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BAP1 complex promotes transcription by opposing PRC1-mediated H2A ubiquitylation

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Listed:
  • Antoine Campagne

    (Paris Sciences et Lettres Research University, Sorbonne University
    INSERM U934/CNRS UMR3215)

  • Ming-Kang Lee

    (Paris Sciences et Lettres Research University, Sorbonne University
    INSERM U934/CNRS UMR3215)

  • Dina Zielinski

    (Paris Sciences et Lettres Research University, Sorbonne University
    INSERM U934/CNRS UMR3215
    INSERM U900, Mines ParisTech)

  • Audrey Michaud

    (Paris Sciences et Lettres Research University, Sorbonne University
    INSERM U934/CNRS UMR3215)

  • Stéphanie Corre

    (Paris Sciences et Lettres Research University, Sorbonne University
    INSERM U934/CNRS UMR3215)

  • Florent Dingli

    (Paris Sciences et Lettres Research University, Sorbonne University)

  • Hong Chen

    (Paris Sciences et Lettres Research University, Sorbonne University
    INSERM U934/CNRS UMR3215)

  • Lara Z. Shahidian

    (Helmholtz Zentrum München)

  • Ivaylo Vassilev

    (Paris Sciences et Lettres Research University, Sorbonne University
    INSERM U934/CNRS UMR3215
    INSERM U900, Mines ParisTech)

  • Nicolas Servant

    (Paris Sciences et Lettres Research University, Sorbonne University
    INSERM U900, Mines ParisTech)

  • Damarys Loew

    (Paris Sciences et Lettres Research University, Sorbonne University)

  • Eric Pasmant

    (University of Paris Descartes)

  • Sophie Postel-Vinay

    (Université Paris-Saclay)

  • Michel Wassef

    (Paris Sciences et Lettres Research University, Sorbonne University
    INSERM U934/CNRS UMR3215)

  • Raphaël Margueron

    (Paris Sciences et Lettres Research University, Sorbonne University
    INSERM U934/CNRS UMR3215)

Abstract

In Drosophila, a complex consisting of Calypso and ASX catalyzes H2A deubiquitination and has been reported to act as part of the Polycomb machinery in transcriptional silencing. The mammalian homologs of these proteins (BAP1 and ASXL1/2/3, respectively), are frequently mutated in various cancer types, yet their precise functions remain unclear. Using an integrative approach based on isogenic cell lines generated with CRISPR/Cas9, we uncover an unanticipated role for BAP1 in gene activation. This function requires the assembly of an enzymatically active BAP1-associated core complex (BAP1.com) containing one of the redundant ASXL proteins. We investigate the mechanism underlying BAP1.com-mediated transcriptional regulation and show that it does not participate in Polycomb-mediated silencing. Instead, our results establish that the function of BAP1.com is to safeguard transcriptionally active genes against silencing by the Polycomb Repressive Complex 1.

Suggested Citation

  • Antoine Campagne & Ming-Kang Lee & Dina Zielinski & Audrey Michaud & Stéphanie Corre & Florent Dingli & Hong Chen & Lara Z. Shahidian & Ivaylo Vassilev & Nicolas Servant & Damarys Loew & Eric Pasmant , 2019. "BAP1 complex promotes transcription by opposing PRC1-mediated H2A ubiquitylation," Nature Communications, Nature, vol. 10(1), pages 1-15, December.
    • Handle: RePEc:nat:natcom:v:10:y:2019:i:1:d:10.1038_s41467-018-08255-x
    DOI: 10.1038/s41467-018-08255-x
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    Cited by:

    1. Moritz Binder & Ryan M. Carr & Terra L. Lasho & Christy M. Finke & Abhishek A. Mangaonkar & Christopher L. Pin & Kurt R. Berger & Amelia Mazzone & Sandeep Potluri & Tamas Ordog & Keith D. Robertson & , 2022. "Oncogenic gene expression and epigenetic remodeling of cis-regulatory elements in ASXL1-mutant chronic myelomonocytic leukemia," Nature Communications, Nature, vol. 13(1), pages 1-14, December.
    2. Nidhi Rohatgi & Wei Zou & Yongjia Li & Kevin Cho & Patrick L. Collins & Eric Tycksen & Gaurav Pandey & Carl J. DeSelm & Gary J. Patti & Anwesha Dey & Steven L. Teitelbaum, 2023. "BAP1 promotes osteoclast function by metabolic reprogramming," Nature Communications, Nature, vol. 14(1), pages 1-16, December.
    3. 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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