期刊
JOURNAL OF CELL BIOLOGY
卷 195, 期 7, 页码 1093-1101出版社
ROCKEFELLER UNIV PRESS
DOI: 10.1083/jcb.201106093
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- Bio Imaging Research Center at the Gwangju Institute of Science and Technology
- Science Research Center [R11-2005-009-03005-0]
- Basic Science Research Program [20110025944]
- Brain Korea 21 Project
- National Research Foundation of Korea [2010-0022423, 2011-0006425] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
T he 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 (gamma-complex protein with WD repeats), gamma-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 gamma-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.
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