Ceramide structure dictates glycosphingolipid nanodomain assembly and function

Gangliosides such as GM1 present in the outer leaflet of the plasma membrane of eukaryotic cells are essential for many cellular functions and pathogenic interactions. Here the authors show that the acyl chain structure of GM1 determines the establishment of nanodomains when actively clustered by ac...

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Autores principales:	Senthil Arumugam, Stefanie Schmieder, Weria Pezeshkian, Ulrike Becken, Christian Wunder, Dan Chinnapen, John Hjort Ipsen, Anne K. Kenworthy, Wayne Lencer, Satyajit Mayor, Ludger Johannes
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/41a538c93c3c48b9859f96ed5bb6999e
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spelling	oai:doaj.org-article:41a538c93c3c48b9859f96ed5bb6999e2021-12-02T17:23:48ZCeramide structure dictates glycosphingolipid nanodomain assembly and function10.1038/s41467-021-23961-92041-1723https://doaj.org/article/41a538c93c3c48b9859f96ed5bb6999e2021-06-01T00:00:00Zhttps://doi.org/10.1038/s41467-021-23961-9https://doaj.org/toc/2041-1723Gangliosides such as GM1 present in the outer leaflet of the plasma membrane of eukaryotic cells are essential for many cellular functions and pathogenic interactions. Here the authors show that the acyl chain structure of GM1 determines the establishment of nanodomains when actively clustered by actin, which depended on membrane cholesterol and phosphatidylserine or superimposed by the GM1-binding bacterial cholera toxin.Senthil ArumugamStefanie SchmiederWeria PezeshkianUlrike BeckenChristian WunderDan ChinnapenJohn Hjort IpsenAnne K. KenworthyWayne LencerSatyajit MayorLudger JohannesNature PortfolioarticleScienceQENNature Communications, Vol 12, Iss 1, Pp 1-12 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Senthil Arumugam Stefanie Schmieder Weria Pezeshkian Ulrike Becken Christian Wunder Dan Chinnapen John Hjort Ipsen Anne K. Kenworthy Wayne Lencer Satyajit Mayor Ludger Johannes Ceramide structure dictates glycosphingolipid nanodomain assembly and function
description	Gangliosides such as GM1 present in the outer leaflet of the plasma membrane of eukaryotic cells are essential for many cellular functions and pathogenic interactions. Here the authors show that the acyl chain structure of GM1 determines the establishment of nanodomains when actively clustered by actin, which depended on membrane cholesterol and phosphatidylserine or superimposed by the GM1-binding bacterial cholera toxin.
format	article
author	Senthil Arumugam Stefanie Schmieder Weria Pezeshkian Ulrike Becken Christian Wunder Dan Chinnapen John Hjort Ipsen Anne K. Kenworthy Wayne Lencer Satyajit Mayor Ludger Johannes
author_facet	Senthil Arumugam Stefanie Schmieder Weria Pezeshkian Ulrike Becken Christian Wunder Dan Chinnapen John Hjort Ipsen Anne K. Kenworthy Wayne Lencer Satyajit Mayor Ludger Johannes
author_sort	Senthil Arumugam
title	Ceramide structure dictates glycosphingolipid nanodomain assembly and function
title_short	Ceramide structure dictates glycosphingolipid nanodomain assembly and function
title_full	Ceramide structure dictates glycosphingolipid nanodomain assembly and function
title_fullStr	Ceramide structure dictates glycosphingolipid nanodomain assembly and function
title_full_unstemmed	Ceramide structure dictates glycosphingolipid nanodomain assembly and function
title_sort	ceramide structure dictates glycosphingolipid nanodomain assembly and function
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/41a538c93c3c48b9859f96ed5bb6999e
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Ceramide structure dictates glycosphingolipid nanodomain assembly and function

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