A comprehensive framework of E2-RING E3 interactions of the human ubiquitin-proteasome system
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Covalent attachment of ubiquitin to substrates is crucial to protein degradation, transcription regulation and cell signalling. Highly specific interactions between ubiquitin-conjugating enzymes (E2) and ubiquitin protein E3 ligases fulfil essential roles in this process. We performed a global yeast-two hybrid screen to study the specificity of interactions between catalytic domains of the 35 human E2s with 250 RING-type E3s. Our analysis showed over 300 high-quality interactions, uncovering a large fraction of new E2-E3 pairs. Both within the E2 and the E3 cohorts, several members were identified that are more versatile in their interaction behaviour than others. We also found that the physical interactions of our screen compare well with reported functional E2-E3 pairs in in vitro ubiquitination experiments. For validation we confirmed the interaction of several versatile E2s with E3s in in vitro protein interaction assays and we used mutagenesis to alter the E3 interactions of the E2 specific for K63 linkages, UBE2N(Ubc13), towards the K48-specific UBE2D2(UbcH5B). Our data provide a detailed, genome-wide overview of binary E2-E3 interactions of the human ubiquitination system.
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E3 ligases can interact with multiple E2 partners.
“The ability of E3 ligases to interact with multiple E2 partners is supported by recent global E2-E3 interaction screens (26,27).”
A large-scale computational and experimental study of interacting E2/E3 pairs revealed additional E2 enzymes that might contribute to Mdm2 ubiquitin ligase activity.
“Interestingly, a large-scale computational and experimental study of interacting E2/E3 pairs has revealed additional E2 s that might contribute to Mdm2 ubiquitin ligase activity [25].”
From The p53 orchestra: Mdm2 and Mdmx set the tone (2010) · cites this paper as [25]
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- Authors
- van Wijk, S. J. L., de Vries, S. J., Kemmeren, P., Huang, A., Boelens, R., Bonvin, A. M. J. J., & Timmers, H. T. M.
- Affiliations
- University Medical Center Utrecht (NL)
- Utrecht University (NL)
- Corresponding author
- Timmers, H Th Marc
- Venue
- Molecular Systems Biology
- Published
- 2009-08-18
- Volume
- 5
- Issue
- 1
- Pages
- 295-295
- ISSN
- 1744-4292 (ISSN-L)
- PMC
- PMC2736652
- OpenAlex
- W2116612021
- Cited by
- 164
- References
- 63
- Citations by year
- 2026: 3 · 2025: 7 · 2024: 5 · 2023: 8 · 2022: 11 · 2021: 7 · 2020: 9 · 2019: 10 · 2018: 14 · 2017: 6 · 2016: 7 · 2015: 10 · 2014: 9 · 2013: 17 · 2012: 21
- FWCI
- 5.50
- Type
- journal article
- Language
- en
- Update notices
- erratum (2009-10-13)
- Open access
- gold
- doi.org
- Licence
- Locations
- Molecular Systems Biology (publishedVersion, other-oa)
- Europe PMC (PubMed Central) (publishedVersion, cc-by-nc-nd)
- PubMed Central (publishedVersion, cc-by-nc-nd)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion)
- Utrecht University Repository (Utrecht University) (submittedVersion, other-oa)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Degradation and Inhibitors
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › NF-κB Signaling Pathways
- Keywords
- E2 ubiquitin-conjugating enzyme, RING E3 ligases, ubiquitination, ubiquitin-proteasome system, protein-protein interaction, yeast two-hybrid screen, UBE2N, UBE2D2, protein degradation
- MeSH terms
- Escherichia coli, Glutathione Transferase, Humans, Mutation, Proteins, Mutagenesis, Genome, Genome, Fungal, Catalytic Domain, Two-Hybrid System Techniques, Ubiquitin, Protein Interaction Mapping, Ubiquitin-Conjugating Enzymes, Cell Line, Tumor, Proteasome Endopeptidase Complex
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