Evidence map›Paper›PMID 15067017›Full record

ArticleThe Journal of cell biology2004

Role of YidC in folding of polytopic membrane proteins.

Shushi Nagamori, Irina N Smirnova, H Ronald Kaback

Abstract read
In one paragraph

Article in The Journal of cell biology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 85 papers.

0numbers the graph read from it
0cells of the map it votes in
85citing 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

85 citing papers in PubMed.

  1. Review
  2. Review
  3. The versatile role of YidC in membrane protein biosynthesis and quality control.Biochimica et biophysica acta. Molecular cell research · 2025
    Review
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Review
  10. Article
  11. Review
  12. Article
  13. Untangling the complexity of membrane protein folding.Current opinion in structural biology · 2022
    Review
  14. The mechanisms of integral membrane protein biogenesis.Nature reviews. Molecular cell biology · 2022
    Review
  15. Lipid bilayer induces contraction of the denatured state ensemble of a helical-bundle membrane protein.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  16. Article
  17. Review
  18. Review
  19. Cotranslational Biogenesis of Membrane Proteins in Bacteria.Frontiers in molecular biosciences · 2022
    Review
  20. Article

25 more citing papers are in PubMed but not listed here.

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

3 authors.

Shushi Nagamori5-748 Macdonald Research Laboratories, Rm. 6720, P.O. Box 951662, Howard Hughes Medical Institute, University of California, Los Angeles, Los Angeles, CA 90095-1662, USA.
Irina N Smirnova
H Ronald Kaback

Funding

NEW APPROACHES TO MEMBRANE PROTEIN STRUCTURESR01DK051131 · NIDDK · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI KABACK, HOWARD RONALD · 1996 to 2014
$5.2M
Dynamics of the Lactose Permease of Escherichia ColiR56DK051131 · NIDDK · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI KABACK, HOWARD RONALD · 2015 to 2015
$154k
NIDDK NIH HHS DK51131NIDDK NIH HHS R01 DK051131NIDDK NIH HHS R56 DK051131
6 · The paper itself

Abstract

YidC of Echerichia coli, a member of the conserved Alb3/Oxa1/YidC family, is postulated to be important for biogenesis of membrane proteins. Here, we use as a model the lactose permease (LacY), a membrane transport protein with a known three-dimensional structure, to determine whether YidC plays a role in polytopic membrane protein insertion and/or folding. Experiments in vivo and with an in vitro transcription/translation/insertion system demonstrate that YidC is not necessary for insertion per se, but plays an important role in folding of LacY. By using the in vitro system and two monoclonal antibodies directed against conformational epitopes, LacY is shown to bind the antibodies poorly in YidC-depleted membranes. Moreover, LacY also folds improperly in proteoliposomes prepared without YidC. However, when the proteoliposomes are supplemented with purified YidC, LacY folds correctly. The results indicate that YidC plays a primary role in folding of LacY into its final tertiary conformation via an interaction that likely occurs transiently during insertion into the lipid phase of the membrane.

Indexed as

Protein FoldingAntibodies, MonoclonalCarrier ProteinsEpitopesEscherichia coliEscherichia coli ProteinsIntracellular MembranesMembrane LipidsMembrane ProteinsMembrane Transport ProteinsModels, MolecularMolecular ChaperonesMonosaccharide Transport ProteinsProtein BindingProtein BiosynthesisProtein TransportAntibodies, MonoclonalCarrier ProteinsEpitopesEscherichia coli ProteinsLacY protein, E coliMembrane LipidsMembrane ProteinsMembrane Transport ProteinsMolecular ChaperonesMonosaccharide Transport ProteinsProteolipidsproteoliposomesSymportersYIDC protein, E coli

Identifiers

PMID15067017
PMCPMC2172087

What OpenQuestion holds

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LicenceCC BY-NC-SA
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.