Evidence map›Paper›PMID 23579615›Full record

ArticlePloS one2013

Differential lipid dependence of the function of bacterial sodium channels.

Nazzareno D'Avanzo, Emily C McCusker, Andrew M Powl, Andrew J Miles, Colin G Nichols, B A Wallace

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

15 citing papers in PubMed, 23 citations in OpenAlex.

  1. Article
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  6. Cryo-EM structures of a lipid-sensitive pentameric ligand-gated ion channel embedded in a phosphatidylcholine-only bilayer.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  7. Article
  8. Article
  9. Cell-free expression of a functional pore-only sodium channel.Protein expression and purification · 2015
    Article
  10. Review
  11. Article
  12. Review
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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

6 authors at 4 institutions in 3 countries.

Nazzareno D'AvanzoDepartment of Physiology and GEPROM (Group d'étude des Proteins Membranaires), Université de Montréal, Montréal, Québec, Canada.
Emily C McCusker
Andrew M Powl
Andrew J Miles
Colin G Nichols
B A Wallace
Birkbeck, University of London · GBInstitute of Structural and Molecular Biology · GBUniversité de Montréal · CAWashington University in St. Louis · US

Funding

Rectification &Block of Ion Channel CurrentsR01HL054171 · NHLBI · WASHINGTON UNIVERSITY · PI NICHOLS, COLIN G · 1995 to 2017
$4.5M
LIPID REGULATION OF PURIFIED EUKARYOTIC POTASSIUM CHANNELSK99HL112300 · NHLBI · WASHINGTON UNIVERSITY · PI D'AVANZO, NAZZARENO · 2012 to 2012
$47k
Biotechnology and Biological Sciences Research Council BB/H01070X/1NHLBI NIH HHS HL54171NHLBI NIH HHS K99 HL112300NHLBI NIH HHS K99 HL112300-01NHLBI NIH HHS R01 HL054171
6 · The paper itself

Abstract

The lipid bilayer is important for maintaining the integrity of cellular compartments and plays a vital role in providing the hydrophobic and charged interactions necessary for membrane protein structure, conformational flexibility and function. To directly assess the lipid dependence of activity for voltage-gated sodium channels, we compared the activity of three bacterial sodium channel homologues (NaChBac, NavMs, and NavSp) by cumulative (22)Na(+) uptake into proteoliposomes containing a 3∶1 ratio of 1-palmitoyl 2-oleoyl phosphatidylethanolamine and different "guest" glycerophospholipids. We observed a unique lipid profile for each channel tested. NavMs and NavSp showed strong preference for different negatively-charged lipids (phosphatidylinositol and phosphatidylglycerol, respectively), whilst NaChBac exhibited a more modest variation with lipid type. To investigate the molecular bases of these differences we used synchrotron radiation circular dichroism spectroscopy to compare structures in liposomes of different composition, and molecular modeling and electrostatics calculations to rationalize the functional differences seen. We then examined pore-only constructs (with voltage sensor subdomains removed) and found that in these channels the lipid specificity was drastically reduced, suggesting that the specific lipid influences on voltage-gated sodium channels arise primarily from their abilities to interact with the voltage-sensing subdomains.

Indexed as

Lipid MetabolismAmino Acid SequenceBacteriaCircular DichroismGene ExpressionLipid BilayersModels, MolecularMolecular Sequence DataPhosphatidylinositol 4,5-DiphosphateProtein ConformationSequence AlignmentSodiumStatic ElectricityVoltage-Gated Sodium ChannelsLipid BilayersPhosphatidylinositol 4,5-DiphosphateSodiumVoltage-Gated Sodium Channels

Identifiers

PMID23579615
PMCPMC3620320
OpenAlexW2104888262

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.