votes in
126citing papers in PubMed
–field-weighted citation impact
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

126 citing papers in PubMed.

  1. Review
  2. Article
  3. Centriolar satellites regulateMolecular biology of the cell · 2026
    Article
  4. Review
  5. Article
  6. Centriolar satellites regulatebioRxiv : the preprint server for biology · 2026
    Article
  7. Article
  8. Article
  9. Review
  10. DysregulatedLife science alliance · 2025
    Article
  11. Article
  12. Review
  13. Review
  14. Article
  15. Role of PLK4 inhibition in cancer therapy.Cancer metastasis reviews · 2025
    Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

66 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

9 authors.

Nikola S DzhindzhevDepartment of Genetics, University of Cambridge, Cambridge CB2 3EH, UK. Electronic address: nsd23@cam.ac.uk.
George TzolovskyDepartment of Genetics, University of Cambridge, Cambridge CB2 3EH, UK.
Zoltan LipinszkiDepartment of Genetics, University of Cambridge, Cambridge CB2 3EH, UK.
Sandra SchneiderDepartment of Genetics, University of Cambridge, Cambridge CB2 3EH, UK.
Ramona LattaoDepartment of Genetics, University of Cambridge, Cambridge CB2 3EH, UK.
Jingyan FuDepartment of Genetics, University of Cambridge, Cambridge CB2 3EH, UK.
Janusz 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. Electronic address: dmg25@cam.ac.uk.

Funding

DROSOPHILA GENOMICS RESOURCE CENTERP40OD010949 · OD · TRUSTEES OF INDIANA UNIVERSITY · PI Andrew Zelhof · 2012 to 2026
$9.4M
Cancer Research UK 11431Medical Research CouncilNIH HHS 2P40OD010949-10A1NIH HHS P40 OD010949
6 · The paper itself

Abstract

Centrioles are 9-fold symmetrical structures at the core of centrosomes and base of cilia whose dysfunction has been linked to a wide range of inherited diseases and cancer. Their duplication is regulated by a protein kinase of conserved structure, the C. elegans ZYG-1 or its Polo-like kinase 4 (Plk4) counterpart in other organisms. Although Plk4's centriolar partners and mechanisms that regulate its stability are known, its crucial substrates for centriole duplication have never been identified. Here we show that Drosophila Plk4 phosphorylates four conserved serines in the STAN motif of the core centriole protein Ana2 to enable it to bind and recruit its Sas6 partner. Ana2 and Sas6 normally load onto both mother and daughter centrioles immediately after their disengagement toward the end of mitosis to seed procentriole formation. Nonphosphorylatable Ana2 still localizes to the centriole but can no longer recruit Sas6 and centriole duplication fails. Thus, following centriole disengagement, recruitment of Ana2 and its phosphorylation by Plk4 are the earliest known events in centriole duplication to recruit Sas6 and thereby establish the architecture of the new procentriole engaged with its parent.

Indexed as

Amino Acid SequenceAnimalsCell Cycle ProteinsCentriolesDrosophilaDrosophila ProteinsMicrotubule-Associated ProteinsMolecular Sequence DataPhosphorylationProtein Serine-Threonine KinasesSequence AlignmentAna2 protein, DrosophilaCell Cycle ProteinsDrosophila ProteinsMicrotubule-Associated ProteinsProtein Serine-Threonine KinasesSak protein, DrosophilaSas-6 protein, Drosophila

Identifiers

PMID25264260
PMCPMC4229625

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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.