ArticleThe Journal of cell biology2023
PLK4 self-phosphorylation drives the selection of a single site for procentriole assembly.
Article in The Journal of cell biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 12 papers.
What it found
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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.
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.
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Who cites it
12 citing papers in PubMed, 14 citations in OpenAlex.
- Article
- Tipping the balance: synthesis and evaluation of centrinone-based degraders of polo-like kinase 4.RSC chemical biology · 2026Article
- CDK1 and CEP97 cooperatively control centriole length to orchestrate ciliogenesis and developmental patterning.Genes & development · 2026Article
- Critical constituents and assembly principles of centriole biogenesis in human cells.Nature reviews. Molecular cell biology · 2026Review
- Investigating the Mechanisms of Pazopanib-induced Hepatotoxicity: Insights from Network Toxicology, Microarray Analysis, and Machine Learning.Current medicinal chemistry · 2026Article
- Visualizing Drosophila centrioles by expansion microscopy.Journal of cell science · 2026Article
- PLK4: Master Regulator of Centriole Duplication and Its Therapeutic Potential.Cytoskeleton (Hoboken, N.J.) · 2025Review
- Binding of CEP152 to PLK4 stimulates kinase activity to promote centriole assembly.Molecular biology of the cell · 2025Article
- Amplified centrosomes-more than just a threat.EMBO reports · 2024Review
- Generating CRISPR-edited clonal lines of culturedBiology methods & protocols · 2024Article
- A simple Turing reaction-diffusion model explains how PLK4 breaks symmetry during centriole duplication and assembly.PLoS biology · 2023Article
- A simple Turing reaction-diffusion model explains how PLK4 breaks symmetry during centriole duplication and assembly.PLoS biology · 2023Article
Corrections and comments
- Erratum issued
Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Polo-like kinase 4 (PLK4) is a key regulator of centriole biogenesis, but how PLK4 selects a single site for procentriole assembly remains unclear. Using ultrastructure expansion microscopy, we show that PLK4 localizes to discrete sites along the wall of parent centrioles. While there is variation in the number of sites PLK4 occupies on the parent centriole, most PLK4 localize at a dominant site that directs procentriole assembly. Inhibition of PLK4 activity leads to stable binding of PLK4 to the centriole and increases occupancy to a maximum of nine sites. We show that self-phosphorylation of an unstructured linker promotes the release of active PLK4 from the centriole to drive the selection of a single site for procentriole assembly. Preventing linker phosphorylation blocks PLK4 turnover, leading to supernumerary sites of PLK4 localization and centriole amplification. Therefore, self-phosphorylation is a major driver of the spatial patterning of PLK4 at the centriole and plays a critical role in selecting a single centriole duplication site.
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Registered trials
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.