Evidence map›Paper›PMID 24852487›Full record

ArticleNature communications2014

eIF2B is a decameric guanine nucleotide exchange factor with a γ2ε2 tetrameric core.

Yuliya Gordiyenko, Carla Schmidt, Martin D Jennings, Dijana Matak-Vinkovic, Graham D Pavitt, Carol V Robinson

Open access · hybridAbstract read
In one paragraph

Article in Nature communications, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
3.8field-weighted citation impact, top 6% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

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.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

44 citing papers in PubMed, 75 citations in OpenAlex.

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  16. GCN2-Like Kinase Modulates Stress Granule Formation During Nutritional Stress inFrontiers in cellular and infection microbiology · 2020
    Article
  17. Analysis of Long Non-Coding RNA inFrontiers in cellular and infection microbiology · 2020
    Article
  18. Article
  19. Review
  20. Phosphorylation and Signal Transduction Pathways in Translational Control.Cold Spring Harbor perspectives in biology · 2019
    Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 3 institutions in 1 country.

Yuliya Gordiyenko1] Department of Chemistry, Physical and Theoretical Chemistry Laboratory, University of Oxford, South Parks Road, Oxford OX1 3QZ, UK [2] MRC Laboratory of Molecular Biology, University of Cambridge, Francis Crick Avenue, Cambridge CB2 0QH, UK [3].
Carla Schmidt1] Department of Chemistry, Physical and Theoretical Chemistry Laboratory, University of Oxford, South Parks Road, Oxford OX1 3QZ, UK [2].
Martin D JenningsFaculty of Life Sciences, Michael Smith Building, University of Manchester, Oxford Road, Manchester M13 9PT, UK.
Dijana Matak-VinkovicDepartment of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK.
Graham D PavittFaculty of Life Sciences, Michael Smith Building, University of Manchester, Oxford Road, Manchester M13 9PT, UK.
Carol V RobinsonDepartment of Chemistry, Physical and Theoretical Chemistry Laboratory, University of Oxford, South Parks Road, Oxford OX1 3QZ, UK.
University of Oxford · GBUniversity of Manchester · GBUniversity of Cambridge · GB

Funding

Biotechnology and Biological Sciences Research Council BB/F013272/1Biotechnology and Biological Sciences Research Council BB/H010599/1Medical Research Council MC_U105184332Wellcome Trust 088150Wellcome Trust 088150/B/09/Z
6 · The paper itself

Abstract

eIF2B facilitates and controls protein synthesis in eukaryotes by mediating guanine nucleotide exchange on its partner eIF2. We combined mass spectrometry (MS) with chemical cross-linking, surface accessibility measurements and homology modelling to define subunit stoichiometry and interactions within eIF2B and eIF2. Although it is generally accepted that eIF2B is a pentamer of five non-identical subunits (α-ε), here we show that eIF2B is a decamer. MS and cross-linking of eIF2B complexes allows us to propose a model for the subunit arrangements within eIF2B where the subunit assembly occurs through catalytic γ- and ε-subunits, with regulatory subunits arranged in asymmetric trimers associated with the core. Cross-links between eIF2 and eIF2B allow modelling of interactions that contribute to nucleotide exchange and its control by eIF2 phosphorylation. Finally, we identify that GTP binds to eIF2Bγ, prompting us to propose a multi-step mechanism for nucleotide exchange.

Indexed as

Protein MultimerizationCross-Linking ReagentsElectrophoresis, Polyacrylamide GelEukaryotic Initiation Factor-2Eukaryotic Initiation Factor-2BGuanosine TriphosphateHydrophobic and Hydrophilic InteractionsMass SpectrometryModels, MolecularProtein BindingProtein Structure, TertiaryProtein SubunitsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSolventsStructural Homology, ProteinCross-Linking ReagentsEukaryotic Initiation Factor-2Eukaryotic Initiation Factor-2BGuanosine TriphosphateProtein SubunitsSaccharomyces cerevisiae ProteinsSolvents

Identifiers

PMID24852487
PMCPMC4046112
OpenAlexW2149112086

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

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.