Evidence map›Paper›PMID 24753257›Full record

ArticleThe Journal of biological chemistry2014

Structural and functional profiling of the lateral gate of the Sec61 translocon.

Johannes H Reithinger, Chewon Yim, Sungmin Kim, Hunsang Lee, Hyun Kim

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
0.6field-weighted citation impact, top 34% 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

13 citing papers in PubMed, 17 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. A unifying model for membrane protein biogenesis.Nature structural & molecular biology · 2024
    Review
  6. Mechanism of Protein Translocation by the Sec61 Translocon Complex.Cold Spring Harbor perspectives in biology · 2023
    Review
  7. Review
  8. Review
  9. Article
  10. Article
  11. Article
  12. Marginally hydrophobic transmembrane α-helices shaping membrane protein folding.Protein science : a publication of the Protein Society · 2015
    Review
  13. 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

5 authors at 1 institution in 1 country.

Johannes H ReithingerCenter for Biomembrane Research, Department of Biochemistry and Biophysics, Stockholm University, SE-106 91 Stockholm, Sweden.
Chewon YimFrom the School of Biological Sciences, Seoul National University, Seoul 151-747, South Korea and.
Sungmin KimFrom the School of Biological Sciences, Seoul National University, Seoul 151-747, South Korea and.
Hunsang LeeFrom the School of Biological Sciences, Seoul National University, Seoul 151-747, South Korea and.
Hyun KimFrom the School of Biological Sciences, Seoul National University, Seoul 151-747, South Korea and joy@snu.ac.kr.
Stockholm University · SE

Funding

Environmental Health Perspectives, NIEHS27302C0031 · NIEHS · 2008 to 2008
$1.2M
2016 SETAC Asia/Pacific ConferenceR13ES027302 · NIEHS · SOCIETY/ENVIRONMENTAL TOXICOLOGY/CHEM · PI MENZIE, CHARLES · 2016 to 2016
$6k
NIEHS NIH HHS 27302C0031
6 · The paper itself

Abstract

The evolutionarily conserved Sec61 translocon mediates the translocation and membrane insertion of proteins. For the integration of proteins into the membrane, the Sec61 translocon opens laterally to the lipid bilayer. Previous studies suggest that the lateral opening of the channel is mediated by the helices TM2b and TM7 of a pore-forming subunit of the Sec61 translocon. To map key residues in TM2b and TM7 in yeast Sec61 that modulate lateral gating activity, we performed alanine scanning and in vivo site-directed photocross-linking experiments. Alanine scanning identified two groups of critical residues in the lateral gate, one group that leads to defects in the translocation and membrane insertion of proteins and the other group that causes faster translocation and facilitates membrane insertion. Photocross-linking data show that the former group of residues is located at the interface of the lateral gate. Furthermore, different degrees of defects for the membrane insertion of single- and double-spanning membrane proteins were observed depending on whether the mutations were located in TM2b or TM7. These results demonstrate subtle differences in the molecular mechanism of the signal sequence binding/opening of the lateral gate and membrane insertion of a succeeding transmembrane segment in a polytopic membrane protein.

Indexed as

Cell MembraneEndoplasmic ReticulumLipid BilayersMembrane Transport ProteinsProtein Structure, SecondaryProtein TransportSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSEC Translocation ChannelsStructure-Activity RelationshipLipid BilayersMembrane Transport ProteinsSaccharomyces cerevisiae ProteinsSEC61 protein, S cerevisiaeSEC Translocation ChannelsEndoplasmic Reticulum (ER)MembraneMembrane ProteinProtein TranslocationYeast

Identifiers

PMID24753257
PMCPMC4140938
OpenAlexW1966843959

What OpenQuestion holds

Textmetadata
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.