Evidence map›Paper›PMID 25556658›Full record

ArticleDevelopmental cell2015

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 and 13 more

Open access · bronzeAbstract read
PubMed Publisher
In one paragraph

Article in Developmental cell, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 71 papers.

0numbers the graph read from it
0cells of the map it votes in
71citing papers in PubMed
6.2field-weighted citation impact, top 3% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

71 citing papers in PubMed, 108 citations in OpenAlex.

  1. Review
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  3. Preserving centromere identity: right amounts of CENP-A at the right place and time.Chromosome research : an international journal on the molecular, supramolecular and evolutionary aspects of chromosome biology · 2025
    Review
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  13. CENP-I directly targets centromeric DNA to support CENP-A deposition and centromere maintenance.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  14. Review
  15. Review
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11 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

23 authors at 5 institutions in 2 countries.

Zhouliang YuNational Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China; University of Chinese Academy of Sciences, Beijing 100049, China.
Xiang ZhouNational Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China.
Wenjing WangNational Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China.
Wenqiang DengNational Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China; University of Chinese Academy of Sciences, Beijing 100049, China.
Junnan FangNational Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China; University of Chinese Academy of Sciences, Beijing 100049, China.
Hao HuNational Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China; University of Chinese Academy of Sciences, Beijing 100049, China.
Zichen WangNational Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China.
Shangze LiCollege of Life Sciences, Wuhan University, Wuhan, Hubei 430072, China.
Lei CuiNational Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China; Laboratory of Noncoding RNAs, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China.
Jing ShenNational Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China.
Linhui ZhaiState Key Laboratory of Proteomics, Beijing Proteome Research Center, Beijing Institute of Radiation Medicine, Beijing 102206, China.
Shengyi PengUniversity of Chinese Academy of Sciences, Beijing 100049, China; State Key Laboratory of Brain and Cognitive Sciences, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China.
Jiemin WongInstitute of Biomedical Sciences and School of Life Sciences, East China Normal University, Shanghai 200241, China.
Shuo DongDepartment of Medicine, Baylor College of Medicine, Houston, TX 77030, USA.
Zengqiang YuanState Key Laboratory of Brain and Cognitive Sciences, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China.
Guangshuo OuNational Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China.
Xiaodong ZhangCollege of Life Sciences, Wuhan University, Wuhan, Hubei 430072, China.
Ping XuState Key Laboratory of Proteomics, Beijing Proteome Research Center, Beijing Institute of Radiation Medicine, Beijing 102206, China.
Jizhong LouLaboratory of Noncoding RNAs, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China.
Na YangNational Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China.
Ping ChenNational Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China.
Rui-Ming XuNational Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China.
Guohong LiNational Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China. Electronic address: liguohong@sun5.ibp.ac.cn.
Chinese Academy of Sciences · CNBeijing Proteome Research Center · CNWuhan University · CNBaylor College of Medicine · USEast China Normal University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

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.

Indexed as

AutoantigensBlotting, WesternCDC2 Protein KinaseCell CycleCentromereCentromere Protein AChromatinChromosomal Proteins, Non-HistoneCyclin-Dependent KinasesDNA-Binding ProteinsFluorescent Antibody TechniqueHEK293 CellsHeLa CellsHumansImmunoprecipitationMitosisAutoantigensCDC2 Protein KinaseCDK1 protein, humanCENPA protein, humanCentromere Protein AChromatinChromosomal Proteins, Non-HistoneCyclin-Dependent KinasesDNA-Binding ProteinsHJURP protein, humanNucleosomesProtein Phosphatase 1Serine

Identifiers

PMID25556658
OpenAlexW2155658260

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.