ArticleNucleic acids research2016
eIF2β is critical for eIF5-mediated GDP-dissociation inhibitor activity and translational control.
Article in Nucleic acids research, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 23 citations in OpenAlex.
- Molecular basis for the interactions of eIF2β with eIF5, eIF2B, and 5MP1 and their regulation by CK2.RNA (New York, N.Y.) · 2025Article
- Review
- Cyst stem cell lineage eIF5 non-autonomously prevents testicular germ cell tumor formation via eIF1A/eIF2γ-mediated pre-initiation complex.Stem cell research & therapy · 2022Article
- The metaphorical swiss army knife: The multitude and diverse roles of HEAT domains in eukaryotic translation initiation.Nucleic acids research · 2022Review
- Dynamic interaction network involving the conserved intrinsically disordered regions in human eIF5.Biophysical chemistry · 2022Article
- Quantifying the Binding of Fluorescently Labeled Guanine Nucleotides and Initiator tRNA to Eukaryotic Translation Initiation Factor 2.Methods in molecular biology (Clifton, N.J.) · 2022Article
- GTP binding to translation factor eIF2B stimulates its guanine nucleotide exchange activity.iScience · 2021Article
- Established and Emerging Regulatory Roles of Eukaryotic Translation Initiation Factor 5B (eIF5B).Frontiers in genetics · 2021Review
- eIF2B and the Integrated Stress Response: A Structural and Mechanistic View.Biochemistry · 2020Article
- uORF-mediated translational control: recently elucidated mechanisms and implications in cancer.RNA biology · 2019Review
- Structural basis for the inhibition of translation through eIF2α phosphorylation.Nature communications · 2019Article
- Protein Synthesis Initiation in Eukaryotic Cells.Cold Spring Harbor perspectives in biology · 2018Review
- Molecular Determinants of the Regulation of Development and Metabolism by Neuronal eIF2α Phosphorylation inGenetics · 2017Article
- Fail-safe control of translation initiation by dissociation of eIF2α phosphorylated ternary complexes.eLife · 2017Article
Corrections and comments
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Authors and funding
9 authors at 2 institutions in 1 country.
Funding
Abstract
In protein synthesis translation factor eIF2 binds initiator tRNA to ribosomes and facilitates start codon selection. eIF2 GDP/GTP status is regulated by eIF5 (GAP and GDI functions) and eIF2B (GEF and GDF activities), while eIF2α phosphorylation in response to diverse signals is a major point of translational control. Here we characterize a growth suppressor mutation in eIF2β that prevents eIF5 GDI and alters cellular responses to reduced eIF2B activity, including control of GCN4 translation. By monitoring the binding of fluorescent nucleotides and initiator tRNA to purified eIF2 we show that the eIF2β mutation does not affect intrinsic eIF2 affinities for these ligands, neither does it interfere with eIF2 binding to 43S pre-initiation complex components. Instead we show that the eIF2β mutation prevents eIF5 GDI stabilizing nucleotide binding to eIF2, thereby altering the off-rate of GDP from eIF2•GDP/eIF5 complexes. This enables cells to grow with reduced eIF2B GEF activity but impairs activation of GCN4 targets in response to amino acid starvation. These findings provide support for the importance of eIF5 GDI activity in vivo and demonstrate that eIF2β acts in concert with eIF5 to prevent premature release of GDP from eIF2γ and thereby ensure tight control of protein synthesis initiation.
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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.