Evidence map›Paper›PMID 32710822›Full record

ArticleBiophysical journal2020

Induction of Ordered Lipid Raft Domain Formation by Loss of Lipid Asymmetry.

Johnna Wellman St Clair, Shinako Kakuda, Erwin London

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
2.3field-weighted citation impact, top 11% 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

19 citing papers in PubMed, 34 citations in OpenAlex.

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  5. Frontiers in microbiology · 2024
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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

3 authors at 1 institution in 1 country.

Johnna Wellman St ClairDepartment of Biochemistry and Cell Biology, Stony Brook University, Stony Brook, New York.
Shinako KakudaDepartment of Biochemistry and Cell Biology, Stony Brook University, Stony Brook, New York.
Erwin LondonDepartment of Biochemistry and Cell Biology, Stony Brook University, Stony Brook, New York. Electronic address: erwin.london@stonybrook.edu.
Stony Brook University · US

Funding

TRANSFORMATIVE LIPID EXCHANGE APPROACHES TO STUDY MEMBRANE ORGANIZATIONR35GM122493 · NIGMS · STATE UNIVERSITY NEW YORK STONY BROOK · PI Erwin London · 2017 to 2026
$5.6M
DEFINING PRINCIPLES AND FUNCTIONS OF MEMBRANE ORGANIZATION USING ASYMMETRIC VESICLESR01GM112638 · NIGMS · STATE UNIVERSITY NEW YORK STONY BROOK · PI LONDON, ERWIN · 2015 to 2017
$922k
NIGMS NIH HHS R01 GM112638NIGMS NIH HHS R35 GM122493
6 · The paper itself

Abstract

How lipid asymmetry impacts ordered lipid domain (raft) formation may yield important clues to how ordered domain formation is regulated in vivo. Under some conditions, a sphingomyelin (SM) and cholesterol-rich ordered domain in one leaflet induces ordered domain formation in the corresponding region of an opposite leaflet composed of unsaturated phosphatidylcholine (PC) and cholesterol. In other conditions, the formation of ordered domains in a SM and cholesterol-rich leaflet can be suppressed by an opposite leaflet containing unsaturated PC and cholesterol. To explore how PC unsaturation influences the balance between these behaviors, domain formation was studied in asymmetric and symmetric lipid vesicles composed of egg SM, cholesterol, and either unsaturated dioleoyl PC (DOPC) or 1-palmitoyl 2-oleoyl PC (POPC). The temperature dependence of ordered domain formation was measured using Förster resonance energy transfer, which detects nanodomains as well as large domains. In cholesterol-containing asymmetric SM+PC outside/PC inside vesicles, the PC-containing inner leaflet tended to destabilize ordered domain formation in the SM+PC-containing outer leaflet relative to ordered domain stability in cholesterol-containing symmetric SM/PC vesicles. Residual ordered domain formation was detected in cholesterol-containing asymmetric SM+DOPC outside/DOPC inside vesicles, but ordered domain formation was completely or almost completely suppressed by asymmetry in cholesterol-containing SM+POPC outside/POPC inside vesicles over the entire temperature range measured. Suppression of ordered domain formation in the latter vesicles was confirmed by fluorescence anisotropy measurements. Because mixtures of SM, POPC, and cholesterol form domains in symmetric vesicles, and this lipid composition mimics plasma membranes to a significant degree, it is possible that under some conditions in vivo the loss of lipid asymmetry could trigger ordered domain formation.

Indexed as

Membrane MicrodomainsPhosphatidylcholinesCell MembraneCholesterolFluorescence Resonance Energy TransferLipid BilayersSphingomyelinsCholesterolLipid BilayersPhosphatidylcholinesSphingomyelins

Identifiers

PMID32710822
PMCPMC7399498
OpenAlexW3041750699

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.