Evidence map›Paper›PMID 39289545›Full record

ArticleNature structural & molecular biology2025

Structural basis for translational control by the human 48S initiation complex.

Valentyn Petrychenko, Sung-Hui Yi, David Liedtke, Bee-Zen Peng, Marina V Rodnina, Niels Fischer

Erratum issuedAbstract read
In one paragraph

Article in Nature structural & molecular biology, 2025. 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 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
–field-weighted citation impact
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

26 citing papers in PubMed.

  1. Article
  2. Review
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  5. Article
  6. Review
  7. Article
  8. Article
  9. Review
  10. Article
  11. Review
  12. Structural basis for non-AUG translation regulation by 5MPs.bioRxiv : the preprint server for biology · 2025
    Article
  13. Review
  14. Structural insights into the role of eIF3 in translation mediated by the HCV IRES.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  15. Article
  16. Article
  17. eIF1 and eIF5 dynamically control translation start site fidelity.Nature structural & molecular biology · 2025
    Article
  18. Article
  19. Article
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors.

Valentyn PetrychenkoProject Group Molecular Machines in Motion, Department of Physical Biochemistry, Max Planck Institute for Multidisciplinary Sciences, Göttingen, Germany.
Sung-Hui YiDepartment of Physical Biochemistry, Max Planck Institute for Multidisciplinary Sciences, Göttingen, Germany.
David LiedtkeProject Group Molecular Machines in Motion, Department of Physical Biochemistry, Max Planck Institute for Multidisciplinary Sciences, Göttingen, Germany.
Bee-Zen PengDepartment of Physical Biochemistry, Max Planck Institute for Multidisciplinary Sciences, Göttingen, Germany.
Marina V RodninaDepartment of Physical Biochemistry, Max Planck Institute for Multidisciplinary Sciences, Göttingen, Germany.
Niels FischerProject Group Molecular Machines in Motion, Department of Physical Biochemistry, Max Planck Institute for Multidisciplinary Sciences, Göttingen, Germany. niels.fischer@mpinat.mpg.de.ORCID http://orcid.org/0000-0002-4609-4052

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The selection of an open reading frame (ORF) for translation of eukaryotic mRNA relies on remodeling of the scanning 48S initiation complex into an elongation-ready 80S ribosome. Using cryo-electron microscopy, we visualize the key commitment steps orchestrating 48S remodeling in humans. The mRNA Kozak sequence facilitates mRNA scanning in the 48S open state and stabilizes the 48S closed state by organizing the contacts of eukaryotic initiation factors (eIFs) and ribosomal proteins and by reconfiguring mRNA structure. GTPase-triggered large-scale fluctuations of 48S-bound eIF2 facilitate eIF5B recruitment, transfer of initiator tRNA from eIF2 to eIF5B and the release of eIF5 and eIF2. The 48S-bound multisubunit eIF3 complex controls ribosomal subunit joining by coupling eIF exchange to gradual displacement of the eIF3c N-terminal domain from the intersubunit interface. These findings reveal the structural mechanism of ORF selection in human cells and explain how eIF3 could function in the context of the 80S ribosome.

Indexed as

Eukaryotic Initiation FactorsProtein BiosynthesisCryoelectron MicroscopyEukaryotic Initiation Factor-3HumansModels, MolecularOpen Reading FramesPeptide Chain Initiation, TranslationalRibosomal ProteinsRibosomesRNA, MessengerEukaryotic Initiation Factor-3Eukaryotic Initiation FactorsRibosomal ProteinsRNA, Messenger

Identifiers

PMID39289545
PMCPMC11746136

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Registered trials

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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.