期刊
JOURNAL OF CELL BIOLOGY
卷 220, 期 2, 页码 -出版社
ROCKEFELLER UNIV PRESS
DOI: 10.1083/jcb.202009083
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资金
- National Institutes of Health [GM074207]
- Japan Society for the Promotion of Science
- Cancer Cell Biology training grant from the National Institutes of Health [T32 CA067754]
- Ruth L. Kirschstein Postdoctoral Individual National Research Service Award [F32GM125347]
PLK1 not only controls the expansion of PCM, but also independently regulates the generation of binding sites for gamma-tubulin complexes on the PCM matrix. Inhibiting PLK1-dependent gamma-tubulin docking sites leads to spindle defects and impaired chromosome segregation, highlighting the importance of phospho-regulated centrosomal gamma-tubulin docking sites in spindle assembly.
Centrosomes are composed of a centriolar core surrounded by a pericentriolar material (PCM) matrix that docks microtubulenucleating gamma-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.-tubulin complexes on the PCM matrix. Selectively preventing the generation of PLK1-dependent gamma-tubulin docking sites led to spindle defects and impaired chromosome segregation without affecting PCM expansion, highlighting the importance of phospho-regulated centrosomal.-tubulin docking sites in spindle assembly. Inhibiting both.-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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