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Polycomb group-mediated histone H2A monoubiquitination in epigenome regulation and nuclear processes

Author

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  • Haithem Barbour

    (University of Montréal)

  • Salima Daou

    (University of Montréal
    Sinai Health System)

  • Michael Hendzel

    (University of Alberta, Room 3332 Cross Cancer Institute, 11560 University Avenue NW)

  • El Bachir Affar

    (University of Montréal)

Abstract

Histone posttranslational modifications are key regulators of chromatin-associated processes including gene expression, DNA replication and DNA repair. Monoubiquitinated histone H2A, H2Aub (K118 in Drosophila or K119 in vertebrates) is catalyzed by the Polycomb group (PcG) repressive complex 1 (PRC1) and reversed by the PcG-repressive deubiquitinase (PR-DUB)/BAP1 complex. Here we critically assess the current knowledge regarding H2Aub deposition and removal, its crosstalk with PcG repressive complex 2 (PRC2)-mediated histone H3K27 methylation, and the recent attempts toward discovering its readers and solving its enigmatic functions. We also discuss mounting evidence of the involvement of H2A ubiquitination in human pathologies including cancer, while highlighting some knowledge gaps that remain to be addressed.

Suggested Citation

  • Haithem Barbour & Salima Daou & Michael Hendzel & El Bachir Affar, 2020. "Polycomb group-mediated histone H2A monoubiquitination in epigenome regulation and nuclear processes," Nature Communications, Nature, vol. 11(1), pages 1-16, December.
    • Handle: RePEc:nat:natcom:v:11:y:2020:i:1:d:10.1038_s41467-020-19722-9
    DOI: 10.1038/s41467-020-19722-9
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    Cited by:

    1. James Godwin & Mohan Govindasamy & Kiruba Nedounsejian & Eduardo March & Ronan Halton & Clara Bourbousse & Léa Wolff & Antoine Fort & Michal Krzyszton & Jesús López Corrales & Szymon Swiezewski & Fred, 2024. "The UBP5 histone H2A deubiquitinase counteracts PRCs-mediated repression to regulate Arabidopsis development," Nature Communications, Nature, vol. 15(1), pages 1-14, December.
    2. Yu Zhang & Min Ma & Meng Liu & Aiqing Sun & Xiaoyun Zheng & Kunpeng Liu & Chunmei Yin & Chuanshun Li & Cizhong Jiang & Xiaoyu Tu & Yuda Fang, 2023. "Histone H2A monoubiquitination marks are targeted to specific sites by cohesin subunits in Arabidopsis," Nature Communications, Nature, vol. 14(1), pages 1-12, December.
    3. Pawel Mikulski & Philip Wolff & Tiancong Lu & Mathias Nielsen & Elsa Franco Echevarria & Danling Zhu & Julia I. Questa & Gerhard Saalbach & Carlo Martins & Caroline Dean, 2022. "VAL1 acts as an assembly platform co-ordinating co-transcriptional repression and chromatin regulation at Arabidopsis FLC," Nature Communications, Nature, vol. 13(1), pages 1-12, December.
    4. Julian Cheron & Leonardo Beccari & Perrine Hagué & Romain Icick & Chloé Despontin & Teresa Carusone & Matthieu Defrance & Sagar Bhogaraju & Elena Martin-Garcia & Roberto Capellan & Rafael Maldonado & , 2023. "USP7/Maged1-mediated H2A monoubiquitination in the paraventricular thalamus: an epigenetic mechanism involved in cocaine use disorder," Nature Communications, Nature, vol. 14(1), pages 1-18, December.
    5. C. W. Ryan & S. L. Regan & E. F. Mills & B. T. McGrath & E. Gong & Y. T. Lai & J. B. Sheingold & K. Patel & T. Horowitz & A. Moccia & Y. C. Tsan & A. Srivastava & S. L. Bielas, 2024. "RING1 missense variants reveal sensitivity of DNA damage repair to H2A monoubiquitination dosage during neurogenesis," Nature Communications, Nature, vol. 15(1), pages 1-20, December.

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