Evidence map›Paper›PMID 39121224›Full record

ArticleScience advances2024

A ubiquitin-specific, proximity-based labeling approach for the identification of ubiquitin ligase substrates.

Urbi Mukhopadhyay, Sophie Levantovsky, Teresa Maria Carusone, Sarah Gharbi, Frank Stein, Christian Behrends, Sagar Bhogaraju

Abstract read
In one paragraph

Article in Science advances, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
–field-weighted citation impact
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

24 citing papers in PubMed.

  1. Review
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  4. Proteomics-Driven Strategies for Proximity-Inducing Drug Discovery.Angewandte Chemie (International ed. in English) · 2026
    Review
  5. Review
  6. AbioRxiv : the preprint server for biology · 2026
    Article
  7. Review
  8. Article
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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

7 authors.

Urbi MukhopadhyayEuropean Molecular Biology Laboratory, 71 avenue des Martyrs, 38042 Grenoble, France.ORCID 0000-0002-7918-3051
Sophie LevantovskyMunich Cluster for Systems Neurology, Medical Faculty, Ludwig-Maximilians-Universität München, Munich, Germany.ORCID 0000-0002-0918-6871
Teresa Maria CarusoneEuropean Molecular Biology Laboratory, 71 avenue des Martyrs, 38042 Grenoble, France.ORCID 0000-0002-4069-2617
Sarah GharbiEuropean Molecular Biology Laboratory, 71 avenue des Martyrs, 38042 Grenoble, France.ORCID 0009-0008-4792-9411
Frank SteinProteomics Core Facility, European Molecular Biology Laboratory, Heidelberg, Germany.ORCID 0000-0001-9695-1692
Christian BehrendsMunich Cluster for Systems Neurology, Medical Faculty, Ludwig-Maximilians-Universität München, Munich, Germany.ORCID 0000-0002-9184-7607
Sagar BhogarajuEuropean Molecular Biology Laboratory, 71 avenue des Martyrs, 38042 Grenoble, France.ORCID 0000-0001-9998-5927

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Over 600 E3 ligases in humans execute ubiquitination of specific target proteins in a spatiotemporal manner to elicit desired signaling effects. Here, we developed a ubiquitin-specific proximity-based labeling method to selectively biotinylate substrates of a given ubiquitin ligase. By fusing the biotin ligase BirA and an Avi-tag variant to the candidate E3 ligase and ubiquitin, respectively, we were able to specifically enrich bona fide substrates of a ligase using a one-step streptavidin pulldown under denaturing conditions. We applied our method, which we named Ub-POD, to the really interesting new gene (RING) E3 ligase RAD18 and identified proliferating cell nuclear antigen and several other critical players in the DNA damage repair pathway. Furthermore, we successfully applied Ub-POD to the RING ubiquitin ligase tumor necrosis factor receptor-associated factor 6 and a U-box-type E3 ubiquitin ligase carboxyl terminus of Hsc70-interacting protein. We anticipate that our method could be widely adapted to all classes of ubiquitin ligases to identify substrates.

Indexed as

UbiquitinUbiquitinationUbiquitin-Protein LigasesBiotinylationDNA-Binding ProteinsHumansProliferating Cell Nuclear AntigenProtein BindingStaining and LabelingSubstrate SpecificityDNA-Binding ProteinsProliferating Cell Nuclear AntigenRAD18 protein, humanUbiquitinUbiquitin-Protein Ligases

Identifiers

PMID39121224
PMCPMC11313854

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Registered trials

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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.