Evidence map›Paper›PMID 34318747›Full record

ArticleeLife2021

Processing of the ribosomal ubiquitin-like fusion protein FUBI-eS30/FAU is required for 40S maturation and depends on USP36.

Jasmin van den Heuvel, Caroline Ashiono, Ludovic C Gillet, Kerstin Dörner, Emanuel Wyler, Ivo Zemp, Ulrike Kutay

Open access · goldAbstract read
In one paragraph

Article in eLife, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.7field-weighted citation impact, top 15% 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

21 citing papers in PubMed, 37 citations in OpenAlex.

  1. RNAViruses · 2026
    Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Review
  14. Almost 50 Years of Monomeric Extracellular Ubiquitin (eUb).Pharmaceuticals (Basel, Switzerland) · 2024
    Review
  15. Article
  16. Review
  17. Review
  18. Article
  19. Article
  20. Review
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

7 authors at 1 institution in 1 country.

Jasmin van den HeuvelInstitute of Biochemistry, Department of Biology, ETH Zurich, Zurich, Switzerland.
Caroline AshionoInstitute of Biochemistry, Department of Biology, ETH Zurich, Zurich, Switzerland.
Ludovic C GilletInstitute of Biochemistry, Department of Biology, ETH Zurich, Zurich, Switzerland.ORCID 0000-0002-1001-3265
Kerstin DörnerInstitute of Biochemistry, Department of Biology, ETH Zurich, Zurich, Switzerland.
Emanuel WylerInstitute of Biochemistry, Department of Biology, ETH Zurich, Zurich, Switzerland.ORCID 0000-0002-9884-1806
Ivo ZempInstitute of Biochemistry, Department of Biology, ETH Zurich, Zurich, Switzerland.ORCID 0000-0003-1549-9871
Ulrike KutayInstitute of Biochemistry, Department of Biology, ETH Zurich, Zurich, Switzerland.ORCID 0000-0002-8257-7465
ETH Zurich · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In humans and other holozoan organisms, the ribosomal protein eS30 is synthesized as a fusion protein with the ubiquitin-like protein FUBI. However, FUBI is not part of the mature 40S ribosomal subunit and cleaved off by an as-of-yet unidentified protease. How FUBI-eS30 processing is coordinated with 40S subunit maturation is unknown. To study the mechanism and importance of FUBI-eS30 processing, we expressed non-cleavable mutants in human cells, which affected late steps of cytoplasmic 40S maturation, including the maturation of 18S rRNA and recycling of late-acting ribosome biogenesis factors. Differential affinity purification of wild-type and non-cleavable FUBI-eS30 mutants identified the deubiquitinase USP36 as a candidate FUBI-eS30 processing enzyme. Depletion of USP36 by RNAi or CRISPRi indeed impaired FUBI-eS30 processing and moreover, purified USP36 cut FUBI-eS30 in vitro. Together, these data demonstrate the functional importance of FUBI-eS30 cleavage and identify USP36 as a novel protease involved in this process.

Indexed as

Ribosome Subunits, Small, EukaryoticCloning, MolecularGene DeletionGene Expression RegulationHeLa CellsHumansRibosomal ProteinsRNA Processing, Post-TranscriptionalUbiquitinsUbiquitin ThiolesteraseFAU protein, humanRibosomal ProteinsUbiquitinsUbiquitin ThiolesteraseUSP36 protein, humanbiochemistrycell biologychemical biologyDUBFUBIhumannucleolusribosome biogenesistranslationubiquitin

Identifiers

PMID34318747
PMCPMC8354635
OpenAlexW3160957478

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.