ArticleNature communications2023
Molecular basis for recognition and deubiquitination of 40S ribosomes by Otu2.
Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 19 citations in OpenAlex.
- Novel insights into the assembly of the yeast translation initiation multifactor complex: The critical role of eIF5.Protein science : a publication of the Protein Society · 2026Article
- Braess' Paradox in Enzyme Kinetics: Asymmetry from Population Balance without Direct Cooperativity.Journal of chemical theory and computation · 2026Article
- Proximity proteomics reveals OTUD6B regulation of stress granule dynamics through coalescence with VCP/p97.Cell death & disease · 2026Article
- Article
- The ribosome ubiquitination code: fine-tuning translation under stress.Trends in biochemical sciences · 2025Review
- Crucial roles of Grr1 in splicing and translation of HAC1 mRNA upon unfolded stress response.Nature communications · 2025Article
- Structural basis of AUC codon discrimination during translation initiation in yeast.Nucleic acids research · 2024Article
- OTUD6 deubiquitination of RPS7/eS7 on the free 40 S ribosome regulates global protein translation and stress.Nature communications · 2024Article
- Mitochondrial Ribosomal Protein MRPS15 Is a Component of Cytosolic Ribosomes and Regulates Translation in Stressed Cardiomyocytes.International journal of molecular sciences · 2024Article
- The structure of a human translation initiation complex reveals two independent roles for the helicase eIF4A.Nature structural & molecular biology · 2024Article
- Roles of the CCR4-Not complex in translation and dynamics of co-translation events.Wiley interdisciplinary reviews. RNA · 2023Review
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Authors and funding
10 authors at 5 institutions in 5 countries.
Funding
Abstract
In actively translating 80S ribosomes the ribosomal protein eS7 of the 40S subunit is monoubiquitinated by the E3 ligase Not4 and deubiquitinated by Otu2 upon ribosomal subunit recycling. Despite its importance for translation efficiency the exact role and structural basis for this translational reset is poorly understood. Here, structural analysis by cryo-electron microscopy of native and reconstituted Otu2-bound ribosomal complexes reveals that Otu2 engages 40S subunits mainly between ribosome recycling and initiation stages. Otu2 binds to several sites on the intersubunit surface of the 40S that are not occupied by any other 40S-binding factors. This binding mode explains the discrimination against 80S ribosomes via the largely helical N-terminal domain of Otu2 as well as the specificity for mono-ubiquitinated eS7 on 40S. Collectively, this study reveals mechanistic insights into the Otu2-driven deubiquitination steps for translational reset during ribosome recycling/(re)initiation.
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