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Arkadia/RNF111 is a SUMO-targeted ubiquitin ligase with preference for substrates marked with SUMO1-capped SUMO2/3 chain

Author

Listed:
  • Annie M. Sriramachandran

    (University of Cologne, Center of Molecular Biosciences
    Institute of Molecular Biology)

  • Katrin Meyer-Teschendorf

    (University of Cologne, Center of Molecular Biosciences
    University of Cologne)

  • Stefan Pabst

    (University of Cologne, Center of Molecular Biosciences)

  • Helle D. Ulrich

    (Institute of Molecular Biology)

  • Niels H. Gehring

    (University of Cologne, Center of Molecular Biosciences)

  • Kay Hofmann

    (University of Cologne, Center of Molecular Biosciences)

  • Gerrit J. K. Praefcke

    (University of Cologne, Center of Molecular Biosciences
    University of Cologne
    Department of Haematology and Transfusion Medicine)

  • R. Jürgen Dohmen

    (University of Cologne, Center of Molecular Biosciences)

Abstract

Modification with SUMO regulates many eukaryotic proteins. Down-regulation of sumoylated forms of proteins involves either their desumoylation, and hence recycling of the unmodified form, or their proteolytic targeting by ubiquitin ligases that recognize their SUMO modification (termed STUbL or ULS). STUbL enzymes such as Uls1 and Slx5-Slx8 in budding yeast or RNF4 and Arkadia/RNF111 in humans bear multiple SUMO interaction motifs to recognize substrates carrying poly-SUMO chains. Using yeast as experimental system and isothermal titration calorimetry, we here show that Arkadia specifically selects substrates carrying SUMO1-capped SUMO2/3 hybrid conjugates and targets them for proteasomal degradation. Our data suggest that a SUMO1-specific binding site in Arkadia with sequence similarity to a SUMO1-binding site in DPP9 is required for targeting endogenous hybrid SUMO conjugates and PML nuclear bodies in human cells. We thus characterize Arkadia as a STUbL with a preference for substrate proteins marked with distinct hybrid SUMO chains.

Suggested Citation

  • Annie M. Sriramachandran & Katrin Meyer-Teschendorf & Stefan Pabst & Helle D. Ulrich & Niels H. Gehring & Kay Hofmann & Gerrit J. K. Praefcke & R. Jürgen Dohmen, 2019. "Arkadia/RNF111 is a SUMO-targeted ubiquitin ligase with preference for substrates marked with SUMO1-capped SUMO2/3 chain," Nature Communications, Nature, vol. 10(1), pages 1-12, December.
    • Handle: RePEc:nat:natcom:v:10:y:2019:i:1:d:10.1038_s41467-019-11549-3
    DOI: 10.1038/s41467-019-11549-3
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    Cited by:

    1. Andrej Paluda & Adam J. Middleton & Claudia Rossig & Peter D. Mace & Catherine L. Day, 2022. "Ubiquitin and a charged loop regulate the ubiquitin E3 ligase activity of Ark2C," Nature Communications, Nature, vol. 13(1), pages 1-12, December.
    2. Orhi Barroso-Gomila & Fredrik Trulsson & Veronica Muratore & Iñigo Canosa & Laura Merino-Cacho & Ana Rosa Cortazar & Coralia Pérez & Mikel Azkargorta & Ibon Iloro & Arkaitz Carracedo & Ana M. Aransay , 2021. "Identification of proximal SUMO-dependent interactors using SUMO-ID," Nature Communications, Nature, vol. 12(1), pages 1-19, December.
    3. Shichang Liu & Erin Atkinson & Adriana Paulucci-Holthauzen & Bin Wang, 2023. "A CK2 and SUMO-dependent, PML NB-involved regulatory mechanism controlling BLM ubiquitination and G-quadruplex resolution," Nature Communications, Nature, vol. 14(1), pages 1-15, December.

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