Revealing the Raft Domain Organization in the Plasma Membrane by Single-Molecule Imaging of Fluorescent Ganglioside Analogs

Methods in Enzymology
Kenichi G N SuzukiAkihiro Kusumi

Abstract

Gangliosides have been implicated in a variety of physiological processes, particularly in the formation and function of raft domains in the plasma membrane. However, the scarcity of suitable fluorescent ganglioside analogs had long prevented us from determining exactly how gangliosides perform their functions in the live-cell plasma membrane. With the development of new fluorescent ganglioside analogs, as described by Komura et al. (2017), this barrier has been broken. We can now address the dynamic behaviors of gangliosides in the live-cell plasma membrane, using fluorescence microscopy, particularly by single-fluorescent molecule imaging and tracking. Single-molecule tracking of fluorescent GM1 and GM3 revealed that these molecules are transiently and dynamically recruited to monomers (monomer-associated rafts) and homodimer rafts of the raftophilic GPI-anchored protein CD59 in quiescent cells, with exponential residency times of 12 and 40ms, respectively, in a manner dependent on raft-lipid interactions. Upon CD59 stimulation, which induces CD59-cluster signaling rafts, the fluorescent GM1 and GM3 analogs were recruited to the signaling rafts, with a lifetime of 48ms. These results represent the first direct evidence that G...Continue Reading

Citations

Nov 25, 2019·Traffic·Akihiro KusumiKenichi G N Suzuki
Jan 9, 2019·Frontiers in Cell and Developmental Biology·Roger J Morris
Jun 18, 2021·Nature Communications·Senthil ArumugamLudger Johannes
Jun 4, 2021·Journal of Neurochemistry·Kristina Mlinac-JerkovicMarija Heffer
Aug 28, 2021·International Journal of Molecular Sciences·Laurent FernandezPierre-Emmanuel Milhiet

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