ArticleCell reports2017
Molecular Landscape of the Ribosome Pre-initiation Complex during mRNA Scanning: Structural Role for eIF3c and Its Control by eIF5.
Erratum issuedOpen access · goldAbstract read
In one paragraph
Article in Cell reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 46 papers.
0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed
3.2field-weighted citation impact, top 7% of its field
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.
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.
Who cites it
46 citing papers in PubMed, 66 citations in OpenAlex.
- The eIF5-mimic protein 5MP1: a regulator of translation stringency and a multifaceted oncogene.Journal of biochemistry · 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
- Eukaryotic initiation factor eIF3 facilitates loading of eukaryotic release factor eRF1 or suppressor tRNA to the ribosome.Nucleic acids research · 2026Article
- eIF3: a critical player in mRNA recruitment to the ribosome with emerging roles across translation.Biochemical Society transactions · 2025Review
- Molecular basis for the interactions of eIF2β with eIF5, eIF2B, and 5MP1 and their regulation by CK2.RNA (New York, N.Y.) · 2025Article
- Inhibitors of eIF1A-ribosome interaction unveil uORF-dependent regulation of translation initiation and antitumor and antiviral effects.The EMBO journal · 2025Article
- Exploring the interaction dynamics of eukaryotic translation initiation factor 2.Biochemical Society transactions · 2025Review
- Raman spectroscopy and bioinformatics-based identification of key genes and pathways capable of distinguishing between diffuse large B cell lymphoma and chronic lymphocytic leukemia.Frontiers in immunology · 2025Article
- The molecular basis of translation initiation and its regulation in eukaryotes.Nature reviews. Molecular cell biology · 2024Review
- Translation Fidelity and Respiration Deficits in CLPP-Deficient Tissues: Mechanistic Insights from Mitochondrial Complexome Profiling.International journal of molecular sciences · 2023Article
- Translational fidelity screens in mammalian cells reveal eIF3 and eIF4G2 as regulators of start codon selectivity.Nucleic acids research · 2023Article
- Between Order and Chaos: Understanding the Mechanism and Pathology of RAN Translation.Biological & pharmaceutical bulletin · 2023Review
- Label-free protocol to quantify protein affinity using isothermal titration calorimetry and bio-layer interferometry of a human eIF5-mimic protein.STAR protocols · 2022Article
- eIF3 Interacts with Selenoprotein mRNAs.Biomolecules · 2022Article
- Inhibitors of eIF4G1-eIF1 uncover its regulatory role of ER/UPR stress-response genes independent of eIF2α-phosphorylation.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Conformational rearrangements upon start codon recognition in human 48S translation initiation complex.Nucleic acids research · 2022Article
- Non-AUG translation initiation in mammals.Genome biology · 2022Review
- Translational recoding by chemical modification of non-AUG start codon ribonucleotide bases.Science advances · 2022Article
- Dynamic interaction network involving the conserved intrinsically disordered regions in human eIF5.Biophysical chemistry · 2022Article
- Role of eIF3C Overexpression in Predicting Prognosis of Intrahepatic Cholangiocarcinoma.Digestive diseases and sciences · 2022Article
Corrections and comments
- Erratum issued
Authors and funding
28 authors at 11 institutions in 3 countries.
Eiji ObayashiShimane University School of Medicine, Izumo, Shimane 690-8504, Japan.
Rafael E LunaDepartment of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115, USA.
Takashi NagataInstitute of Advanced Energy, Kyoto University, Uji, Kyoto 611-0011, Japan.
Pilar Martin-MarcosLaboratory of Gene Regulation and Development, Eunice Kennedy Shriver National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892, USA.
Hiroyuki HiraishiMolecular Cellular Developmental Biology Program, Division of Biology, Kansas State University, Manhattan, KS 66506, USA.
Chingakham Ranjit SinghMolecular Cellular Developmental Biology Program, Division of Biology, Kansas State University, Manhattan, KS 66506, USA.
Jan Peter ErzbergerDepartment of Biology, Institute of Molecular Biology and Biophysics, ETH Zurich, 8093 Zurich, Switzerland.
Fan ZhangLaboratory of Gene Regulation and Development, Eunice Kennedy Shriver National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892, USA.
Haribabu ArthanariDepartment of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115, USA.
Jacob MorrisMolecular Cellular Developmental Biology Program, Division of Biology, Kansas State University, Manhattan, KS 66506, USA.
Riccardo PellarinCalifornia Institute for Quantitative Biosciences, University of California, San Francisco, San Francisco, CA 94158, USA.
Chelsea MooreMolecular Cellular Developmental Biology Program, Division of Biology, Kansas State University, Manhattan, KS 66506, USA.
Ian HarmonMolecular Cellular Developmental Biology Program, Division of Biology, Kansas State University, Manhattan, KS 66506, USA.
Evangelos PapadopoulosDepartment of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115, USA.
Hisashi YoshidaGraduate School of Medical Life Science, Yokohama City University, Tsurumi-ku, Yokohama 230-0045, Japan; Drug Design Group, Kanagawa Academy of Science and Technology, Takatsu-ku, Kawasaki 213-0012, Japan.
Mahmoud L NasrDepartment of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115, USA.
Satoru UnzaiGraduate School of Medical Life Science, Yokohama City University, Tsurumi-ku, Yokohama 230-0045, Japan.
Brytteny ThompsonMolecular Cellular Developmental Biology Program, Division of Biology, Kansas State University, Manhattan, KS 66506, USA.
Eric AubeMolecular Cellular Developmental Biology Program, Division of Biology, Kansas State University, Manhattan, KS 66506, USA.
Samantha HustakMolecular Cellular Developmental Biology Program, Division of Biology, Kansas State University, Manhattan, KS 66506, USA.
Florian StengelDepartment of Biology, Institute of Molecular Systems Biology, ETH Zurich, 8093 Zurich, Switzerland.
Eddie DagracaDepartment of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115, USA.
Asokan AnanbandamCOBRE-PSF, University of Kansas, Lawrence, KS 66047, USA.
Philip GaoCOBRE-PSF, University of Kansas, Lawrence, KS 66047, USA.
Takeshi UranoShimane University School of Medicine, Izumo, Shimane 690-8504, Japan.
Alan G HinnebuschLaboratory of Gene Regulation and Development, Eunice Kennedy Shriver National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892, USA.
Gerhard WagnerDepartment of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115, USA.
Katsura AsanoMolecular Cellular Developmental Biology Program, Division of Biology, Kansas State University, Manhattan, KS 66506, USA. Electronic address: kasano@ksu.edu.
Kansas State University · USHarvard University · USETH Zurich · CHNational Institutes of Health · USShimane University · JPUniversity of Kansas · USEunice Kennedy Shriver National Institute of Child Health and Human Development · USKanagawa Academy of Science and Technology · JPKyoto University · JPQB3 · USYokohama City University · JP
Funding
Translational & Transcriptional Control Of Gene Expression By Nutrients In YeastZIAHD001004 · NICHD · EUNICE KENNEDY SHRIVER NATIONAL INSTITUTE OF CHILD HEALTH & HUMAN DEVELOPMENT · PI HINNEBUSCH, ALAN G · 2009 to 2025
$34.4MT CELL SPECIFIC TRANSCRIPTION COMPLEXESP01GM047467 · NIGMS · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI WAGNER, GERHARD · 1992 to 2017
$28.6MProtein Structure Laboratory P30GM110761 · NIGMS · UNIVERSITY OF KANSAS LAWRENCE · PI HANZLIK, ROBERT P · 2014 to 2018
$5.6MSTRUCTURAL BASIS OF TRANSLATION INITIATION BY EIF-4ER01CA068262 · NCI · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI WAGNER, GERHARD · 1996 to 2015
$3.6MStudies on start codon selection by eukaryotic ribosomesR01GM064781 · NIGMS · KANSAS STATE UNIVERSITY · PI ASANO, KATSURA · 2002 to 2010
$2.4MRoles of Eukaryotic Translation Initiation Factors in Gene ExpressionR01CA200913 · NCI · HARVARD MEDICAL SCHOOL · PI WAGNER, GERHARD · 2016 to 2020
$2.3MNCI NIH HHS R01 CA068262NCI NIH HHS R01 CA200913NIGMS NIH HHS P01 GM047467NIGMS NIH HHS P30 GM110761NIGMS NIH HHS R01 GM064781
Abstract
During eukaryotic translation initiation, eIF3 binds the solvent-accessible side of the 40S ribosome and recruits the gate-keeper protein eIF1 and eIF5 to the decoding center. This is largely mediated by the N-terminal domain (NTD) of eIF3c, which can be divided into three parts: 3c0, 3c1, and 3c2. The N-terminal part, 3c0, binds eIF5 strongly but only weakly to the ribosome-binding surface of eIF1, whereas 3c1 and 3c2 form a stoichiometric complex with eIF1. 3c1 contacts eIF1 through Arg-53 and Leu-96, while 3c2 faces 40S protein uS15/S13, to anchor eIF1 to the scanning pre-initiation complex (PIC). We propose that the 3c0:eIF1 interaction diminishes eIF1 binding to the 40S, whereas 3c0:eIF5 interaction stabilizes the scanning PIC by precluding this inhibitory interaction. Upon start codon recognition, interactions involving eIF5, and ultimately 3c0:eIF1 association, facilitate eIF1 release. Our results reveal intricate molecular interactions within the PIC, programmed for rapid scanning-arrest at the start codon.
Indexed as
Peptide Chain Initiation, TranslationalAmino Acid SequenceBinding SitesEukaryotic Initiation Factor-1Eukaryotic Initiation Factor-3Eukaryotic Initiation Factor-5Magnetic Resonance SpectroscopyModels, MolecularMutationProtein BindingProtein SubunitsRibosomesRNA, MessengerSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsEukaryotic Initiation Factor-1Eukaryotic Initiation Factor-3Eukaryotic Initiation Factor-5Protein SubunitsRNA, MessengerSaccharomyces cerevisiae ProteinseIF1eIF3eIF5ribosomal pre-initiation complexribosomestart codon selectiontranslation initiation
Identifiers
What OpenQuestion holds
Textmetadata
LicenceTDM
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.