Journal
DEVELOPMENTAL CELL
Volume 32, Issue 1, Pages 68-81Publisher
CELL PRESS
DOI: 10.1016/j.devcel.2014.11.030
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Funding
- Ministry of Science and Technology [2011CB966300]
- National Natural Science Foundation of China [91219202, 91019007, 31210103914, 31000566]
- Chinese Academy of Sciences [XDA01010304, KSZD-EW-Z-009]
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The H3 histone variant CENP-A is an epigenetic marker critical for the centromere identity and function. However, the precise regulation of the spatiotemporal deposition and propagation of CENP-A at centromeres during the cell cycle is still poorly understood. Here, we show that CENP-A is phosphorylated at Ser68 during early mitosis by Cdk1. Our results demonstrate that phosphorylation of Ser68 eliminates the binding of CENP-A to the assembly factor HJURP, thus preventing the premature loading of CENP-A to the centromere prior to mitotic exit. Because Cdk1 activity is at its minimum at the mitotic exit, the ratio of Cdk1/PP1 alpha activity changes in favor of Ser68 dephosphorylation, thus making CENP-A available for centromeric deposition by HJURP. Thus, we reveal that dynamic phosphorylation of CENP-A Ser68 orchestrates the spatiotemporal assembly of newly synthesized CENP-A at active centromeres during the cell cycle.
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