Evidence map›Paper›PMID 37983950›Full record

ArticleEMBO reports2023

Molecular view of ER membrane remodeling by the Sec61/TRAP translocon.

Sudeep Karki, Matti Javanainen, Shahid Rehan, Dale Tranter, Juho Kellosalo, Juha T Huiskonen, Lotta Happonen, Ville Paavilainen

Open access · hybridAbstract read
In one paragraph

Article in EMBO reports, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
3.1field-weighted citation impact, top 8% 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

14 citing papers in PubMed, 16 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Lipid Scrambling Pathways in the Sec61 Translocon Complex.Journal of the American Chemical Society · 2025
    Article
  6. Review
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
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

8 authors at 2 institutions in 3 countries.

Sudeep Karki *Institute of Biotechnology, University of Helsinki, Helsinki, Finland.ORCID 0000-0003-3851-1204
Matti Javanainen *Institute of Biotechnology, University of Helsinki, Helsinki, Finland.ORCID 0000-0003-4858-364X
Shahid Rehan *Institute of Biotechnology, University of Helsinki, Helsinki, Finland.ORCID 0000-0003-1329-8056
Dale Tranter *Institute of Biotechnology, University of Helsinki, Helsinki, Finland.
Juho KellosaloInstitute of Biotechnology, University of Helsinki, Helsinki, Finland.
Juha T Huiskonen *Institute of Biotechnology, University of Helsinki, Helsinki, Finland.ORCID 0000-0002-0348-7323
Lotta HapponenDivision of Infection Medicine, Department of Clinical Sciences, Lund University, Lund, Sweden.ORCID 0000-0002-5922-4549
Ville PaavilainenInstitute of Biotechnology, University of Helsinki, Helsinki, Finland.ORCID 0000-0002-3160-7767
University of Helsinki · FILund University · SE

Funding

Academy of Finland (AKA) 314669Academy of Finland (AKA) 314672Academy of Finland (AKA) 338160Academy of Finland (AKA) 338836Jane and Aatos Erkko FoundationSigrid Juselius Foundation
6 · The paper itself

Abstract

Protein translocation across the endoplasmic reticulum (ER) membrane is an essential step during protein entry into the secretory pathway. The conserved Sec61 protein-conducting channel facilitates polypeptide translocation and coordinates cotranslational polypeptide-processing events. In cells, the majority of Sec61 is stably associated with a heterotetrameric membrane protein complex, the translocon-associated protein complex (TRAP), yet the mechanism by which TRAP assists in polypeptide translocation remains unknown. Here, we present the structure of the core Sec61/TRAP complex bound to a mammalian ribosome by cryogenic electron microscopy (cryo-EM). Ribosome interactions anchor the Sec61/TRAP complex in a conformation that renders the ER membrane locally thinner by significantly curving its lumenal leaflet. We propose that TRAP stabilizes the ribosome exit tunnel to assist nascent polypeptide insertion through Sec61 and provides a ratcheting mechanism into the ER lumen mediated by direct polypeptide interactions.

Indexed as

Endoplasmic ReticulumMembrane ProteinsAnimalsCalcium-Binding ProteinsMammalsMembrane GlycoproteinsPeptidesProtein TransportReceptors, Cytoplasmic and NuclearReceptors, PeptideSEC Translocation ChannelsCalcium-Binding ProteinsMembrane GlycoproteinsMembrane ProteinsPeptidesReceptors, Cytoplasmic and NuclearReceptors, PeptideSEC Translocation Channelssignal sequence receptorcryo-EMmembrane proteinsprotein translocationsecretory proteinsstructural biology

Identifiers

PMID37983950
PMCPMC10702806
OpenAlexW4388869319

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.