ArticleThe Journal of cell biology2021
Polo-like kinase 1 independently controls microtubule-nucleating capacity and size of the centrosome.
Article in The Journal of cell biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.
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Who cites it
49 citing papers in PubMed, 82 citations in OpenAlex.
- Light-induced spindle assembly through Aurora A clustering.EMBO reports · 2026Article
- Polo/PLK1 phosphorylation relieves Centrosomin/Cnn autoinhibition to promote centrosome scaffold assembly.The EMBO journal · 2026Article
- Centrosome-Signaling Pathway Crosstalk: A Core Hub From Cellular Homeostasis to Disease.Cytoskeleton (Hoboken, N.J.) · 2026Review
- The centriculum, a membrane reticulum that surrounds Caenorhabditis elegans centrosomes, might serve as a microtubule filter.Journal of cell science · 2026Article
- Bora, CEP192 and Cenexin regulate distinct Plk1-dependent cell and centrosome cycle transitions.Nature communications · 2026Article
- Phosphorylation remodels the mitotic centrosome matrix to generate bipartite γ-tubulin complex docking sites.Science advances · 2026Article
- A cell cycle-dependent transition of acetylation to phosphorylation regulates timely centrosome maturation.Nature communications · 2026Article
- Orchestrating homolog segregation in meiosis I: molecular logic and regulatory networks with emphasis on male metaphase I.Cell communication and signaling : CCS · 2026Review
- Tags Attached to the Centrosomal Protein SPD-5 Can Disrupt Centrosome Flattening During Anaphase of the 1-cellmicroPublication biology · 2026Article
- Aurora A regulates the material property of spindle poles to orchestrate nuclear organization at mitotic exit.The EMBO journal · 2025Article
- Polo-Like Kinase 1 Phosphorylation Tunes the Functional Viscoelastic Properties of the Centrosome Scaffold.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Phosphorylation remodels the mitotic centrosome matrix to generate bipartite γ-tubulin complex docking sites.bioRxiv : the preprint server for biology · 2025Article
- Inactivation of microtubule organizing center function of the centrosome is required for neuronal development and centriole elimination.bioRxiv : the preprint server for biology · 2025Article
- PLK-1 suppresses centrosome maturation and microtubule polymerization to ensure faithful oocyte meiosis.The Journal of cell biology · 2025Article
- RAS/ERK signaling and PLK1: Coordinating developmental regulation and disease mechanisms.Current opinion in cell biology · 2025Review
- Hybrid incompatibility emerges at the one-cell stage in interspecies Caenorhabditis embryos.Current biology : CB · 2025Article
- In vitro reconstitution of a minimal human centrosome scaffold capable of forming and clustering microtubule asters.Journal of cell science · 2025Article
- PLK1 Downregulation Attenuates ET-1-Induced Cardiomyocyte Hypertrophy by Suppressing the ERK1/2 Pathway.Journal of cardiovascular translational research · 2025Article
- Enhancement of CEP215 dynamics for spindle pole assembly during mitosis.Journal of cell science · 2025Article
- Enhancement of CEP215 dynamics for spindle pole assembly during mitosis.Journal of cell science · 2025Article
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
Abstract
Centrosomes are composed of a centriolar core surrounded by a pericentriolar material (PCM) matrix that docks microtubule-nucleating γ-tubulin complexes. During mitotic entry, the PCM matrix increases in size and nucleating capacity in a process called centrosome maturation. Polo-like kinase 1 (PLK1) is recruited to centrosomes and phosphorylates PCM matrix proteins to drive their self-assembly, which leads to PCM expansion. Here, we show that in addition to controlling PCM expansion, PLK1 independently controls the generation of binding sites for γ-tubulin complexes on the PCM matrix. Selectively preventing the generation of PLK1-dependent γ-tubulin docking sites led to spindle defects and impaired chromosome segregation without affecting PCM expansion, highlighting the importance of phospho-regulated centrosomal γ-tubulin docking sites in spindle assembly. Inhibiting both γ-tubulin docking and PCM expansion by mutating substrate target sites recapitulated the effects of loss of centrosomal PLK1 on the ability of centrosomes to catalyze spindle assembly.
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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.