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Ubiquitin docking at the proteasome through a novel pleckstrin-homology domain interaction

Author

Listed:
  • Patrick Schreiner

    (Lehrstuhl für Biochemie, Technische Universität München, Lichtenbergstrasse 4, D-85747 Garching, Germany)

  • Xiang Chen

    (Molecular Biology and Biophysics, University of Minnesota, Minneapolis, Minnesota 55455, USA)

  • Koraljka Husnjak

    (Institute for Biochemistry II and Cluster of Excellence Macromolecular Complexes, Goethe University, Theodor-Stern-Kai 7, D-60590 Frankfurt (Main), Germany
    Tumor Biology Program, Mediterranean Institute for Life Sciences, Mestrovicevo setaliste, 21000 Split, Croatia)

  • Leah Randles

    (Molecular Biology and Biophysics, University of Minnesota, Minneapolis, Minnesota 55455, USA)

  • Naixia Zhang

    (Molecular Biology and Biophysics, University of Minnesota, Minneapolis, Minnesota 55455, USA)

  • Suzanne Elsasser

    (Harvard Medical School, 240 Longwood Avenue, Boston, Massachusetts 02115, USA)

  • Daniel Finley

    (Harvard Medical School, 240 Longwood Avenue, Boston, Massachusetts 02115, USA)

  • Ivan Dikic

    (Institute for Biochemistry II and Cluster of Excellence Macromolecular Complexes, Goethe University, Theodor-Stern-Kai 7, D-60590 Frankfurt (Main), Germany
    Tumor Biology Program, Mediterranean Institute for Life Sciences, Mestrovicevo setaliste, 21000 Split, Croatia
    Medical School University of Split, Soltanska 2, 21000 Split, Croatia)

  • Kylie J. Walters

    (Molecular Biology and Biophysics, University of Minnesota, Minneapolis, Minnesota 55455, USA)

  • Michael Groll

    (Lehrstuhl für Biochemie, Technische Universität München, Lichtenbergstrasse 4, D-85747 Garching, Germany
    Institute of Biochemistry, Charité-Universitatsmedizin Berlin CCM, Monbijoustraße 2, D-10117 Berlin, Germany)

Abstract

Proteasomes: Ubiquitin binding via Rpn 13 The 26S proteasome is a multisubunit complex that selectively degrades ubiquitin conjugated proteins. Two studies show that a known component of the proteasome, Rpn13 functions as a novel ubiquitin binding receptor. Structural studies reveal a novel mode of ubiquitin recognition. Rpn 13 is also a receptor for a deubiquitinating enzyme, suggesting a linkage between ubiquitin chain recognition and disassembly.

Suggested Citation

  • Patrick Schreiner & Xiang Chen & Koraljka Husnjak & Leah Randles & Naixia Zhang & Suzanne Elsasser & Daniel Finley & Ivan Dikic & Kylie J. Walters & Michael Groll, 2008. "Ubiquitin docking at the proteasome through a novel pleckstrin-homology domain interaction," Nature, Nature, vol. 453(7194), pages 548-552, May.
    • Handle: RePEc:nat:nature:v:453:y:2008:i:7194:d:10.1038_nature06924
    DOI: 10.1038/nature06924
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    Cited by:

    1. Xiuxiu Lu & Monika Chandravanshi & Venkata R. Sabbasani & Snehal Gaikwad & V. Keith Hughitt & Nana Gyabaah-Kessie & Bradley T. Scroggins & Sudipto Das & Wazo Myint & Michelle E. Clapp & Charles D. Sch, 2024. "A structure-based designed small molecule depletes hRpn13Pru and a select group of KEN box proteins," Nature Communications, Nature, vol. 15(1), pages 1-18, December.
    2. Xiuxiu Lu & Venkata R. Sabbasani & Vasty Osei-Amponsa & Christine N. Evans & Julianna C. King & Sergey G. Tarasov & Marzena Dyba & Sudipto Das & King C. Chan & Charles D. Schwieters & Sulbha Choudhari, 2021. "Structure-guided bifunctional molecules hit a DEUBAD-lacking hRpn13 species upregulated in multiple myeloma," Nature Communications, Nature, vol. 12(1), pages 1-18, December.

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