Evidence map›Paper›PMID 28077870›Full record

ArticleNature2017

The role of interfacial lipids in stabilizing membrane protein oligomers.

Kallol Gupta, Joseph A C Donlan, Jonathan T S Hopper, Povilas Uzdavinys, Michael Landreh, Weston B Struwe, David Drew, Andrew J Baldwin, Phillip J Stansfeld, Carol V Robinson

Open access · greenAbstract read
In one paragraph

Article in Nature, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 227 papers.

0numbers the graph read from it
0cells of the map it votes in
227citing papers in PubMed
22.6field-weighted citation impact, top 1% 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

227 citing papers in PubMed, 419 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. pH-dependent activation of the NaNature communications · 2026
    Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Review
  20. Article

167 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

10 authors at 2 institutions in 2 countries.

Kallol Gupta *Department of Chemistry, University of Oxford, 12 Mansfield Road, Oxford OX1 3TA.
Joseph A C Donlan *Department of Chemistry, University of Oxford, 12 Mansfield Road, Oxford OX1 3TA.
Jonathan T S Hopper *Department of Chemistry, University of Oxford, 12 Mansfield Road, Oxford OX1 3TA.
Povilas UzdavinysCentre for Biomembrane Research, Department of Biochemistry and Biophysics, Stockholm University, Stockholm SE-106 91, Sweden.
Michael LandrehDepartment of Chemistry, University of Oxford, 12 Mansfield Road, Oxford OX1 3TA.
Weston B StruweDepartment of Chemistry, University of Oxford, 12 Mansfield Road, Oxford OX1 3TA.
David DrewCentre for Biomembrane Research, Department of Biochemistry and Biophysics, Stockholm University, Stockholm SE-106 91, Sweden.
Andrew J BaldwinDepartment of Chemistry, University of Oxford, 12 Mansfield Road, Oxford OX1 3TA.
Phillip J StansfeldDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU.
Carol V RobinsonDepartment of Chemistry, University of Oxford, 12 Mansfield Road, Oxford OX1 3TA.
University of Oxford · GBStockholm University · SE

Funding

European Research Council 641317Medical Research Council MR/N020413/1Wellcome Trust
6 · The paper itself

Abstract

Oligomerization of membrane proteins in response to lipid binding has a critical role in many cell-signalling pathways but is often difficult to define or predict. Here we report the development of a mass spectrometry platform to determine simultaneously the presence of interfacial lipids and oligomeric stability and to uncover how lipids act as key regulators of membrane-protein association. Evaluation of oligomeric strength for a dataset of 125 α-helical oligomeric membrane proteins reveals an absence of interfacial lipids in the mass spectra of 12 membrane proteins with high oligomeric stability. For the bacterial homologue of the eukaryotic biogenic transporters (LeuT, one of the proteins with the lowest oligomeric stability), we found a precise cohort of lipids within the dimer interface. Delipidation, mutation of lipid-binding sites or expression in cardiolipin-deficient Escherichia coli abrogated dimer formation. Molecular dynamics simulation revealed that cardiolipin acts as a bidentate ligand, bridging across subunits. Subsequently, we show that for the Vibrio splendidus sugar transporter SemiSWEET, another protein with low oligomeric stability, cardiolipin shifts the equilibrium from monomer to functional dimer. We hypothesized that lipids are essential for dimerization of the Na

Indexed as

Bacterial ProteinsBinding SitesCardiolipinsCell MembraneEscherichia coliEscherichia coli ProteinsLigandsLipidsMass SpectrometryMembrane ProteinsModels, MolecularMolecular Dynamics SimulationMoritellaProtein MultimerizationProtein StabilityReceptors, G-Protein-CoupledBacterial ProteinsCardiolipinsEscherichia coli ProteinsLigandsLipidsMembrane ProteinsNhaA protein, E coliReceptors, G-Protein-CoupledSodium-Hydrogen Exchangers

Identifiers

PMID28077870
PMCPMC5501331
OpenAlexW2578365017

What OpenQuestion holds

Textmetadata
LicenceTDM
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.