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TET2 promotes histone O-GlcNAcylation during gene transcription

Author

Listed:
  • Qiang Chen

    (University of Michigan Medical School, 1150 West Medical Center Drive, 5560A MSRBII, Ann Arbor, Michigan 48109, USA)

  • Yibin Chen

    (University of Michigan Medical School, 1150 West Medical Center Drive, 5560A MSRBII, Ann Arbor, Michigan 48109, USA)

  • Chunjing Bian

    (University of Michigan Medical School, 1150 West Medical Center Drive, 5560A MSRBII, Ann Arbor, Michigan 48109, USA)

  • Ryoji Fujiki

    (Institute of Molecular and Cellular Biosciences, University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-0032, Japan
    JST, PRESTO, 4-1-8 Honcho Kawaguchi, Saitama 332-0012, Japan)

  • Xiaochun Yu

    (University of Michigan Medical School, 1150 West Medical Center Drive, 5560A MSRBII, Ann Arbor, Michigan 48109, USA)

Abstract

TET2 is shown to associate with OGT, which catalyses O-GlcNAcylation, and the two enzymes are found together at transcription start sites; TET2 facilitates the activity of OGT in O-GlcNAcylation of histone 2B, and epigenetic modifications to both DNA and histones by TET2 and OGT may be important in gene transcription regulation.

Suggested Citation

  • Qiang Chen & Yibin Chen & Chunjing Bian & Ryoji Fujiki & Xiaochun Yu, 2013. "TET2 promotes histone O-GlcNAcylation during gene transcription," Nature, Nature, vol. 493(7433), pages 561-564, January.
    • Handle: RePEc:nat:nature:v:493:y:2013:i:7433:d:10.1038_nature11742
    DOI: 10.1038/nature11742
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    Cited by:

    1. Richard W. Meek & James N. Blaza & Jil A. Busmann & Matthew G. Alteen & David J. Vocadlo & Gideon J. Davies, 2021. "Cryo-EM structure provides insights into the dimer arrangement of the O-linked β-N-acetylglucosamine transferase OGT," Nature Communications, Nature, vol. 12(1), pages 1-10, December.
    2. Lijun Wang & Xiuling You & Dengfeng Ruan & Rui Shao & Hai-Qiang Dai & Weiliang Shen & Guo-Liang Xu & Wanlu Liu & Weiguo Zou, 2022. "TET enzymes regulate skeletal development through increasing chromatin accessibility of RUNX2 target genes," Nature Communications, Nature, vol. 13(1), pages 1-15, December.

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