Evidence map›Paper›PMID 37443395›Full record

ArticleNature chemical biology2023

Molecular basis for ubiquitin/Fubi cross-reactivity in USP16 and USP36.

Rachel O'Dea, Nafizul Kazi, Alicia Hoffmann-Benito, Zhou Zhao, Sarah Recknagel, Kim Wendrich, Petra Janning, Malte Gersch

Open access · hybridAbstract read
In one paragraph

Article in Nature chemical biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
4.2field-weighted citation impact, top 5% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

20 citing papers in PubMed, 27 citations in OpenAlex.

  1. Review
  2. Article
  3. Synthetic Strategies for Activity-Based Probes to Decode Ubiquitin-Like Modifiers.Chemistry (Weinheim an der Bergstrasse, Germany) · 2026
    Review
  4. Article
  5. Article
  6. Review
  7. Article
  8. Selective Lysine Ubiquitination Using Activated Phenol Esters.Chembiochem : a European journal of chemical biology · 2025
    Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Review
  15. Article
  16. Review
  17. Article
  18. Review
  19. USP16 is an ISG15 cross-reactive deubiquitinase that targets pro-ISG15 and ISGylated proteins involved in metabolism.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors at 2 institutions in 1 country.

Rachel O'DeaChemical Genomics Centre, Max Planck Institute of Molecular Physiology, Dortmund, Germany.ORCID 0000-0002-3712-1178
Nafizul KaziChemical Genomics Centre, Max Planck Institute of Molecular Physiology, Dortmund, Germany.ORCID 0009-0004-3775-1497
Alicia Hoffmann-BenitoChemical Genomics Centre, Max Planck Institute of Molecular Physiology, Dortmund, Germany.
Zhou ZhaoChemical Genomics Centre, Max Planck Institute of Molecular Physiology, Dortmund, Germany.ORCID 0000-0001-9350-7238
Sarah RecknagelChemical Genomics Centre, Max Planck Institute of Molecular Physiology, Dortmund, Germany.
Kim WendrichChemical Genomics Centre, Max Planck Institute of Molecular Physiology, Dortmund, Germany.ORCID 0000-0002-8305-2847
Petra JanningDepartment of Chemical Biology, Max Planck Institute of Molecular Physiology, Dortmund, Germany.
Malte GerschChemical Genomics Centre, Max Planck Institute of Molecular Physiology, Dortmund, Germany. malte.gersch@mpi-dortmund.mpg.de.ORCID 0000-0003-2767-9589
TU Dortmund University · DEMax Planck Institute of Molecular Physiology · DE

Funding

Deutsche Forschungsgemeinschaft (German Research Foundation) 424228829 - SFB1430Max-Planck-Gesellschaft (Max Planck Society) CGC-III-352S
6 · The paper itself

Abstract

Ubiquitin and ubiquitin-like proteins typically use distinct machineries to facilitate diverse functions. The immunosuppressive ubiquitin-like protein Fubi is synthesized as an N-terminal fusion to a ribosomal protein (Fubi-S30). Its proteolytic maturation by the nucleolar deubiquitinase USP36 is strictly required for translationally competent ribosomes. What endows USP36 with this activity, how Fubi is recognized and whether other Fubi proteases exist are unclear. Here, we report a chemical tool kit that facilitated the discovery of dual ubiquitin/Fubi cleavage activity in USP16 in addition to USP36 by chemoproteomics. Crystal structures of USP36 complexed with Fubi and ubiquitin uncover its substrate recognition mechanism and explain how other deubiquitinases are restricted from Fubi. Furthermore, we introduce Fubi C-terminal hydrolase measurements and reveal a synergistic role of USP16 in Fubi-S30 maturation. Our data highlight how ubiquitin/Fubi specificity is achieved in a subset of human deubiquitinases and open the door to a systematic investigation of the Fubi system.

Indexed as

UbiquitinUbiquitin ThiolesteraseCell NucleolusEndopeptidasesHumansUbiquitinsEndopeptidasesUbiquitinUbiquitinsUbiquitin ThiolesteraseUSP16 protein, humanUSP36 protein, human

Identifiers

PMID37443395
PMCPMC10611586
OpenAlexW4384206345

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.