Evidence map›Paper›PMID 34843684›Full record

ArticleJournal of lipid research2022

Loss of plasma membrane lipid asymmetry can induce ordered domain (raft) formation.

Shinako Kakuda, Pavana Suresh, Guangtao Li, Erwin London

Open access · goldAbstract read
In one paragraph

Article in Journal of lipid research, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.0field-weighted citation impact, top 25% 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

16 citing papers in PubMed, 20 citations in OpenAlex.

  1. Article
  2. Protein-enhanced small molecule disruptors of ordered membrane domains.Proceedings of the National Academy of Sciences of the United States of America · 2026
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  13. Experimentally determined leaflet-leaflet phase diagram of an asymmetric lipid bilayer.Proceedings of the National Academy of Sciences of the United States of America · 2023
    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

4 authors at 1 institution in 1 country.

Shinako KakudaDepartment of Biochemistry and Cell Biology, Stony Brook University, Stony Brook, NY, USA.
Pavana SureshDepartment of Biochemistry and Cell Biology, Stony Brook University, Stony Brook, NY, USA.
Guangtao LiDepartment of Biochemistry and Cell Biology, Stony Brook University, Stony Brook, NY, USA.
Erwin LondonDepartment of Biochemistry and Cell Biology, Stony Brook University, Stony Brook, NY, USA. 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
NIGMS NIH HHS R35 GM122493
6 · The paper itself

Abstract

In some cases, lipids in one leaflet of an asymmetric artificial lipid vesicle suppress the formation of ordered lipid domains (rafts) in the opposing leaflet. Whether this occurs in natural membranes is unknown. Here, we investigated this issue using plasma membrane vesicles (PMVs) from rat leukemia RBL-2H3 cells. Membrane domain formation and order was assessed by fluorescence resonance energy transfer and fluorescence anisotropy. We found that ordered domains in PMVs prepared from cells by N-ethyl maleimide (NEM) treatment formed up to ∼37°C, whereas ordered domains in symmetric vesicles formed from the extracted PMV lipids were stable up to 55°C, indicating the stability of ordered domains was substantially decreased in intact PMVs. This behavior paralleled lesser ordered domain stability in artificial asymmetric lipid vesicles relative to the corresponding symmetric vesicles, suggesting intact PMVs exhibit some degree of lipid asymmetry. This was supported by phosphatidylserine mislocalization on PMV outer leaflets as judged by annexin binding, which indicated NEM-induced PMVs are much more asymmetric than PMVs formed by dithiothreitol/paraformaldehyde treatment. Destroying asymmetry by reconstitution of PMVs using detergent dilution also showed stabilization of domain formation, even though membrane proteins remained associated with reconstituted vesicles. Similar domain stabilization was observed in artificial asymmetric lipid vesicles after destroying asymmetry via detergent reconstitution. Proteinase K digestion of proteins had little effect on domain stability in NEM PMVs. We conclude that loss of PMV lipid asymmetry can induce ordered domain formation. The dynamic control of lipid asymmetry in cells may regulate domain formation in plasma membranes.

Indexed as

Cell MembraneMembrane MicrodomainsAnimalsCell Line, TumorMembrane LipidsRatsMembrane Lipidsannexindithiothreitolfluorescence anisotropyfluorescence resonance energy transferleaflet asymmetrylipid raftsliquid orderedmembrane domainsN-ethyl maleimideplasma membrane vesicles

Identifiers

PMID34843684
PMCPMC8953672
OpenAlexW3215710678

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.