Evidence map›Paper›PMID 26555268›Full record

ArticleThe Journal of biological chemistry2016

Structure of UBE2Z Enzyme Provides Functional Insight into Specificity in the FAT10 Protein Conjugation Machinery.

Julien Schelpe, Didier Monté, Frédérique Dewitte, Titia K Sixma, Prakash Rucktooa

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
1.4field-weighted citation impact, top 19% 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

23 citing papers in PubMed, 35 citations in OpenAlex.

  1. Article
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  4. Review
  5. Article
  6. Review
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  8. Article
  9. Article
  10. Ubiquitin Proteasome Gene Signatures in Ependymoma Molecular Subtypes.International journal of molecular sciences · 2022
    Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. UBA6 and Its Bispecific Pathways for Ubiquitin and FAT10.International journal of molecular sciences · 2019
    Review
  17. Article
  18. Article
  19. Review
  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

5 authors at 3 institutions in 2 countries.

Julien SchelpeFrom the UMR8576 CNRS-Université de Lille, 50 Avenue de Halley, 59658 Villeneuve d'Ascq, France and.
Didier MontéFrom the UMR8576 CNRS-Université de Lille, 50 Avenue de Halley, 59658 Villeneuve d'Ascq, France and.
Frédérique DewitteFrom the UMR8576 CNRS-Université de Lille, 50 Avenue de Halley, 59658 Villeneuve d'Ascq, France and.
Titia K SixmaDivision of Biochemistry and Centre for Biomedical Genetics, Netherlands Cancer Institute, Plesmanlaan 121, 1066 CX Amsterdam, The Netherlands.
Prakash RucktooaFrom the UMR8576 CNRS-Université de Lille, 50 Avenue de Halley, 59658 Villeneuve d'Ascq, France and Division of Biochemistry and Centre for Biomedical Genetics, Netherlands Cancer Institute, Plesmanlaan 121, 1066 CX Amsterdam, The Netherlands prakash.rucktooa@univ-lille1.fr.
Centre National de la Recherche Scientifique · FRUniversité de Lille · FRThe Netherlands Cancer Institute · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

FAT10 conjugation, a post-translational modification analogous to ubiquitination, specifically requires UBA6 and UBE2Z as its activating (E1) and conjugating (E2) enzymes. Interestingly, these enzymes can also function in ubiquitination. We have determined the crystal structure of UBE2Z and report how the different domains of this E2 enzyme are organized. We further combine our structural data with mutational analyses to understand how specificity is achieved in the FAT10 conjugation pathway. We show that specificity toward UBA6 and UBE2Z lies within the C-terminal CYCI tetrapeptide in FAT10. We also demonstrate that this motif slows down transfer rates for FAT10 from UBA6 onto UBE2Z.

Indexed as

Amino Acid SequenceCrystallography, X-RayKineticsMolecular Sequence DataMutant ProteinsPeptidesProtein Structure, SecondaryProtein Structure, TertiarySubstrate SpecificityUbiquitin-Activating EnzymesUbiquitin-Conjugating EnzymesUbiquitinsMutant ProteinsPeptidesUbiquitin-Activating EnzymesUbiquitin-Conjugating EnzymesUbiquitinscrystal structureFAT10post-translational modification (PTM)UBE2Zubiquitinubiquitin-conjugating enzyme (E2 enzyme)ubiquitylation (ubiquitination)UBL conjugation

Identifiers

PMID26555268
PMCPMC4705383
OpenAlexW2225725670

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.