ArticleCell discovery2015
eIF2 interactions with initiator tRNA and eIF2B are regulated by post-translational modifications and conformational dynamics.
Article in Cell discovery, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
What it found
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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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
20 citing papers in PubMed, 34 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
- In-silico characterization and expression study of eIF genes associated with abiotic stresses in potato (Solanum tuberosum L.).Scientific reports · 2025Article
- Protein aggregation and biomolecular condensation in hypoxic environments (Review).International journal of molecular medicine · 2024Review
- Recruitment of trimeric eIF2 by phosphatase non-catalytic subunit PPP1R15B.Molecular cell · 2024Article
- Signaling plasticity in the integrated stress response.Frontiers in cell and developmental biology · 2023Review
- Review
- Dual contribution of the mTOR pathway and of the metabolism of amino acids in prostate cancer.Cellular oncology (Dordrecht, Netherlands) · 2022Review
- Signaling by the integrated stress response kinase PKR is fine-tuned by dynamic clustering.The Journal of cell biology · 2022Article
- Regulation and function of elF2B in neurological and metabolic disorders.Bioscience reports · 2022Review
- In-Cell Labeling and Mass Spectrometry for Systems-Level Structural Biology.Chemical reviews · 2022Review
- Phosphorylation of a reinitiation supporting protein, RISP, determines its function in translation reinitiation.Nucleic acids research · 2021Article
- Crosslinking mass spectrometry: A link between structural biology and systems biology.Protein science : a publication of the Protein Society · 2021Review
- eIF2B-catalyzed nucleotide exchange and phosphoregulation by the integrated stress response.Science (New York, N.Y.) · 2019Article
- Data-independent Acquisition Improves Quantitative Cross-linking Mass Spectrometry.Molecular & cellular proteomics : MCP · 2019Article
- Quantitative cross-linking/mass spectrometry to elucidate structural changes in proteins and their complexes.Nature protocols · 2019Article
- Protein Dynamics in Solution by Quantitative Crosslinking/Mass Spectrometry.Trends in biochemical sciences · 2018Review
- Adaptation of Plasmodium falciparum to its transmission environment.Nature ecology & evolution · 2018Article
- Novel mechanisms of eIF2B action and regulation by eIF2α phosphorylation.Nucleic acids research · 2017Article
- Acetylation and phosphorylation control both local and global stability of the chloroplast FScientific reports · 2017Article
- Dimer interface of bovine cytochrome c oxidase is influenced by local posttranslational modifications and lipid binding.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Translation of messenger RNA (mRNA) into proteins is key to eukaryotic gene expression and begins when initiation factor-2 (eIF2) delivers methionyl initiator tRNA (Met-tRNAi (Met)) to ribosomes. This first step is controlled by eIF2B mediating guanine nucleotide exchange on eIF2. We isolated eIF2 from yeast and used mass spectrometry to study the intact complex, and found that eIF2β is the most labile of the three subunits (eIF2α/β/γ). We then compared conformational dynamics of the ternary complex eIF2:GTP:Met-tRNAi (Met) with apo eIF2 using comparative chemical cross-linking. Results revealed high conformational dynamics for eIF2α in apo eIF2 while in the ternary complex all three subunits are constrained. Novel post-translational modifications identified here in both eIF2 and eIF2B were combined with established sites, and located within protein sequences and homology models. We found clustering at subunit interfaces and highly phosphorylated unstructured regions, at the N-terminus of eIF2β, and also between the eIF2Bε core and catalytic domains. We propose that modifications of these unstructured regions have a key role in regulating interactions between eIF2 and eIF2B, as well as other eIFs.
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What OpenQuestion holds
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.