ArticleThe EMBO journal2002
Direct eIF2-eIF3 contact in the multifactor complex is important for translation initiation in vivo.
Article in The EMBO journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 70 papers.
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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.
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Who cites it
70 citing papers in PubMed, 130 citations in OpenAlex.
- mActa pharmaceutica Sinica. B · 2025Review
- A dynamic compositional equilibrium governs mRNA recognition by eIF3.bioRxiv : the preprint server for biology · 2024Article
- eIF3j inhibits translation of a subset of circular RNAs in eukaryotic cells.Nucleic acids research · 2022Article
- Eukaryotic translation initiation factor 3 subunit B promotes head and neck cancer via CEBPB translation.Cancer cell international · 2022Article
- Phosphorylation of a reinitiation supporting protein, RISP, determines its function in translation reinitiation.Nucleic acids research · 2021Article
- Ribosome quality control antagonizes the activation of the integrated stress response on colliding ribosomes.Molecular cell · 2021Article
- A structural inventory of native ribosomal ABCE1-43S pre-initiation complexes.The EMBO journal · 2021Article
- eIF3 and Its mRNA-Entry-Channel Arm Contribute to the Recruitment of mRNAs With Long 5'-Untranslated Regions.Frontiers in molecular biosciences · 2021Article
- Selective Translation Complex Profiling Reveals Staged Initiation and Co-translational Assembly of Initiation Factor Complexes.Molecular cell · 2020Article
- Engineered transient and stable overexpression of translation factors eIF3i and eIF3c in CHOK1 and HEK293 cells gives enhanced cell growth associated with increased c-Myc expression and increased recombinant protein synthesis.Metabolic engineering · 2020Article
- Adapted formaldehyde gradient cross-linking protocol implicates human eIF3d and eIF3c, k and l subunits in the 43S and 48S pre-initiation complex assembly, respectively.Nucleic acids research · 2020Article
- uS3/Rps3 controls fidelity of translation termination and programmed stop codon readthrough in co-operation with eIF3.Nucleic acids research · 2019Article
- Fission Yeast Asc1 Stabilizes the Interaction between Eukaryotic Initiation Factor 3a and Rps0A/uS2 for Protein Synthesis.Molecular and cellular biology · 2019Article
- Binding of eIF3 in complex with eIF5 and eIF1 to the 40S ribosomal subunit is accompanied by dramatic structural changes.Nucleic acids research · 2019Article
- Control of Translation at the Initiation Phase During Glucose Starvation in Yeast.International journal of molecular sciences · 2019Review
- Protein Synthesis Initiation in Eukaryotic Cells.Cold Spring Harbor perspectives in biology · 2018Review
- eIF2A, an initiator tRNA carrier refractory to eIF2α kinases, functions synergistically with eIF5B.Cellular and molecular life sciences : CMLS · 2018Article
- Identification of a 57S translation complex containing closed-loop factors and the 60S ribosome subunit.Scientific reports · 2018Article
- Embraced by eIF3: structural and functional insights into the roles of eIF3 across the translation cycle.Nucleic acids research · 2017Article
- Deletion of eIF2β lysine stretches creates a dominant negative that affects the translation and proliferation in human cell line: A tool for arresting the cell growth.Cancer biology & therapy · 2017Article
10 more citing papers are in PubMed but not listed here.
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Translation initiation factor 3 (eIF3) of Saccharo myces cerevisiae forms a multifactor complex (MFC) with eIFs 1, 2, 5 and Met-tRNA(i)(Met). We previously constructed a subunit interaction model for the MFC. Here we incorporated affinity tags into the three largest eIF3 subunits (eIF3a/TIF32, eIF3b/PRT1 and eIF3c/NIP1) and deleted predicted binding domains in each tagged protein. By characterizing the mutant subcomplexes, we confirmed all key predictions of our model and uncovered new interactions of NIP1 with PRT1 and of TIF32 with eIF1. In addition to the contact between eIF2 and the N-terminal domain (NTD) of NIP1 bridged by eIF5, the C-terminal domain (CTD) of TIF32 binds eIF2 directly and is required for eIF2-eIF3 association in vivo. Overexpressing a CTD-less form of TIF32 exacerbated the initiation defect of an eIF5 mutation that weakens the NIP1-eIF5-eIF2 connection. Thus, the two independent eIF2-eIF3 contacts have additive effects on translation in vivo. Overexpressing the NIP1-NTD sequestered eIF1-eIF5-eIF2 in a defective subcomplex that derepressed GCN4 translation, providing the first in vivo evidence that association with eIF3 promotes binding of eIF2 and Met-tRNA(i)(Met) to 40S ribosomes.
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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.