PLK1 phosphorylation of pericentrin initiates centrosome maturation at the onset of mitosis
PLK1 phosphorylation of pericentrin initiates centrosome maturation at the onset of mitosis
The microtubule-organizing activity of the centrosome oscillates during the cell cycle, reaching its highest level at mitosis. At the onset of mitosis, the centrosome undergoes maturation, which is characterized by a drastic expansion of the pericentriolar matrix (PCM) and a robust increase in microtubule-organizing activity. It is known that PLK1 is critical for the initiation of centrosome maturation. In this paper, we report that pericentrin (PCNT), a PCM protein, was specifically phosphorylated by PLK1 during mitosis. Phosphoresistant point mutants of PCNT did not recruit centrosomal proteins, such as CEP192, GCP-WD (γ-complex protein with WD repeats), γ-tubulin, Aurora A, and PLK1, into the centrosome during mitosis. However, centrosomal recruitment of CEP215 depended on PCNT irrespective of its phosphorylation status. Furthermore, ectopic expression of PLK1-PCNT fusion proteins induced the centrosomal accumulation of CEP192, GCP-WD, and γ-tubulin even in interphase cells, mimicking centrosome maturation. Based on these results, we propose that PLK1-mediated phosphorylation of PCNT initiates centrosome maturation by organizing the spindle pole–specific PCM lattice.
- Seoul National University Korea (Republic of)
Centrosome, Recombinant Fusion Proteins, Mitosis, Cell Cycle Proteins, Spindle Apparatus, Protein Serine-Threonine Kinases, Microtubules, Models, Biological, Polo-Like Kinase 1, Proto-Oncogene Proteins, Humans, Protein Isoforms, Antigens, Phosphorylation, Interphase, Research Articles, Cells, Cultured, HeLa Cells
Centrosome, Recombinant Fusion Proteins, Mitosis, Cell Cycle Proteins, Spindle Apparatus, Protein Serine-Threonine Kinases, Microtubules, Models, Biological, Polo-Like Kinase 1, Proto-Oncogene Proteins, Humans, Protein Isoforms, Antigens, Phosphorylation, Interphase, Research Articles, Cells, Cultured, HeLa Cells
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