Evidence map›Paper›PMID 33305433›Full record

ArticleThe EMBO journal2021

Architecture of the active post-translational Sec translocon.

Tsai-Hsuan Weng, Wieland Steinchen, Birgitta Beatrix, Otto Berninghausen, Thomas Becker, Gert Bange, Jingdong Cheng, Roland Beckmann

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
4.7field-weighted citation impact, top 5% 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

29 citing papers in PubMed, 43 citations in OpenAlex.

  1. Article
  2. Review
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  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Mechanism of Protein Translocation by the Sec61 Translocon Complex.Cold Spring Harbor perspectives in biology · 2023
    Review
  15. Article
  16. Article
  17. Article
  18. Targeting of Proteins for Translocation at the Endoplasmic Reticulum.International journal of molecular sciences · 2022
    Review
  19. The mechanisms of integral membrane protein biogenesis.Nature reviews. Molecular cell biology · 2022
    Review
  20. 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

8 authors at 1 institution in 1 country.

Tsai-Hsuan WengGene Center Munich, Department of Biochemistry, University of Munich, Munich, Germany.ORCID 0000-0002-3708-6384
Wieland SteinchenDepartment of Chemistry, SYNMIKRO Research Center, Philipps-University Marburg, Marburg, Germany.
Birgitta BeatrixGene Center Munich, Department of Biochemistry, University of Munich, Munich, Germany.
Otto BerninghausenGene Center Munich, Department of Biochemistry, University of Munich, Munich, Germany.
Thomas BeckerGene Center Munich, Department of Biochemistry, University of Munich, Munich, Germany.ORCID 0000-0001-8458-2738
Gert BangeDepartment of Chemistry, SYNMIKRO Research Center, Philipps-University Marburg, Marburg, Germany.ORCID 0000-0002-7826-0932
Jingdong ChengGene Center Munich, Department of Biochemistry, University of Munich, Munich, Germany.ORCID 0000-0003-4442-377X
Roland BeckmannGene Center Munich, Department of Biochemistry, University of Munich, Munich, Germany.ORCID 0000-0003-4291-3898
Philipps University of Marburg · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In eukaryotes, most secretory and membrane proteins are targeted by an N-terminal signal sequence to the endoplasmic reticulum, where the trimeric Sec61 complex serves as protein-conducting channel (PCC). In the post-translational mode, fully synthesized proteins are recognized by a specialized channel additionally containing the Sec62, Sec63, Sec71, and Sec72 subunits. Recent structures of this Sec complex in the idle state revealed the overall architecture in a pre-opened state. Here, we present a cryo-EM structure of the yeast Sec complex bound to a substrate, and a crystal structure of the Sec62 cytosolic domain. The signal sequence is inserted into the lateral gate of Sec61α similar to previous structures, yet, with the gate adopting an even more open conformation. The signal sequence is flanked by two Sec62 transmembrane helices, the cytoplasmic N-terminal domain of Sec62 is more rigidly positioned, and the plug domain is relocated. We crystallized the Sec62 domain and mapped its interaction with the C-terminus of Sec63. Together, we obtained a near-complete and integrated model of the active Sec complex.

Indexed as

Binding SitesCryoelectron MicroscopyCrystallography, X-RayEndoplasmic ReticulumHeat-Shock ProteinsMembrane Transport ProteinsModels, MolecularProtein BindingProtein ConformationProtein DomainsProtein Processing, Post-TranslationalSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsHeat-Shock ProteinsMembrane Transport ProteinsSaccharomyces cerevisiae ProteinsSEC62 protein, S cerevisiaeSEC63 protein, S cerevisiaepost-translational translocationprotein translocationsec complexsignal sequence

Identifiers

PMID33305433
PMCPMC7849165
OpenAlexW3111474448

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.