Evidence map›Paper›PMID 31672968›Full record

ArticleNature communications2019

Phase separation of Polo-like kinase 4 by autoactivation and clustering drives centriole biogenesis.

Jung-Eun Park, Liang Zhang, Jeong Kyu Bang, Thorkell Andresson, Frank DiMaio, Kyung S Lee

Abstract read
In one paragraph

Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.

0numbers the graph read from it
0cells of the map it votes in
52citing 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

52 citing papers in PubMed.

  1. Review
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  8. Role of PLK4 inhibition in cancer therapy.Cancer metastasis reviews · 2025
    Review
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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

6 authors.

Jung-Eun ParkLaboratory of Metabolism, National Cancer Institute, National Institutes of Health, 9000 Rockville Pike, Bethesda, MD, 20892, USA.ORCID http://orcid.org/0000-0001-9929-830X
Liang ZhangLaboratory of Metabolism, National Cancer Institute, National Institutes of Health, 9000 Rockville Pike, Bethesda, MD, 20892, USA.ORCID http://orcid.org/0000-0002-8338-784X
Jeong Kyu BangDivision of Magnetic Resonance, Korea Basic Science Institute, 162 Yeongudanji-ro, Ochang-eup, Cheongju, 28119, Republic of Korea.ORCID http://orcid.org/0000-0001-5916-0912
Thorkell AndressonProtein Characterization Laboratory, Frederick National Laboratory for Cancer Research and Leidos Biomedical Research Inc., 8560 Progress Drive, Frederick, MD, 21702, USA.
Frank DiMaioDepartment of Biochemistry and Institute for Protein Design, University of Washington, 1705 NE Pacific Street, Seattle, WA, 98195, USA.
Kyung S LeeLaboratory of Metabolism, National Cancer Institute, National Institutes of Health, 9000 Rockville Pike, Bethesda, MD, 20892, USA. kyunglee@mail.nih.gov.ORCID http://orcid.org/0000-0001-8326-7162

Funding

Protein structure determination from low-resolution experimental dataR01GM123089 · NIGMS · UNIVERSITY OF WASHINGTON · PI DIMAIO, FRANK P · 2017 to 2025
$2.6M
NIGMS NIH HHS R01 GM123089
6 · The paper itself

Abstract

Tight control of centriole duplication is critical for normal chromosome segregation and the maintenance of genomic stability. Polo-like kinase 4 (Plk4) is a key regulator of centriole biogenesis. How Plk4 dynamically promotes its symmetry-breaking relocalization and achieves its procentriole-assembly state remains unknown. Here we show that Plk4 is a unique kinase that utilizes its autophosphorylated noncatalytic cryptic polo-box (CPB) to phase separate and generate a nanoscale spherical condensate. Analyses of the crystal structure of a phospho-mimicking, condensation-proficient CPB mutant reveal that a disordered loop at the CPB PB2-tip region is critically required for Plk4 to generate condensates and induce procentriole assembly. CPB phosphorylation also promotes Plk4's dissociation from the Cep152 tether while binding to downstream STIL, thus allowing Plk4 condensate to serve as an assembling body for centriole biogenesis. This study uncovers the mechanism underlying Plk4 activation and may offer strategies for anti-Plk4 intervention against genomic instability and cancer.

Indexed as

Organelle BiogenesisAnimalsCell Cycle ProteinsCell Line, TumorCentriolesHEK293 CellsHumansImaging, Three-DimensionalIntracellular Signaling Peptides and ProteinsMicroscopy, ConfocalPhosphorylationProtein BindingProtein Serine-Threonine KinasesSf9 CellsSpodopteraCell Cycle ProteinsCEP152 protein, humanIntracellular Signaling Peptides and ProteinsPLK4 protein, humanProtein Serine-Threonine KinasesSTIL protein, human

Identifiers

PMID31672968
PMCPMC6823436

What OpenQuestion holds

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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.