Polo-like kinase 1 independently controls microtubule-nucleating capacity and size of the centrosome

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Journal of Cell Biology. 2021 Jul;220. doi: 10.1083/jcb.202009083

Polo-like kinase 1 independently controls microtubule-nucleating capacity and size of the centrosome Wang (Shaohe) Lab

Ohta M, Zhao Z, Wu D, Wang S, Harrison JL, Gómez-Cavazos JS, Desai A, Oegema KF

Note: Research in this publication was not performed at Janelia.

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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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Polo-like kinase 1 independently controls microtubule-nucleating capacity and size of the centrosome

Note: Research in this publication was not performed at Janelia.

Abstract

Janelia Authors