IDEAS home Printed from https://ideas.repec.org/a/nat/natcom/v7y2016i1d10.1038_ncomms13343.html
   My bibliography  Save this article

BMI1 regulates PRC1 architecture and activity through homo- and hetero-oligomerization

Author

Listed:
  • Felicia Gray

    (University of Michigan)

  • Hyo Je Cho

    (University of Michigan)

  • Shirish Shukla

    (University of Michigan)

  • Shihan He

    (University of Michigan)

  • Ashley Harris

    (Translational Oncology Program, University of Michigan
    University of Michigan)

  • Bohdan Boytsov

    (University of Michigan)

  • Łukasz Jaremko

    (Deutsches Zentrum fur Neurodegenerative Erkrankungen (DZNE)
    Max-Planck Institute of Biophysical Chemistry)

  • Mariusz Jaremko

    (Max-Planck Institute of Biophysical Chemistry)

  • Borries Demeler

    (The University of Texas Health Science Center at San Antonio)

  • Elizabeth R. Lawlor

    (University of Michigan
    Translational Oncology Program, University of Michigan
    University of Michigan)

  • Jolanta Grembecka

    (University of Michigan)

  • Tomasz Cierpicki

    (University of Michigan)

Abstract

BMI1 is a core component of the polycomb repressive complex 1 (PRC1) and emerging data support a role of BMI1 in cancer. The central domain of BMI1 is involved in protein–protein interactions and is essential for its oncogenic activity. Here, we present the structure of BMI1 bound to the polyhomeotic protein PHC2 illustrating that the central domain of BMI1 adopts an ubiquitin-like (UBL) fold and binds PHC2 in a β-hairpin conformation. Unexpectedly, we find that the UBL domain is involved in homo-oligomerization of BMI1. We demonstrate that both the interaction of BMI1 with polyhomeotic proteins and homo-oligomerization via UBL domain are necessary for H2A ubiquitination activity of PRC1 and for clonogenic potential of U2OS cells. Here, we also emphasize need for joint application of NMR spectroscopy and X-ray crystallography to determine the overall structure of the BMI1–PHC2 complex.

Suggested Citation

  • Felicia Gray & Hyo Je Cho & Shirish Shukla & Shihan He & Ashley Harris & Bohdan Boytsov & Łukasz Jaremko & Mariusz Jaremko & Borries Demeler & Elizabeth R. Lawlor & Jolanta Grembecka & Tomasz Cierpick, 2016. "BMI1 regulates PRC1 architecture and activity through homo- and hetero-oligomerization," Nature Communications, Nature, vol. 7(1), pages 1-12, December.
    • Handle: RePEc:nat:natcom:v:7:y:2016:i:1:d:10.1038_ncomms13343
    DOI: 10.1038/ncomms13343
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/ncomms13343
    File Function: Abstract
    Download Restriction: no
    File URL: https://libkey.io/10.1038/ncomms13343?utm_source=ideas
    LibKey link: if access is restricted and if your library uses this service, LibKey will redirect you to where you can use your library subscription to access this item
    ---><---

    Citations

    Citations are extracted by the CitEc Project, subscribe to its RSS feed for this item.
    as


    Cited by:

    1. Shuo-Shuo Liu & Tian-Xia Jiang & Fan Bu & Ji-Lan Zhao & Guang-Fei Wang & Guo-Heng Yang & Jie-Yan Kong & Yun-Fan Qie & Pei Wen & Li-Bin Fan & Ning-Ning Li & Ning Gao & Xiao-Bo Qiu, 2024. "Molecular mechanisms underlying the BIRC6-mediated regulation of apoptosis and autophagy," Nature Communications, Nature, vol. 15(1), pages 1-16, December.
    2. Jorine M. Eeftens & Manya Kapoor & Davide Michieletto & Clifford P. Brangwynne, 2021. "Polycomb condensates can promote epigenetic marks but are not required for sustained chromatin compaction," Nature Communications, Nature, vol. 12(1), pages 1-12, December.

    More about this item

    Statistics

    Access and download statistics

    Corrections

    All material on this site has been provided by the respective publishers and authors. You can help correct errors and omissions. When requesting a correction, please mention this item's handle: RePEc:nat:natcom:v:7:y:2016:i:1:d:10.1038_ncomms13343. See general information about how to correct material in RePEc.

    If you have authored this item and are not yet registered with RePEc, we encourage you to do it here. This allows to link your profile to this item. It also allows you to accept potential citations to this item that we are uncertain about.

    We have no bibliographic references for this item. You can help adding them by using this form .

    If you know of missing items citing this one, you can help us creating those links by adding the relevant references in the same way as above, for each refering item. If you are a registered author of this item, you may also want to check the "citations" tab in your RePEc Author Service profile, as there may be some citations waiting for confirmation.

    For technical questions regarding this item, or to correct its authors, title, abstract, bibliographic or download information, contact: Sonal Shukla or Springer Nature Abstracting and Indexing (email available below). General contact details of provider: http://www.nature.com .

    Please note that corrections may take a couple of weeks to filter through the various RePEc services.

    IDEAS is a RePEc service. RePEc uses bibliographic data supplied by the respective publishers.