Evidence map›Paper›PMID 24980795›Full record

ArticleStructure (London, England : 1993)2014

Structure of the C. elegans ZYG-1 cryptic polo box suggests a conserved mechanism for centriolar docking of Plk4 kinases.

Ekaterina Shimanovskaya, Valeria Viscardi, Johannes Lesigang, Molly M Lettman, Renping Qiao, Dmitri I Svergun, Adam Round, Karen Oegema, Gang Dong

Abstract read
In one paragraph

Article in Structure (London, England : 1993), 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing 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

31 citing papers in PubMed.

  1. Article
  2. Distinct D-box Motifs in SPD-2 Mediate APC/CbioRxiv : the preprint server for biology · 2025
    Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Appearing and disappearing acts of cilia.Journal of biosciences · 2023
    Review
  10. Article
  11. A combinedCell cycle (Georgetown, Tex.) · 2022
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Structural and Functional Analyses of the FAM46C/Plk4 Complex.Structure (London, England : 1993) · 2020
    Article
  17. Review
  18. Article
  19. Review
  20. Mitotic Cell Division inGenetics · 2019
    Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

9 authors.

Ekaterina ShimanovskayaMax F. Perutz Laboratories, Medical University of Vienna, 1030 Vienna, Austria.
Valeria ViscardiDepartment of Cellular and Molecular Medicine, Ludwig Institute for Cancer Research, University of California, San Diego, La Jolla, CA 92093, USA.
Johannes LesigangMax F. Perutz Laboratories, Medical University of Vienna, 1030 Vienna, Austria.
Molly M LettmanDepartment of Cellular and Molecular Medicine, Ludwig Institute for Cancer Research, University of California, San Diego, La Jolla, CA 92093, USA.
Renping QiaoMax F. Perutz Laboratories, Medical University of Vienna, 1030 Vienna, Austria.
Dmitri I SvergunEuropean Molecular Biology Laboratory, Hamburg Unit, EMBL c/o DESY, Notkestrasse 85, 22603 Hamburg, Germany.
Adam RoundEuropean Molecular Biology Laboratory, Grenoble Outstation, 6 rue Jules Horowitz, 38042 Grenoble, France; Unit for Virus Host-Cell Interactions, University Grenoble Alpes-EMBL-CNRS, 6 rue Jules Horowitz, 38042 Grenoble, France.
Karen OegemaDepartment of Cellular and Molecular Medicine, Ludwig Institute for Cancer Research, University of California, San Diego, La Jolla, CA 92093, USA. Electronic address: koegema@ucsd.edu.
Gang DongMax F. Perutz Laboratories, Medical University of Vienna, 1030 Vienna, Austria. Electronic address: gang.dong@meduniwien.ac.at.

Funding

Analysis of Centrosome DynamicsR01GM074207 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI OEGEMA, KAREN F · 2006 to 2025
$6.6M
Austrian Science Fund FWF P 23440NIGMS NIH HHS R01 GM074207NIGMS NIH HHS R01-GM074207
6 · The paper itself

Abstract

Plk4 family kinases control centriole assembly. Plk4s target mother centrioles through an interaction between their cryptic polo box (CPB) and acidic regions in the centriolar receptors SPD-2/Cep192 and/or Asterless/Cep152. Here, we report a crystal structure for the CPB of C. elegans ZYG-1, which forms a Z-shaped dimer containing an intermolecular β sheet with an extended basic surface patch. Biochemical and in vivo analysis revealed that electrostatic interactions dock the ZYG-1 CPB basic patch onto the SPD-2-derived acidic region to promote ZYG-1 targeting and new centriole assembly. Analysis of a different crystal form of the Drosophila Plk4 (DmPlk4) CPB suggests that it also forms a Z-shaped dimer. Comparison of the ZYG-1 and DmPlk4 CPBs revealed structural changes in the ZYG-1 CPB that confer selectivity for binding SPD-2 over Asterless-derived acidic regions. Overall, our findings suggest a conserved mechanism for centriolar docking of Plk4 homologs that initiate daughter centriole assembly.

Indexed as

Models, MolecularAmino Acid SequenceAnimalsCaenorhabditis elegansCaenorhabditis elegans ProteinsCentriolesDimerizationMolecular Sequence DataProtein BindingProtein KinasesProtein Serine-Threonine KinasesProtein Structure, TertiarySpecies SpecificityStructure-Activity RelationshipCaenorhabditis elegans ProteinsProtein KinasesProtein Serine-Threonine KinasesSPD-2 protein, C eleganszyg-1 protein, C elegans

Identifiers

PMID24980795
PMCPMC4126857

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Registered trials

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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.