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Proteasome subunit Rpn13 is a novel ubiquitin receptor

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  • Koraljka Husnjak

    (Institute of 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)

  • Suzanne Elsasser

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

  • Naixia Zhang

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

  • Xiang Chen

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

  • Leah Randles

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

  • Yuan Shi

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

  • Kay Hofmann

    (Miltenyi Biotec GmbH, Stoeckheimer Weg 1, D-50829 Koeln, Germany)

  • Kylie J. Walters

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

  • Daniel Finley

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

  • Ivan Dikic

    (Institute of 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)

Abstract

Proteasomal receptors that recognize ubiquitin chains attached to substrates are key mediators of selective protein degradation in eukaryotes. Here we report the identification of a new ubiquitin receptor, Rpn13/ARM1, a known component of the proteasome. Rpn13 binds ubiquitin through a conserved amino-terminal region termed the pleckstrin-like receptor for ubiquitin (Pru) domain, which binds K48-linked diubiquitin with an affinity of approximately 90 nM. Like proteasomal ubiquitin receptor Rpn10/S5a, Rpn13 also binds ubiquitin-like (UBL) domains of UBL-ubiquitin-associated (UBA) proteins. In yeast, a synthetic phenotype results when specific mutations of the ubiquitin binding sites of Rpn10 and Rpn13 are combined, indicating functional linkage between these ubiquitin receptors. Because Rpn13 is also the proteasomal receptor for Uch37, a deubiquitinating enzyme, our findings suggest a coupling of chain recognition and disassembly at the proteasome.

Suggested Citation

  • Koraljka Husnjak & Suzanne Elsasser & Naixia Zhang & Xiang Chen & Leah Randles & Yuan Shi & Kay Hofmann & Kylie J. Walters & Daniel Finley & Ivan Dikic, 2008. "Proteasome subunit Rpn13 is a novel ubiquitin receptor," Nature, Nature, vol. 453(7194), pages 481-488, May.
    • Handle: RePEc:nat:nature:v:453:y:2008:i:7194:d:10.1038_nature06926
    DOI: 10.1038/nature06926
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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. Nathan Jespersen & Kai Ehrenbolger & Rahel R. Winiger & Dennis Svedberg & Charles R. Vossbrinck & Jonas Barandun, 2022. "Structure of the reduced microsporidian proteasome bound by PI31-like peptides in dormant spores," Nature Communications, Nature, vol. 13(1), pages 1-14, December.
    3. 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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