IDEAS home Printed from https://ideas.repec.org/a/nat/nature/v503y2013i7476d10.1038_nature12638.html
   My bibliography  Save this article

Structural basis for ligase-specific conjugation of linear ubiquitin chains by HOIP

Author

Listed:
  • Benjamin Stieglitz

    (MRC National Institute for Medical Research, The Ridgeway, London NW7 1AA, UK)

  • Rohini R. Rana

    (MRC National Institute for Medical Research, The Ridgeway, London NW7 1AA, UK)

  • Marios G. Koliopoulos

    (MRC National Institute for Medical Research, The Ridgeway, London NW7 1AA, UK)

  • Aylin C. Morris-Davies

    (MRC National Institute for Medical Research, The Ridgeway, London NW7 1AA, UK)

  • Veronique Schaeffer

    (Institute of Biochemistry II, Goethe University, School of Medicine, Theodor-Stern-Kai 7, D-60590 Frankfurt (Main), Germany)

  • Evangelos Christodoulou

    (MRC National Institute for Medical Research, The Ridgeway, London NW7 1AA, UK)

  • Steven Howell

    (MRC National Institute for Medical Research, The Ridgeway, London NW7 1AA, UK)

  • Nicholas R. Brown

    (MRC National Institute for Medical Research, The Ridgeway, London NW7 1AA, UK)

  • Ivan Dikic

    (Institute of Biochemistry II, Goethe University, School of Medicine, Theodor-Stern-Kai 7, D-60590 Frankfurt (Main), Germany)

  • Katrin Rittinger

    (MRC National Institute for Medical Research, The Ridgeway, London NW7 1AA, UK)

Abstract

The crystal structure of a complex between the catalytic core of the HOIP subunit of the E3 ligase LUBAC and ubiquitin is reported, yielding insight into the ubiquitin transfer reaction and explaining how HOIP is capable of synthesizing linear ubiquitin chains with high specificity.

Suggested Citation

  • Benjamin Stieglitz & Rohini R. Rana & Marios G. Koliopoulos & Aylin C. Morris-Davies & Veronique Schaeffer & Evangelos Christodoulou & Steven Howell & Nicholas R. Brown & Ivan Dikic & Katrin Rittinger, 2013. "Structural basis for ligase-specific conjugation of linear ubiquitin chains by HOIP," Nature, Nature, vol. 503(7476), pages 422-426, November.
    • Handle: RePEc:nat:nature:v:503:y:2013:i:7476:d:10.1038_nature12638
    DOI: 10.1038/nature12638
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/nature12638
    File Function: Abstract
    Download Restriction: Access to the full text of the articles in this series is restricted.
    File URL: https://libkey.io/10.1038/nature12638?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
    ---><---

    As the access to this document is restricted, you may want to search for a different version of it.

    Citations

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


    Cited by:

    1. Xiangyi S. Wang & Thomas R. Cotton & Sarah J. Trevelyan & Lachlan W. Richardson & Wei Ting Lee & John Silke & Bernhard C. Lechtenberg, 2023. "The unifying catalytic mechanism of the RING-between-RING E3 ubiquitin ligase family," Nature Communications, Nature, vol. 14(1), pages 1-17, December.
    2. Yesheng Fu & Lei Li & Xin Zhang & Zhikang Deng & Ying Wu & Wenzhe Chen & Yuchen Liu & Shan He & Jian Wang & Yuping Xie & Zhiwei Tu & Yadi Lyu & Yange Wei & Shujie Wang & Chun-Ping Cui & Cui Hua Liu & , 2024. "Systematic HOIP interactome profiling reveals critical roles of linear ubiquitination in tissue homeostasis," Nature Communications, Nature, vol. 15(1), pages 1-19, December.
    3. Diego Esposito & Jane Dudley-Fraser & Acely Garza-Garcia & Katrin Rittinger, 2022. "Divergent self-association properties of paralogous proteins TRIM2 and TRIM3 regulate their E3 ligase activity," Nature Communications, Nature, vol. 13(1), pages 1-14, 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:nature:v:503:y:2013:i:7476:d:10.1038_nature12638. 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.