Evidence map›Paper›PMID 26915987›Full record

ArticleScientific reports2016

A mirror code for protein-cholesterol interactions in the two leaflets of biological membranes.

Jacques Fantini, Coralie Di Scala, Luke S Evans, Philip T F Williamson, Francisco J Barrantes

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.

0numbers the graph read from it
0cells of the map it votes in
60citing papers in PubMed
8.9field-weighted citation impact, top 2% 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

60 citing papers in PubMed, 122 citations in OpenAlex.

  1. Review
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  4. The journal of physical chemistry. B · 2026
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  9. Analysis of cholesterol-recognition motifs of the plasma membrane CaJournal of bioenergetics and biomembranes · 2024
    Article
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  15. Article
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  18. ACS chemical biology · 2022
    Article
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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

5 authors at 3 institutions in 3 countries.

Jacques FantiniEA-4674, Interactions Moléculaires et Systèmes Membranaires, Aix-Marseille Université, Marseille, France.
Coralie Di ScalaEA-4674, Interactions Moléculaires et Systèmes Membranaires, Aix-Marseille Université, Marseille, France.
Luke S EvansCentre for Biological Sciences/Institute for Life Sciences, University of Southampton, Southampton, SO17 1BJ, United Kingdom.
Philip T F WilliamsonCentre for Biological Sciences/Institute for Life Sciences, University of Southampton, Southampton, SO17 1BJ, United Kingdom.
Francisco J BarrantesLaboratory of Molecular Neurobiology, Biomedical Research Institute (BIOMED) UCA-CONICET, Faculty of Medical Sciences, Catholic University of Argentina, Buenos Aires, Argentina.
Aix-Marseille Université · FRUniversity of Southampton · GBPontificia Universidad Católica Argentina · AR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cholesterol controls the activity of a wide range of membrane receptors through specific interactions and identifying cholesterol recognition motifs is therefore critical for understanding signaling receptor function. The membrane-spanning domains of the paradigm neurotransmitter receptor for acetylcholine (AChR) display a series of cholesterol consensus domains (referred to as "CARC"). Here we use a combination of molecular modeling, lipid monolayer/mutational approaches and NMR spectroscopy to study the binding of cholesterol to a synthetic CARC peptide. The CARC-cholesterol interaction is of high affinity, lipid-specific, concentration-dependent, and sensitive to single-point mutations. The CARC motif is generally located in the outer membrane leaflet and its reverse sequence CRAC in the inner one. Their simultaneous presence within the same transmembrane domain obeys a "mirror code" controlling protein-cholesterol interactions in the outer and inner membrane leaflets. Deciphering this code enabled us to elaborate guidelines for the detection of cholesterol-binding motifs in any membrane protein. Several representative examples of neurotransmitter receptors and ABC transporters with the dual CARC/CRAC motifs are presented. The biological significance and potential clinical applications of the mirror code are discussed.

Indexed as

Amino Acid MotifsATP-Binding Cassette TransportersCell MembraneCholesterolHumansMagnetic Resonance SpectroscopyModels, MolecularMutationProtein BindingReceptors, CholinergicATP-Binding Cassette TransportersCholesterolReceptors, Cholinergic

Identifiers

PMID26915987
PMCPMC4768152
OpenAlexW2341038434

What OpenQuestion holds

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LicenceCC BY
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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.