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 Ludger Johannes ()
Additional contact information
Senthil Arumugam: Institut Curie, PSL Research University, U1143 INSERM, UMR3666 CNRS, Cellular and Chemical Biology unit
Stefanie Schmieder: Boston Children’s Hospital
Weria Pezeshkian: University of Groningen
Ulrike Becken: Institut Curie, PSL Research University, U1143 INSERM, UMR3666 CNRS, Cellular and Chemical Biology unit
Christian Wunder: Institut Curie, PSL Research University, U1143 INSERM, UMR3666 CNRS, Cellular and Chemical Biology unit
Dan Chinnapen: Boston Children’s Hospital
John Hjort Ipsen: University of Southern Denmark
Anne K. Kenworthy: University of Virginia
Wayne Lencer: Boston Children’s Hospital
Satyajit Mayor: National Centre for Biological Sciences (NCBS)
Ludger Johannes: Institut Curie, PSL Research University, U1143 INSERM, UMR3666 CNRS, Cellular and Chemical Biology unit

Nature Communications, 2021, vol. 12, issue 1, 1-12

Abstract: 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.

Date: 2021
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DOI: 10.1038/s41467-021-23961-9

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