Evidence map›Paper›PMID 33576509›Full record

ArticleThe EMBO journal2021

The UBA domain of conjugating enzyme Ubc1/Ube2K facilitates assembly of K48/K63-branched ubiquitin chains.

Lukas Pluska, Ernst Jarosch, Henrik Zauber, Andreas Kniss, Anita Waltho, Katrin Bagola, Maximilian von Delbrück, Frank Löhr, Brenda A Schulman, Matthias Selbach and 2 more

Open access · greenAbstract read
In one paragraph

Article in The EMBO journal, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
2.8field-weighted citation impact, top 8% 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

18 citing papers in PubMed, 46 citations in OpenAlex.

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  12. From seeds to trees: how E2 enzymes grow ubiquitin chains.Biochemical Society transactions · 2023
    Review
  13. Assembly and disassembly of branched ubiquitin chains.Frontiers in molecular biosciences · 2023
    Review
  14. Ubiquitin-modifying enzymes in Huntington's disease.Frontiers in molecular biosciences · 2023
    Review
  15. Review
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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

12 authors at 3 institutions in 1 country.

Lukas PluskaMax-Delbrück-Center for Molecular Medicine in the Helmholtz Association, Berlin-Buch, Germany.
Ernst JaroschMax-Delbrück-Center for Molecular Medicine in the Helmholtz Association, Berlin-Buch, Germany.
Henrik ZauberMax-Delbrück-Center for Molecular Medicine in the Helmholtz Association, Berlin-Buch, Germany.
Andreas KnissInstitute of Biophysical Chemistry and Center for Biomolecular Magnetic Resonance, Goethe University, Frankfurt am Main, Germany.
Anita WalthoMax-Delbrück-Center for Molecular Medicine in the Helmholtz Association, Berlin-Buch, Germany.
Katrin BagolaMax-Delbrück-Center for Molecular Medicine in the Helmholtz Association, Berlin-Buch, Germany.ORCID 0000-0003-0269-6454
Maximilian von DelbrückMax-Delbrück-Center for Molecular Medicine in the Helmholtz Association, Berlin-Buch, Germany.
Frank LöhrInstitute of Biophysical Chemistry and Center for Biomolecular Magnetic Resonance, Goethe University, Frankfurt am Main, Germany.
Brenda A SchulmanDepartment of Molecular Machines and Signaling, Max Planck Institute of Biochemistry, Martinsried, Germany.ORCID 0000-0002-3083-1126
Matthias SelbachMax-Delbrück-Center for Molecular Medicine in the Helmholtz Association, Berlin-Buch, Germany.
Volker DötschInstitute of Biophysical Chemistry and Center for Biomolecular Magnetic Resonance, Goethe University, Frankfurt am Main, Germany.
Thomas SommerMax-Delbrück-Center for Molecular Medicine in the Helmholtz Association, Berlin-Buch, Germany.ORCID 0000-0001-9990-5202
Max Delbrück Center · DEGoethe University Frankfurt · DEMax Planck Institute of Biochemistry · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The assembly of a specific polymeric ubiquitin chain on a target protein is a key event in the regulation of numerous cellular processes. Yet, the mechanisms that govern the selective synthesis of particular polyubiquitin signals remain enigmatic. The homologous ubiquitin-conjugating (E2) enzymes Ubc1 (budding yeast) and Ube2K (mammals) exclusively generate polyubiquitin linked through lysine 48 (K48). Uniquely among E2 enzymes, Ubc1 and Ube2K harbor a ubiquitin-binding UBA domain with unknown function. We found that this UBA domain preferentially interacts with ubiquitin chains linked through lysine 63 (K63). Based on structural modeling, in vitro ubiquitination experiments, and NMR studies, we propose that the UBA domain aligns Ubc1 with K63-linked polyubiquitin and facilitates the selective assembly of K48/K63-branched ubiquitin conjugates. Genetic and proteomics experiments link the activity of the UBA domain, and hence the formation of this unusual ubiquitin chain topology, to the maintenance of cellular proteostasis.

Indexed as

Computer SimulationModels, StructuralPolyubiquitinProtein DomainsProteomicsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSignal TransductionUbiquitinationUbiquitin-Conjugating EnzymesPolyubiquitinSaccharomyces cerevisiae ProteinsUBC1 protein, S cerevisiaeUBE2K protein, humanUbiquitin-Conjugating Enzymescell stressK48-linkedK63-linkedpolyubiquitinubiquitin-conjugating enzymes

Identifiers

PMID33576509
PMCPMC7957398
OpenAlexW3128179346

What OpenQuestion holds

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LicenceCC BY-NC-ND
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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.