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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
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    Citations

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    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. Jane Dudley-Fraser & Diego Esposito & Katherine A. McPhie & Coltrane Morley-Williams & Tania Auchynnikava & Katrin Rittinger, 2025. "Identification of RING E3 pseudoligases in the TRIM protein family," Nature Communications, Nature, vol. 16(1), pages 1-15, December.
    4. Juraj Ahel & Arda Balci & Victoria Faas & Daniel B. Grabarczyk & Roosa Harmo & Daniel R. Squair & Jiazhen Zhang & Elisabeth Roitinger & Frederic Lamoliatte & Sunil Mathur & Luiza Deszcz & Lillie E. Be, 2025. "ATP functions as a pathogen-associated molecular pattern to activate the E3 ubiquitin ligase RNF213," Nature Communications, Nature, vol. 16(1), pages 1-19, December.
    5. Xiangwei Wu & Huasong Ai & Junxiong Mao & Hongyi Cai & Lu-Jun Liang & Zebin Tong & Zhiheng Deng & Qingyun Zheng & Lei Liu & Man Pan, 2025. "Structural visualization of HECT-type E3 ligase Ufd4 accepting and transferring ubiquitin to form K29/K48-branched polyubiquitination," Nature Communications, Nature, vol. 16(1), pages 1-15, December.
    6. 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.

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