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J Cell Biol. 2011 Dec 26;195(7):1093-101. doi: 10.1083/jcb.201106093. Epub 2011 Dec 19.

PLK1 phosphorylation of pericentrin initiates centrosome maturation at the onset of mitosis.

Author information

1
Department of Biological Sciences, Seoul National University, Seoul 151-747, South Korea.

Abstract

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.

PMID:
22184200
PMCID:
PMC3246884
DOI:
10.1083/jcb.201106093
[Indexed for MEDLINE]
Free PMC Article

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