Evidence map›Paper›PMID 28536532›Full record

ArticleFrontiers in physiology2017

Phase Partitioning of GM1 and Its Bodipy-Labeled Analog Determine Their Different Binding to Cholera Toxin.

Sami Rissanen, Michal Grzybek, Adam Orłowski, Tomasz Róg, Oana Cramariuc, Ilya Levental, Christian Eggeling, Erdinc Sezgin, Ilpo Vattulainen

Open access · goldAbstract read
In one paragraph

Article in Frontiers in physiology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
2.2field-weighted citation impact, top 12% 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

24 citing papers in PubMed, 38 citations in OpenAlex.

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  15. Structured clustering of the glycosphingolipid GM1 is required for membrane curvature induced by cholera toxin.Proceedings of the National Academy of Sciences of the United States of America · 2020
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  16. Article
  17. Synthesis of GbAngewandte Chemie (International ed. in English) · 2019
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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

9 authors at 7 institutions in 6 countries.

Sami RissanenDepartment of Physics, Tampere University of TechnologyTampere, Finland.
Michal GrzybekPaul Langerhans Institute Dresden of the Helmholtz Centre Munich at the University Clinic Carl Gustav Carus, TU DresdenDresden, Germany.
Adam OrłowskiDepartment of Physics, Tampere University of TechnologyTampere, Finland.
Tomasz RógDepartment of Physics, Tampere University of TechnologyTampere, Finland.
Oana CramariucDepartment of Physics, Tampere University of TechnologyTampere, Finland.
Ilya LeventalDepartment of Integrative Biology and Pharmacology, University of Texas Health Science CenterHouston, TX, USA.
Christian EggelingMRC Human Immunology Unit, Weatherall Institute of Molecular Medicine, University of OxfordOxford, UK.
Erdinc SezginMRC Human Immunology Unit, Weatherall Institute of Molecular Medicine, University of OxfordOxford, UK.
Ilpo VattulainenDepartment of Physics, Tampere University of TechnologyTampere, Finland.
Tampere University · FIUniversity of Helsinki · FIMRC Human Immunology Unit · GBTampere University · FITechnische Universität Dresden · DEThe University of Texas Health Science Center at Houston · USUniversity of Oxford · GB

Funding

Medical Research Council G0902418Medical Research Council MC_UU_00008/9Medical Research Council MC_UU_12010/9Medical Research Council MR/K01577X/1
6 · The paper itself

Abstract

Driven by interactions between lipids and proteins, biological membranes display lateral heterogeneity that manifests itself in a mosaic of liquid-ordered (Lo) or raft, and liquid-disordered (Ld) or non-raft domains with a wide range of different properties and compositions. In giant plasma membrane vesicles and giant unilamellar vesicles, specific binding of Cholera Toxin (CTxB) to GM1 glycolipids is a commonly used strategy to label raft domains or Lo membrane environments. However, these studies often use acyl-chain labeled bodipy-GM1 (bdGM1), whose headgroup accessibility and membrane order or phase partitioning may differ from those of GM1, rendering the interpretation of CTxB binding data quite problematic. To unravel the molecular basis of CTxB binding to GM1 and bdGM1, we explored the partitioning and the headgroup presentation of these gangliosides in the Lo and Ld phases using atomistic molecular dynamics simulations complemented by CTxB binding experiments. The conformation of both GM1 and bdGM1 was shown to be largely similar in the Lo and Ld phases. However, bdGM1 showed reduction in receptor availability when reconstituted into synthetic bilayer mixtures, highlighting that membrane phase partitioning of the gangliosides plays a considerable role in CTxB binding. Our results suggest that the CTxB binding is predominately modulated by the partitioning of the receptor to an appropriate membrane phase. Further, given that the Lo and Ld partitioning of bdGM1 differs from those of GM1, usage of bdGM1 for studying GM1 behavior in cells can lead to invalid interpretation of experimental data.

Indexed as

cholera toxingangliosideGM1membrane domainsmodel membranesmolecular dynamics simulations

Identifiers

PMID28536532
PMCPMC5422513
OpenAlexW2613712975

What OpenQuestion holds

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LicenceCC BY
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Registered trials

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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.