Evidence map›Paper›PMID 21353560›Full record

ArticleCurrent biology : CB2011

Identification of a polo-like kinase 4-dependent pathway for de novo centriole formation.

Frank Eckerdt, Tomomi M Yamamoto, Andrea L Lewellyn, James L Maller

Open access · bronzeAbstract read
In one paragraph

Article in Current biology : CB, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
2.6field-weighted citation impact, top 11% 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

23 citing papers in PubMed, 39 citations in OpenAlex.

  1. Article
  2. Appearing and disappearing acts of cilia.Journal of biosciences · 2023
    Review
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. RNA (New York, N.Y.) · 2017
    Article
  9. Article
  10. Article
  11. Article
  12. The centriole duplication cycle.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2014
    Review
  13. Polo-like kinases: structural variations lead to multiple functions.Nature reviews. Molecular cell biology · 2014
    Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  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

4 authors at 1 institution in 1 country.

Frank EckerdtDepartment of Pharmacology, University of Colorado School of Medicine, Aurora, CO 80045, USA.
Tomomi M Yamamoto
Andrea L Lewellyn
James L Maller
University of Colorado Denver · US

Funding

Howard Hughes Medical Institute
6 · The paper itself

Abstract

Supernumerary centrosomes are a key cause of genomic instability in cancer cells. New centrioles can be generated by duplication with a mother centriole as a platform or, in the absence of preexisting centrioles, by formation de novo. Polo-like kinase 4 (Plk4) regulates both modes of centriole biogenesis, and Plk4 deregulation has been linked to tumor development. We show that Plx4, the Xenopus homolog of mammalian Plk4 and Drosophila Sak, induces de novo centriole formation in vivo in activated oocytes and in egg extracts, but not in immature or in vitro matured oocytes. Both kinase activity and the polo-box domain of Plx4 are required for de novo centriole biogenesis. Polarization microscopy in "cycling" egg extracts demonstrates that de novo centriole formation is independent of Cdk2 activity, a major difference compared to template-driven centrosome duplication that is linked to the nuclear cycle and requires cyclinA/E/Cdk2. Moreover, we show that the Mos-MAPK pathway blocks Plx4-dependent de novo centriole formation before fertilization, thereby ensuring paternal inheritance of the centrosome. The results define a new system for studying the biochemical and molecular basis of de novo centriole formation and centriole biogenesis in general.

Indexed as

AnimalsBlotting, WesternCell Cycle ProteinsCentriolesMicroscopy, PolarizationOocytesProtein Serine-Threonine KinasesSignal TransductionXenopusXenopus ProteinsCell Cycle Proteinspolo-like kinase 4, XenopusProtein Serine-Threonine KinasesXenopus Proteins

Identifiers

PMID21353560
PMCPMC3093158
OpenAlexW2022732864

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.