ArticleNucleic acids research2021
Large-scale movement of eIF3 domains during translation initiation modulate start codon selection.
Article in Nucleic acids research, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 34 citations in OpenAlex.
- Anagrelide Remodels the PDE3A-SLFN12 Interactome to Associate with Translation Initiation Machinery in Cancer Cell Lines.Molecular & cellular proteomics : MCP · 2026Article
- Article
- Toward a unifying mechanistic model of eukaryotic translation initiation through integrative single-molecule, structural, and computational insights.Current opinion in structural biology · 2026Review
- 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
- eIF3: a critical player in mRNA recruitment to the ribosome with emerging roles across translation.Biochemical Society transactions · 2025Review
- Structural insights into the role of eIF3 in translation mediated by the HCV IRES.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Deubiquitinases cleave ubiquitin-fused ribosomal proteins and physically counteract their targeting to the UFD pathway.Molecular cell · 2025Article
- Nonstop mutations cause loss of renal tumor suppressor proteinsScience advances · 2025Article
- Structural basis for translational control by the human 48S initiation complex.Nature structural & molecular biology · 2025Article
- Article
- Structural basis of AUC codon discrimination during translation initiation in yeast.Nucleic acids research · 2024Article
- A dynamic compositional equilibrium governs mRNA recognition by eIF3.bioRxiv : the preprint server for biology · 2024Article
- The molecular basis of translation initiation and its regulation in eukaryotes.Nature reviews. Molecular cell biology · 2024Review
- The structure of a human translation initiation complex reveals two independent roles for the helicase eIF4A.Nature structural & molecular biology · 2024Article
- Functional analysis of the AUG initiator codon context reveals novel conserved sequences that disfavor mRNA translation in eukaryotes.Nucleic acids research · 2024Article
- Rapid 40S scanning and its regulation by mRNA structure during eukaryotic translation initiation.Cell · 2022Article
- Selection of start codon during mRNA scanning in eukaryotic translation initiation.Communications biology · 2022Article
- Conformational rearrangements upon start codon recognition in human 48S translation initiation complex.Nucleic acids research · 2022Article
- Eukaryotic initiation factor 4F promotes a reorientation of eukaryotic initiation factor 3 binding on the 5' and the 3' UTRs of barley yellow dwarf virus mRNA.Nucleic acids research · 2022Article
- Regulation of the interactions between human eIF5 and eIF1A by the CK2 kinase.Current research in structural biology · 2022Article
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Authors and funding
6 authors at 5 institutions in 4 countries.
Funding
Abstract
The eukaryotic initiation factor 3 (eIF3) complex is involved in every step of translation initiation, but there is limited understanding of its molecular functions. Here, we present a single particle electron cryomicroscopy (cryo-EM) reconstruction of yeast 48S ribosomal preinitiation complex (PIC) in an open conformation conducive to scanning, with core subunit eIF3b bound on the 40S interface near the decoding center in contact with the ternary complex eIF2·GTP·initiator tRNA. eIF3b is relocated together with eIF3i from their solvent interface locations observed in other PIC structures, with eIF3i lacking 40S contacts. Re-processing of micrographs of our previous 48S PIC in a closed state also suggests relocation of the entire eIF3b-3i-3g-3a-Cter module during the course of initiation. Genetic analysis indicates that high fidelity initiation depends on eIF3b interactions at the 40S subunit interface that promote the closed PIC conformation, or facilitate the relocation of eIF3b/eIF3i to the solvent interface, on start codon selection.
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