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Regulation of p53 activity through lysine methylation

Author

Listed:
  • Sergei Chuikov

    (Robert Wood Johnson Medical School)

  • Julia K. Kurash

    (Molecular Oncology Research Institute, NEMC-Tufts School of Medicine)

  • Jonathan R. Wilson

    (MRC-NIMR)

  • Bing Xiao

    (MRC-NIMR)

  • Neil Justin

    (MRC-NIMR)

  • Gleb S. Ivanov

    (Molecular Oncology Research Institute, NEMC-Tufts School of Medicine)

  • Kristine McKinney

    (Columbia University)

  • Paul Tempst

    (Memorial Sloan Kettering Cancer Center)

  • Carol Prives

    (Columbia University)

  • Steven J. Gamblin

    (MRC-NIMR)

  • Nickolai A. Barlev

    (Molecular Oncology Research Institute, NEMC-Tufts School of Medicine)

  • Danny Reinberg

    (Robert Wood Johnson Medical School)

Abstract

p53 is a tumour suppressor that regulates the cellular response to genotoxic stresses. p53 is a short-lived protein and its activity is regulated mostly by stabilization via different post-translational modifications. Here we report a novel mechanism of p53 regulation through lysine methylation by Set9 methyltransferase. Set9 specifically methylates p53 at one residue within the carboxyl-terminus regulatory region. Methylated p53 is restricted to the nucleus and the modification positively affects its stability. Set9 regulates the expression of p53 target genes in a manner dependent on the p53-methylation site. The crystal structure of a ternary complex of Set9 with a p53 peptide and the cofactor product S-adenosyl-l-homocysteine (AdoHcy) provides the molecular basis for recognition of p53 by this lysine methyltransferase.

Suggested Citation

  • Sergei Chuikov & Julia K. Kurash & Jonathan R. Wilson & Bing Xiao & Neil Justin & Gleb S. Ivanov & Kristine McKinney & Paul Tempst & Carol Prives & Steven J. Gamblin & Nickolai A. Barlev & Danny Reinb, 2004. "Regulation of p53 activity through lysine methylation," Nature, Nature, vol. 432(7015), pages 353-360, November.
    • Handle: RePEc:nat:nature:v:432:y:2004:i:7015:d:10.1038_nature03117
    DOI: 10.1038/nature03117
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    Cited by:

    1. Ji Min Lee & Henrik M. Hammarén & Mikhail M. Savitski & Sung Hee Baek, 2023. "Control of protein stability by post-translational modifications," Nature Communications, Nature, vol. 14(1), pages 1-16, December.
    2. Yan Gu & Yanrong Chen & Lai Wei & Shuang Wu & Kaicheng Shen & Chengxiang Liu & Yan Dong & Yang Zhao & Yue Zhang & Chi Zhang & Wenling Zheng & Jiangyi He & Yunlong Wang & Yifei Li & Xiaoxin Zhao & Hong, 2021. "ABHD5 inhibits YAP-induced c-Met overexpression and colon cancer cell stemness via suppressing YAP methylation," Nature Communications, Nature, vol. 12(1), pages 1-15, December.
    3. Yatian Li & Zhenyue Gao & Yuhong Wang & Bo Pang & Binbin Zhang & Ruxin Hu & Yuqing Wang & Chao Liu & Xuebin Zhang & Jingxuan Yang & Mei Mei & Yongzhi Wang & Xuan Zhou & Min Li & Yu Ren, 2023. "Lysine methylation promotes NFAT5 activation and determines temozolomide efficacy in glioblastoma," Nature Communications, Nature, vol. 14(1), pages 1-19, December.

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