Dynamic phosphorylation of CENP-A at Ser68 orchestrates its cell-cycle-dependent deposition at centromeres

Zhouliang Yu; Xiang Zhou; Wenjing Wang; Wenqiang Deng; Junnan Fang; Hao Hu; Zichen Wang; Shangze Li; Lei Cui; Jing Shen; Linhui Zhai; Shengyi Peng; Jiemin Wong; Shuo Dong; Zengqiang Yuan; Guangshuo Ou; Xiaodong Zhang; Ping Xu; Jizhong Lou; Na Yang; Ping Chen; Rui Ming Xu; Guohong Li

doi:10.1016/j.devcel.2014.11.030

Dynamic phosphorylation of CENP-A at Ser68 orchestrates its cell-cycle-dependent deposition at centromeres

Zhouliang Yu, Xiang Zhou, Wenjing Wang, Wenqiang Deng, Junnan Fang, Hao Hu, Zichen Wang, Shangze Li, Lei Cui, Jing Shen, Linhui Zhai, Shengyi Peng, Jiemin Wong, Shuo Dong, Zengqiang Yuan, Guangshuo Ou, Xiaodong Zhang, Ping Xu, Jizhong Lou, Na YangPing Chen, Rui Ming Xu, Guohong Li

Research output: Contribution to journal › Article › peer-review

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Abstract

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/PP1α 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.

Original language	English
Pages (from-to)	68-81
Number of pages	14
Journal	Developmental Cell
Volume	32
Issue number	1
DOIs	https://doi.org/10.1016/j.devcel.2014.11.030
State	Published - 2015
Externally published	Yes

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Yu, Z., Zhou, X., Wang, W., Deng, W., Fang, J., Hu, H., Wang, Z., Li, S., Cui, L., Shen, J., Zhai, L., Peng, S., Wong, J., Dong, S., Yuan, Z., Ou, G., Zhang, X., Xu, P., Lou, J., ... Li, G. (2015). Dynamic phosphorylation of CENP-A at Ser68 orchestrates its cell-cycle-dependent deposition at centromeres. Developmental Cell, 32(1), 68-81. https://doi.org/10.1016/j.devcel.2014.11.030

@article{55c79d95f0624907906dd8fc118b1f4f,

title = "Dynamic phosphorylation of CENP-A at Ser68 orchestrates its cell-cycle-dependent deposition at centromeres",

abstract = "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/PP1α 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.",

author = "Zhouliang Yu and Xiang Zhou and Wenjing Wang and Wenqiang Deng and Junnan Fang and Hao Hu and Zichen Wang and Shangze Li and Lei Cui and Jing Shen and Linhui Zhai and Shengyi Peng and Jiemin Wong and Shuo Dong and Zengqiang Yuan and Guangshuo Ou and Xiaodong Zhang and Ping Xu and Jizhong Lou and Na Yang and Ping Chen and Xu, {Rui Ming} and Guohong Li",

note = "Publisher Copyright: {\textcopyright} 2015 Elsevier Inc.",

year = "2015",

doi = "10.1016/j.devcel.2014.11.030",

language = "English",

volume = "32",

pages = "68--81",

journal = "Developmental Cell",

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publisher = "Cell Press",

number = "1",

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Yu, Z, Zhou, X, Wang, W, Deng, W, Fang, J, Hu, H, Wang, Z, Li, S, Cui, L, Shen, J, Zhai, L, Peng, S, Wong, J, Dong, S, Yuan, Z, Ou, G, Zhang, X, Xu, P, Lou, J, Yang, N, Chen, P, Xu, RM & Li, G 2015, 'Dynamic phosphorylation of CENP-A at Ser68 orchestrates its cell-cycle-dependent deposition at centromeres', Developmental Cell, vol. 32, no. 1, pp. 68-81. https://doi.org/10.1016/j.devcel.2014.11.030

TY - JOUR

T1 - Dynamic phosphorylation of CENP-A at Ser68 orchestrates its cell-cycle-dependent deposition at centromeres

AU - Yu, Zhouliang

AU - Zhou, Xiang

AU - Wang, Wenjing

AU - Deng, Wenqiang

AU - Fang, Junnan

AU - Hu, Hao

AU - Wang, Zichen

AU - Li, Shangze

AU - Cui, Lei

AU - Shen, Jing

AU - Zhai, Linhui

AU - Peng, Shengyi

AU - Wong, Jiemin

AU - Dong, Shuo

AU - Yuan, Zengqiang

AU - Ou, Guangshuo

AU - Zhang, Xiaodong

AU - Xu, Ping

AU - Lou, Jizhong

AU - Yang, Na

AU - Chen, Ping

AU - Xu, Rui Ming

AU - Li, Guohong

PY - 2015

Y1 - 2015

N2 - 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/PP1α 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.

AB - 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/PP1α 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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DO - 10.1016/j.devcel.2014.11.030

M3 - Article

C2 - 25556658

AN - SCOPUS:84922343527

SN - 1534-5807

VL - 32

SP - 68

EP - 81

JO - Developmental Cell

JF - Developmental Cell

IS - 1

ER -

Dynamic phosphorylation of CENP-A at Ser68 orchestrates its cell-cycle-dependent deposition at centromeres

Abstract

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