Evidence map›Paper›PMID 38896445›Full record

ArticleeLife2024

Structural analysis of the dynamic ribosome-translocon complex.

Aaron J O Lewis, Frank Zhong, Robert J Keenan, Ramanujan S Hegde

Abstract read
In one paragraph

Article in eLife, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing 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

19 citing papers in PubMed.

  1. Article
  2. Review
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  5. Article
  6. Article
  7. Review
  8. Review
  9. Article
  10. SARS-CoV-2 membrane protein biogenesis.bioRxiv : the preprint server for biology · 2026
    Article
  11. Article
  12. Article
  13. Article
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  17. Review
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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

4 authors.

Aaron J O LewisMRC Laboratory of Molecular Biology, Cambridge, United Kingdom.ORCID https://orcid.org/0000-0001-8818-1763
Frank ZhongDepartment of Molecular Genetics and Cell Biology, The University of Chicago, Chicago, United States.
Robert J KeenanDepartment of Biochemistry and Molecular Biology, The University of Chicago, Chicago, United States.ORCID https://orcid.org/0000-0003-1466-0889
Ramanujan S HegdeMRC Laboratory of Molecular Biology, Cambridge, United Kingdom.ORCID https://orcid.org/0000-0001-8338-852X

Funding

Molecular And Cellular Biology Training ProgramT32GM007183 · NIGMS · UNIVERSITY OF CHICAGO · PI GLICK, BENJAMIN S, RICE, PHOEBE A · 1985 to 2021
$23.9M
Membrane protein biogenesis at the ERR35GM145374 · NIGMS · UNIVERSITY OF CHICAGO · PI Robert J Keenan · 2022 to 2026
$3.5M
Medical Research Council MC_UP_A022_1007NIGMS NIH HHS R35 GM145374NIGMS NIH HHS T32 GM007183NIH HHS R35 GM145374NIH HHS T32 GM007183
6 · The paper itself

Abstract

The protein translocon at the endoplasmic reticulum comprises the Sec61 translocation channel and numerous accessory factors that collectively facilitate the biogenesis of secretory and membrane proteins. Here, we leveraged recent advances in cryo-electron microscopy (cryo-EM) and structure prediction to derive insights into several novel configurations of the ribosome-translocon complex. We show how a transmembrane domain (TMD) in a looped configuration passes through the Sec61 lateral gate during membrane insertion; how a nascent chain can bind and constrain the conformation of ribosomal protein uL22; and how the translocon-associated protein (TRAP) complex can adjust its position during different stages of protein biogenesis. Most unexpectedly, we find that a large proportion of translocon complexes contains RAMP4 intercalated into Sec61's lateral gate, widening Sec61's central pore and contributing to its hydrophilic interior. These structures lead to mechanistic hypotheses for translocon function and highlight a remarkably plastic machinery whose conformations and composition adjust dynamically to its diverse range of substrates.

Indexed as

Cryoelectron MicroscopyRibosomesSEC Translocation ChannelsEndoplasmic ReticulumHumansMembrane ProteinsModels, MolecularProtein ConformationProtein TransportRibosomal ProteinsMembrane ProteinsRibosomal ProteinsSEC Translocation Channelscell biologyendoplasmic reticulummammalmembrane protein insertionmembrane transportmolecular biophysicssecretionstructural biologytranslocon

Identifiers

PMID38896445
PMCPMC11186639

What OpenQuestion holds

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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.