Polo-like kinase 1 independently controls microtubule-nucleating capacity and size of the centrosome
| Autor: | Jennifer L. Harrison, Zhiling Zhao, Di Wu, Karen Oegema, Arshad Desai, J Sebastian Gomez-Cavazos, Midori Ohta, Shaohe Wang |
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| Rok vydání: | 2021 |
| Předmět: |
animal structures
Mitosis Cell Cycle Proteins Spindle Apparatus Polo-like kinase Protein Serine-Threonine Kinases Microtubules PLK1 Chromosome segregation Tubulin Microtubule Report Animals Transgenes Phosphorylation Caenorhabditis elegans Caenorhabditis elegans Proteins skin and connective tissue diseases Cytoskeleton Pericentriolar material Centrosome biology urogenital system Cell Biology Cell biology embryonic structures biology.protein Protein Binding Cell Cycle and Division |
| Zdroj: | The Journal of Cell Biology |
| ISSN: | 1540-8140 0021-9525 |
| DOI: | 10.1083/jcb.202009083 |
| Popis: | Centrosomes increase in microtubule nucleating capacity during mitotic entry to catalyze spindle assembly. Ohta et al. show that Polo-like kinase 1 enables this increase by independently controlling the physical expansion of centrosomes and the generation of centrosomal microtubule-nucleating sites. 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. |
| Databáze: | OpenAIRE |
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