Evidence map›Paper›PMID 34135326›Full record

ArticleNature communications2021

Ceramide structure dictates glycosphingolipid nanodomain assembly and function.

Senthil Arumugam, Stefanie Schmieder, Weria Pezeshkian, Ulrike Becken, Christian Wunder, Dan Chinnapen, John Hjort Ipsen, Anne K Kenworthy, Wayne Lencer, Satyajit Mayor and 1 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
3.2field-weighted citation impact, top 7% 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

40 citing papers in PubMed, 53 citations in OpenAlex.

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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

11 authors at 6 institutions in 6 countries.

Senthil Arumugam *Institut Curie, PSL Research University, U1143 INSERM, UMR3666 CNRS, Cellular and Chemical Biology unit, Paris, Cedex, France.
Stefanie Schmieder *Division of Gastroenterology, Boston Children's Hospital, Boston, MA, USA.ORCID 0000-0002-3696-9468
Weria Pezeshkian *Groningen Biomolecular Sciences and Biotechnology Institute and Zernike Institute for Advanced Materials, University of Groningen, Groningen, Netherlands.ORCID 0000-0001-5509-0996
Ulrike BeckenInstitut Curie, PSL Research University, U1143 INSERM, UMR3666 CNRS, Cellular and Chemical Biology unit, Paris, Cedex, France.
Christian WunderInstitut Curie, PSL Research University, U1143 INSERM, UMR3666 CNRS, Cellular and Chemical Biology unit, Paris, Cedex, France.ORCID 0000-0001-9091-0080
Dan ChinnapenDivision of Gastroenterology, Boston Children's Hospital, Boston, MA, USA.
John Hjort IpsenMEMPHYS/PhyLife, Department of Physics, Chemistry and Pharmacy, University of Southern Denmark, Odense M, Denmark.
Anne K KenworthyCenter for Membrane and Cell Physiology, University of Virginia, Charlottesville, VA, USA.ORCID 0000-0001-6567-9059
Wayne LencerDivision of Gastroenterology, Boston Children's Hospital, Boston, MA, USA.ORCID 0000-0001-7346-2730
Satyajit MayorNational Centre for Biological Sciences (NCBS), Bangalore, India. mayor@ncbs.res.in.
Ludger JohannesInstitut Curie, PSL Research University, U1143 INSERM, UMR3666 CNRS, Cellular and Chemical Biology unit, Paris, Cedex, France. ludger.johannes@curie.fr.ORCID 0000-0002-2168-0004
Centre National de la Recherche Scientifique · FRBoston Children's Hospital · USNational Centre for Biological Sciences · INUniversity of Groningen · NLUniversity of Southern Denmark · DKUniversity of Virginia · US

Funding

STRUCTURE-FUNCTION RELATIONSHIPS IN THE ALIMENTARY TRACTP30DK034854 · NIDDK · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI JONATHAN C KAGAN · 1986 to 2026
$32.4M
Function and assembly of toxin-stabilized domainsR01GM106720 · NIGMS · VANDERBILT UNIVERSITY · PI KENWORTHY, ANNE K · 2013 to 2020
$2.7M
DBT-Wellcome Trust India Alliance IA/M/15/1/502018NIDDK NIH HHS P30 DK034854NIGMS NIH HHS R01 GM106720
6 · The paper itself

Abstract

Gangliosides in the outer leaflet of the plasma membrane of eukaryotic cells are essential for many cellular functions and pathogenic interactions. How gangliosides are dynamically organized and how they respond to ligand binding is poorly understood. Using fluorescence anisotropy imaging of synthetic, fluorescently labeled GM1 gangliosides incorporated into the plasma membrane of living cells, we found that GM1 with a fully saturated C16:0 acyl chain, but not with unsaturated C16:1 acyl chain, is actively clustered into nanodomains, which depends on membrane cholesterol, phosphatidylserine and actin. The binding of cholera toxin B-subunit (CTxB) leads to enlarged membrane domains for both C16:0 and C16:1, owing to binding of multiple GM1 under a toxin, and clustering of CTxB. The structure of the ceramide acyl chain still affects these domains, as co-clustering with the glycosylphosphatidylinositol (GPI)-anchored protein CD59 occurs only when GM1 contains the fully saturated C16:0 acyl chain, and not C16:1. Thus, different ceramide species of GM1 gangliosides dictate their assembly into nanodomains and affect nanodomain structure and function, which likely underlies many endogenous cellular processes.

Indexed as

ActinsCD59 AntigensCell MembraneCeramidesCholera ToxinCholesterolGlycosphingolipidsGlycosylphosphatidylinositolsG(M1) GangliosideModels, BiologicalMolecular Dynamics SimulationPhosphatidylserinesActinsCD59 AntigensCD59 protein, humanCeramidesCholera ToxinCholesterolGlycosphingolipidsGlycosylphosphatidylinositolsG(M1) GangliosidePhosphatidylserines

Identifiers

PMID34135326
PMCPMC8209009
OpenAlexW3166930361

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.