Evidence map›Paper›PMID 31575873›Full record

ArticleNature communications2019

The ubiquitin-like modifier FAT10 interferes with SUMO activation.

Annette Aichem, Carolin Sailer, Stella Ryu, Nicola Catone, Nicolas Stankovic-Valentin, Gunter Schmidtke, Frauke Melchior, Florian Stengel, Marcus Groettrup

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
2.7field-weighted citation impact, top 9% 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

28 citing papers in PubMed, 46 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. METTL3-mediated mOncogene · 2024
    Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Signalling mechanisms and cellular functions of SUMO.Nature reviews. Molecular cell biology · 2022
    Review
  17. Article
  18. Thapsigargin: key to new host-directed coronavirus antivirals?Trends in pharmacological sciences · 2022
    Review
  19. Article
  20. Insights in Post-Translational Modifications: Ubiquitin and SUMO.International journal of molecular sciences · 2022
    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

9 authors at 3 institutions in 2 countries.

Annette AichemBiotechnology Institute Thurgau at the University of Konstanz, CH-8280, Kreuzlingen, Switzerland. Annette.Aichem@bitg.ch.
Carolin SailerDepartment of Biology, University of Konstanz, D-78457, Konstanz, Germany.
Stella RyuBiotechnology Institute Thurgau at the University of Konstanz, CH-8280, Kreuzlingen, Switzerland.
Nicola CatoneBiotechnology Institute Thurgau at the University of Konstanz, CH-8280, Kreuzlingen, Switzerland.
Nicolas Stankovic-ValentinZentrum für Molekulare Biologie der Universität Heidelberg, DKFZ-ZMBH Alliance, D-69120, Heidelberg, Germany.
Gunter SchmidtkeDepartment of Biology, Division of Immunology, University of Konstanz, D-78457, Konstanz, Germany.
Frauke MelchiorZentrum für Molekulare Biologie der Universität Heidelberg, DKFZ-ZMBH Alliance, D-69120, Heidelberg, Germany.
Florian StengelDepartment of Biology, University of Konstanz, D-78457, Konstanz, Germany.ORCID http://orcid.org/0000-0003-1447-4509
Marcus GroettrupBiotechnology Institute Thurgau at the University of Konstanz, CH-8280, Kreuzlingen, Switzerland.ORCID http://orcid.org/0000-0002-5423-6399
University of Konstanz · DEHeidelberg University · DEBiotechnology Institute Thurgau · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The covalent attachment of the cytokine-inducible ubiquitin-like modifier HLA-F adjacent transcript 10 (FAT10) to hundreds of substrate proteins leads to their rapid degradation by the 26 S proteasome independently of ubiquitylation. Here, we identify another function of FAT10, showing that it interferes with the activation of SUMO1/2/3 in vitro and down-regulates SUMO conjugation and the SUMO-dependent formation of promyelocytic leukemia protein (PML) bodies in cells. Mechanistically, we show that FAT10 directly binds to and impedes the activity of the heterodimeric SUMO E1 activating enzyme AOS1/UBA2 by competing very efficiently with SUMO for activation and thioester formation. Nevertheless, activation of FAT10 by AOS1/UBA2 does not lead to covalent conjugation of FAT10 with substrate proteins which relies on its cognate E1 enzyme UBA6. Hence, we report that one ubiquitin-like modifier (FAT10) inhibits the conjugation and function of another ubiquitin-like modifier (SUMO) by impairing its activation.

Indexed as

Down-RegulationGene Knockdown TechniquesHEK293 CellsHumansPromyelocytic Leukemia ProteinProteasome Endopeptidase ComplexProtein Processing, Post-TranslationalRecombinant ProteinsSmall Ubiquitin-Related Modifier ProteinsSUMO-1 ProteinTranscription FactorsUbiquitin-Activating EnzymesUbiquitinationUbiquitinsATP dependent 26S proteaseJunB protein, humanPML protein, humanPromyelocytic Leukemia ProteinProteasome Endopeptidase ComplexRecombinant ProteinsSAE1 protein, humanSmall Ubiquitin-Related Modifier ProteinsSUMO-1 ProteinSUMO1 protein, humanSUMO2 protein, humanSUMO3 protein, humanTranscription FactorsUBA2 protein, humanUBA6 protein, humanUBD protein, humanUbiquitin-Activating EnzymesUbiquitins

Identifiers

PMID31575873
PMCPMC6773726
OpenAlexW2977510709

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.