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First published online July 23, 2008

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Safety in numbers for lipid rafts

Lipid rafts, which are cholesterol- and sphingolipid-rich microdomains in the plasma membrane, have been proposed to form `signalling platforms' by fusing in response to extracellular signals. The epidermal growth factor receptor (EGFR) localises to lipid rafts; however, limitations of fluorescence microscopy have made it difficult to determine whether EGFR-containing rafts coalesce when EGFR is activated. Now, Paul van Bergen en Henegouwen and colleagues (p. 2519) overcome this problem by using fluorescence lifetime imaging microscopy (FLIM) to show nanometre-scale colocalisation of EGFR with other lipid-raft components. The authors detect EGFR by using a single-domain antibody from llama, which can label the protein without activating it. They show that EGFR colocalises with the ganglioside GM1 whether cholesterol is present or not; by contrast, GM1 and another lipid-raft marker, glycosylphosphatidylinositol-anchored GFP (GPI-GFP), colocalise only in the presence of cholesterol. Notably, EGFR does not colocalise with GPI-GFP in the resting state, but does when cells are stimulated with EGF. Thus, two classes of GM1-containing microdomain coalesce into larger lipid microdomains in response to EGF. These results provide evidence for the existence of activatable plasma-membrane signalling platforms.

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Related articles in JCS:

EGF induces coalescence of different lipid rafts

Erik G. Hofman, Mika O. Ruonala, Arjen N. Bader, Dave van den Heuvel, Jarno Voortman, Rob C. Roovers, Arie J. Verkleij, Hans C. Gerritsen, and Paul M. P. van Bergen en Henegouwen
JCS 2008 121: 2519-2528. [Abstract] [Full Text]  

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Related articles in JCS Similar articles in this journal Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via Google Scholar Google Scholar Search for Related Content Social Bookmarking                         What's this?