Evidence map›Paper›PMID 23690595›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2013

In vitro reconstitution of lipid-dependent dual topology and postassembly topological switching of a membrane protein.

Heidi Vitrac, Mikhail Bogdanov, William Dowhan

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.

0numbers the graph read from it
0cells of the map it votes in
63citing papers in PubMed
4.5field-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

63 citing papers in PubMed, 98 citations in OpenAlex.

  1. Review
  2. Review
  3. The Evolution of Lipids from Solvents to Substrates.Annual review of biophysics · 2026
    Review
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Review
  13. Review
  14. Review
  15. Review
  16. Cotranslational Biogenesis of Membrane Proteins in Bacteria.Frontiers in molecular biosciences · 2022
    Review
  17. Review
  18. Integrating Membrane Transporter Proteins into Droplet Interface Bilayers.Methods in molecular biology (Clifton, N.J.) · 2021
    Article
  19. Review
  20. How bilayer properties influence membrane protein folding.Protein science : a publication of the Protein Society · 2020
    Review

3 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 at 1 institution in 1 country.

Heidi VitracDepartment of Biochemistry and Molecular Biology and the Center for Membrane Biology, University of Texas Medical School, Houston, TX 77030, USA.
Mikhail Bogdanov
William Dowhan
Texas Medical Center · US

Funding

Structure and Function in Membrane ProteinsR37GM020478 · NIGMS · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI DOWHAN, WILLIAM · 2005 to 2015
$5.4M
NIGMS NIH HHS R37 GM020478NIGMS NIH HHS R37 GM20478
6 · The paper itself

Abstract

Phospholipids could exert their effect on membrane protein topology either directly by interacting with topogenic signals of newly inserted proteins or indirectly by influencing the protein assembly machinery. In vivo lactose permease (LacY) of Escherichia coli displays a mixture of topological conformations ranging from complete inversion of the N-terminal helical bundle to mixed topology and then to completely native topology as phosphatidylethanolamine (PE) is increased from 0% to 70% of membrane phospholipids. These topological conformers are interconvertible by postassembly synthesis or dilution of PE in vivo. To investigate whether coexistence of multiple topological conformers is dependent solely on the membrane lipid composition, we determined the topological organization of LacY in an in vitro proteoliposome system in which lipid composition can be systematically controlled before (liposomes) and after (fliposomes) reconstitution using a lipid exchange technique. Purified LacY reconstituted into preformed liposomes of increasing PE content displayed inverted topology at low PE and then a mixture of inverted and proper topologies with the latter increasing with increasing PE until all LacY adopted its native topology. Interconversion between topological conformers of LacY was observed in a PE dose-dependent manner by either increasing or decreasing PE levels in proteoliposomes postreconstitution of LacY, clearly demonstrating that membrane protein topology can be changed simply by changing membrane lipid composition independent of other cellular factors. The results provide a thermodynamic-based lipid-dependent model for shifting the equilibrium between different conformational states of a membrane protein.

Indexed as

Protein ConformationBlotting, WesternChromatography, Thin LayerElectrophoresis, Polyacrylamide GelEscherichia coliEscherichia coli ProteinsImmunoprecipitationLiposomesMicroscopy, ElectronMonosaccharide Transport ProteinsPhospholipidsSymportersEscherichia coli ProteinsLacY protein, E coliLiposomesMonosaccharide Transport ProteinsPhospholipidsSymporters

Identifiers

PMID23690595
PMCPMC3677496
OpenAlexW2080337688

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.