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A family of unconventional deubiquitinases with modular chain specificity determinants

Author

Listed:
  • Thomas Hermanns

    (University of Cologne)

  • Christian Pichlo

    (University of Cologne)

  • Ilka Woiwode

    (University of Cologne)

  • Karsten Klopffleisch

    (University of Cologne)

  • Katharina F. Witting

    (Leiden University Medical Center)

  • Huib Ovaa

    (Leiden University Medical Center)

  • Ulrich Baumann

    (University of Cologne)

  • Kay Hofmann

    (University of Cologne)

Abstract

Deubiquitinating enzymes (DUBs) regulate ubiquitin signaling by trimming ubiquitin chains or removing ubiquitin from modified substrates. Similar activities exist for ubiquitin-related modifiers, although the enzymes involved are usually not related. Here, we report human ZUFSP (also known as ZUP1 and C6orf113) and fission yeast Mug105 as founding members of a DUB family different from the six known DUB classes. The crystal structure of human ZUFSP in covalent complex with propargylated ubiquitin shows that the DUB family shares a fold with UFM1- and Atg8-specific proteases, but uses a different active site more similar to canonical DUB enzymes. ZUFSP family members differ widely in linkage specificity through differential use of modular ubiquitin-binding domains (UBDs). While the minimalistic Mug105 prefers K48 chains, ZUFSP uses multiple UBDs for its K63-specific endo-DUB activity. K63 specificity, localization, and protein interaction network suggest a role for ZUFSP in DNA damage response.

Suggested Citation

  • Thomas Hermanns & Christian Pichlo & Ilka Woiwode & Karsten Klopffleisch & Katharina F. Witting & Huib Ovaa & Ulrich Baumann & Kay Hofmann, 2018. "A family of unconventional deubiquitinases with modular chain specificity determinants," Nature Communications, Nature, vol. 9(1), pages 1-13, December.
    • Handle: RePEc:nat:natcom:v:9:y:2018:i:1:d:10.1038_s41467-018-03148-5
    DOI: 10.1038/s41467-018-03148-5
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    Cited by:

    1. Ilka Erven & Elena Abraham & Thomas Hermanns & Ulrich Baumann & Kay Hofmann, 2022. "A widely distributed family of eukaryotic and bacterial deubiquitinases related to herpesviral large tegument proteins," Nature Communications, Nature, vol. 13(1), pages 1-17, December.

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