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Recognition of unmethylated histone H3 lysine 4 links BHC80 to LSD1-mediated gene repression

Author

Listed:
  • Fei Lan

    (Harvard Medical School, 77 Ave Louis Pasteur, Boston, Massachusetts 02115, USA)

  • Robert E. Collins

    (Emory University School of Medicine, 1510 Clifton Road, Atlanta, Georgia 30322, USA)

  • Rossella De Cegli

    (Harvard Medical School, 77 Ave Louis Pasteur, Boston, Massachusetts 02115, USA
    Università di Napoli ‘Federico II’, Via S. Pansini 5, 80131 Napoli, Italy
    Present address: Telethon Institute of Genetics and Medicine (TIGEM), Via P. Castellino 111, 80131 Naples, Italy.)

  • Roman Alpatov

    (Harvard Medical School, 77 Ave Louis Pasteur, Boston, Massachusetts 02115, USA)

  • John R. Horton

    (Emory University School of Medicine, 1510 Clifton Road, Atlanta, Georgia 30322, USA)

  • Xiaobing Shi

    (Stanford University, Stanford, California 94305, USA)

  • Or Gozani

    (Stanford University, Stanford, California 94305, USA)

  • Xiaodong Cheng

    (Emory University School of Medicine, 1510 Clifton Road, Atlanta, Georgia 30322, USA)

  • Yang Shi

    (Harvard Medical School, 77 Ave Louis Pasteur, Boston, Massachusetts 02115, USA)

Abstract

BHC80 is a component of the LSD1 co-repressor complex that demethylates histone H3 at lysine 4. The PHD domain of BHC80 interacts with the histone H3 tail only when lysine 4 is unmethylated, and BHC80 function is coupled to that of LSD1 in gene repression.

Suggested Citation

  • Fei Lan & Robert E. Collins & Rossella De Cegli & Roman Alpatov & John R. Horton & Xiaobing Shi & Or Gozani & Xiaodong Cheng & Yang Shi, 2007. "Recognition of unmethylated histone H3 lysine 4 links BHC80 to LSD1-mediated gene repression," Nature, Nature, vol. 448(7154), pages 718-722, August.
    • Handle: RePEc:nat:nature:v:448:y:2007:i:7154:d:10.1038_nature06034
    DOI: 10.1038/nature06034
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    Citations

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    Cited by:

    1. Dimitrios Spiliotopoulos & Andrea Spitaleri & Giovanna Musco, 2012. "Exploring PHD Fingers and H3K4me0 Interactions with Molecular Dynamics Simulations and Binding Free Energy Calculations: AIRE-PHD1, a Comparative Study," PLOS ONE, Public Library of Science, vol. 7(10), pages 1-13, October.
    2. Mandy S. M. Wan & Reyhan Muhammad & Marios G. Koliopoulos & Theodoros I. Roumeliotis & Jyoti S. Choudhary & Claudio Alfieri, 2023. "Mechanism of assembly, activation and lysine selection by the SIN3B histone deacetylase complex," Nature Communications, Nature, vol. 14(1), pages 1-13, December.
    3. Shengyong Yu & Chunhua Zhou & Jiangping He & Zhaokai Yao & Xingnan Huang & Bowen Rong & Hong Zhu & Shijie Wang & Shuyan Chen & Xialian Wang & Baomei Cai & Guoqing Zhao & Yuhan Chen & Lizhan Xiao & He , 2022. "BMP4 drives primed to naïve transition through PGC-like state," Nature Communications, Nature, vol. 13(1), pages 1-15, December.
    4. Yi Liu & Brian Debo & Mingfeng Li & Zhennan Shi & Wanqiang Sheng & Yang Shi, 2021. "LSD1 inhibition sustains T cell invigoration with a durable response to PD-1 blockade," Nature Communications, Nature, vol. 12(1), pages 1-16, December.
    5. Yi Zhang & Guojia Xie & Ji-Eun Lee & Mohamad Zandian & Deepthi Sudarshan & Benjamin Estavoyer & Caroline Benz & Tiina Viita & Golareh Asgaritarghi & Catherine Lachance & Clémence Messmer & Leandro Sim, 2024. "ASXLs binding to the PHD2/3 fingers of MLL4 provides a mechanism for the recruitment of BAP1 to active enhancers," Nature Communications, Nature, vol. 15(1), pages 1-15, December.

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