© 2005 The Japanese Biochemical Society
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Imaging Lipid Rafts
1 Lipid Biology Laboratory, RIKEN (Institute of Physical and Chemical Research) Discovery Research Institute, and 3 Supra-Biomolecular System Research Group, RIKEN Frontier Research System, 2-1, Hirosawa, Wako, Saitama 351-0198; 2 Department of Biophysics, Graduate School of Science, Kyoto University, Kyoto 606-8502; and 4 INSERM U585, INSA (Institut National des Sciences Appliquees)-Lyon, 20 Ave A. Einstein, 69621 Villeurbanne, France
* To whom correspondence should be addressed at: Supra-Biomolecular System Research Group, RIKEN (Institute of Physical and Chemical Research) Frontier Research System, 2-1, Hirosawa, Wako, Saitama 351-0198. Tel: +81-48-467-9612; Fax: +81-48-467-8693; E-mail: kobayasi{at}riken.jp
ABSTRACT
Lipid rafts are plasma membrane microdomains enriched in sphingolipids and cholesterol. These domains have been suggested to serve as platforms for various cellular events, such as signaling and membrane trafficking. However, little is known about the distribution and dynamics of lipids in these microdomains. Here we report investigations carried out using recently developed probes for the lipid components of lipid rafts: lysenin, a sphingomyelin-binding protein obtained from the coelomic fluid of the earthworm Eisenia foetida; and the fluorescein ester of poly(ethyleneglycol) cholesteryl ether (fPEG-Chol), which partitions into cholesterol-rich membranes. Lysenin reveals that the organization of sphingomyelin differs between different cell types and even between different membrane domains within the same cell. When added to live cells, fPEG-Chol is distributed exclusively on the outer leaflet of the plasma membrane and is clustered dynamically upon activation of receptor signaling. The surface-bound fPEG-Chol is slowly internalized via a clathrin-independent pathway into endosomes with lipid raft markers.
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