ReviewProtein science : a publication of the Protein Society2019
Structural basis of generic versus specific E2-RING E3 interactions in protein ubiquitination.
Review in Protein science : a publication of the Protein Society, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed.
- Proteome analyses reveal endoplasmic reticulum stress-induced changes in protein abundance associated with Ube2j2 deficiency in human cell culture.G3 (Bethesda, Md.) · 2026Article
- Computational mapping of productive POI-E3 ligase conformations to guide de novo degrader design: application to WEE1 and PKMYT1 PROTACs.Journal of cheminformatics · 2026Article
- Photocross-linking activity-based probes to capture the dynamics of ubiquitin RING E3 ligase interactions.The Biochemical journal · 2026Article
- Article
- Structural basis of receptor retro-translocation in peroxisomal protein import.bioRxiv : the preprint server for biology · 2026Article
- Targeting the Ubiquitin-Proteasome System for Cancer.MedComm · 2025Review
- TRIM37 prevents ectopic spindle pole assembly by peptide motif recognition and substrate-dependent oligomerization.Nature structural & molecular biology · 2025Article
- The ribosome-associated quality control factor TCF25 imposes K48 specificity on Listerin-mediated ubiquitination of nascent chains by binding and specifically orienting the acceptor ubiquitin.Genes & development · 2025Article
- Structure predictions of MuRF1-UBE2 complexes identify amino acid residues governing interaction selectivity for each MuRF1-E2 pair.The FEBS journal · 2025Article
- TRIM52 maintains cellular fitness and is under tight proteolytic control by multiple giant E3 ligases.Nature communications · 2025Article
- A nanobody that binds to the backside of the ubiquitin conjugating enzyme Ube2G2 differentially affects interactions with its partner E3 Ligases.Communications biology · 2025Article
- Targeted protein degradation using chimeric human E2 ubiquitin-conjugating enzymes.Communications biology · 2024Article
- Role of ubiquitination in the occurrence and development of osteoporosis (Review).International journal of molecular medicine · 2024Review
- Review
- Discovery and characterization of noncanonical E2-conjugating enzymes.Science advances · 2024Article
- Molecular basis for PHF7-mediated ubiquitination of histone H3.Genes & development · 2023Article
- Mechanism of histone H2B monoubiquitination by Bre1.Nature structural & molecular biology · 2023Article
- Structure and functional determinants of Rad6-Bre1 subunits in the histone H2B ubiquitin-conjugating complex.Nucleic acids research · 2023Article
- Article
- Emerging Roles of RNF168 in Tumor Progression.Molecules (Basel, Switzerland) · 2023Review
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2 authors.
Funding
Abstract
Protein ubiquitination is a fundamental regulatory component in eukaryotic cell biology, where a cascade of ubiquitin activating (E1), conjugating (E2), and ligating (E3) enzymes assemble distinct ubiquitin signals on target proteins. E2s specify the type of ubiquitin signal generated, while E3s associate with the E2~Ub conjugate and select the substrate for ubiquitination. Thus, producing the right ubiquitin signal on the right target requires the right E2-E3 pair. The question of how over 600 E3s evolved to discriminate between 38 structurally related E2s has therefore been an area of intensive research, and with over 50 E2-E3 complex structures generated to date, the answer is beginning to emerge. The following review discusses the structural basis of generic E2-RING E3 interactions, contrasted with emerging themes that reveal how specificity can be achieved.
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Registered trials
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.