Lipid Rafts


The knowledge about the structure of the biological membrane changed during the last 70 years. In the 70s, Singer and Nicholson proposed the fluid mosaic model, a major conceptual breakthrough in which amphiphilic proteins reside within the lipid bilayer. In this dynamic structure, components can move laterally. Further works led to major modifications of this model. Indeed, functional aspects of trafficking and signal transduction suggested that lipids and proteins do not distribute randomly but can be sequestered in small domains, thus enhancing protein–protein interactions and speeding up signal transduction and enzyme activity. The ‘raft hypothesis’ was born. Rafts are small and transient microdomains enriched in sphingolipids and sterols, together with specific proteins with important functions. This hypothesis explains the heterogeneity of the distribution of membrane proteins by a spontaneous demixing of lipids to form domains involved in signal transduction, cell trafficking and host–pathogen relationship.

Key Concepts:

  • Biological membranes are organised in small, dynamic and transient domains called lipid rafts.

  • Lipid rafts exist in all eukaryotic cells, mostly in the plasma membrane.

  • Lipid rafts are enriched in sphingolipids and sterols, and depleted in phosphoglycerolipids.

  • Lipid rafts are involved in signal transduction pathways, cell trafficking and host–pathogen relationship.

Keywords: sphingolipids; sterols; phosphoglycerolipids; signalling; domains; epithelial cells; detergent; detergent‐insoluble membranes (DIM); detergent‐resistant membranes (DRM); detergent‐soluble membranes (DSM)

Figure 1.

Animal and plant polarised cells. (a) Polarised animal intestinal epithelial cell exhibit targeting of PM proteins to the basolateral or apical membranes with tight junctions that delineate the two regions by preventing lateral diffusion. Localisation of carbonic anhydrase XII, apical localisation of carbonic anhydrase IV, and basolasteral redistribution of β(1)‐integrin or Na+/K+ ATPase after a pathogen‐induced change in cellular polarity. Dashed lines denote redistributed proteins. (b) Plant cells have cell walls and lack tight junctions to define the polarity of the cell. Four types of PM domains have been documented in plants. Nonpolar localisation of the ATPase, basal localisation of plant hormone auxin transporter PIN1, lateral localisation of GPI‐anchored protein COBRA, apical localisation of auxin transporter AUX1, and vectorial redistribution of PIN3 after a gravitropic stimulus. Reproduced from Murphy et al. with permission of Annual Reviews, Inc.

Figure 2.

Spatial organisation of membrane rafts; Ternary lipid phase diagram for a lipid mixture imitating plasma membrane. (a) Structure of main lipids found in biological membranes. Reproduced from Munro with permission from Elsevier.. (b) Spatial organisation of sterols, phosphoglycerolipids and sphingolipids in raft domains. Reproduced from Quinn with permission from Elsevier. (c) Phase diagrams at 37 °C of three‐component bilayer mixture at different concentration (egg‐phosphatidylcholine:egg‐sphingomyelin:cholesterol, that is, a high‐ and low‐melting point lipids together with sterol) showing the co‐existence of Lo and Ld phases. Around the diagram is depicted structures of lipid bilayers with G:gel phase, solid ordered; Ld: liquid disordered phase; Lo=liquid ordered phase. Reproduced from Simons K and Ikonen E (1997) Functional Rafts in Cell Membranes. Nature 387(6633): 569–572.

Figure 3.

Chemical structures of some animal and plant raft lipids. Reproduced from Bodin S, Tronchere H and Payrastre B (2003) Lipid Rafts Are Critical Membrane Domains in Blood Platelet Activation Processes. Biochimica et Biophysica Acta 1610: 247–257, with permission from Elsevier.

Figure 4.

Proteins found enriched in membrane raft of the plasma membrane according to their anchorage and putative coalescence of raft after stimulus. (a) Caveolin are shown in green in a caveolae, a morphologically discrete flask‐shaped structure with raft properties. Acylated proteins (orange) partition into rafts (yellow) in the inner leaflet of the PM, and in close proximity to caveolin. Glycosphingolipid‐enriched domains (pink) are shown in the outer leaflet of the PM, enriched in GPI‐anchored proteins (red). All these domains are too small to resolve by fluorescence microscopy, with the exception of caveolae. (b) Stimuli‐induced raft (in red) coalescence, which facilitates the clustering of signalling‐related molecules allowing a rapid signal transduction inside the cells.Reproduced from Kenworthy A (2002) Peering Inside Lipid Rafts and Caveolae. Trends in Biochemical Sciences 27(9): 435–437, with permission from Elsevier.



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Further Reading

Binder WH, Barragan V and Menger FM (2003) Domains and rafts in lipid membranes. Angewandte Chemie International Edition (England) 42: 5802–5827.

Furt F, Lefebvre B, Cullimore J, Bessoule JJ and Mongrand S (2007) Plant lipid rafts: fluctuat nec mergitur. Plant Signaling & Behavior 2: 508–511.

Furt F, Simon‐Plas F and Mongrand S (2011) Lipids of the plasma membrane. In: Murphy AS, Wendy P and Schulz B (eds) The Plant Plasma Membrane. Plant Cell Monographs 19, pp. 3–30. Heidelberg: Springer‐Verlag.

Grecco HE, Schmick M and Bastiaens PI (2011) Signaling from the living plasma membrane. Cell 144: 897–909.

Mongrand S, Stanislas T, Bayer EM, Lherminier J and Simon‐Plas F (2010) Membrane rafts in plant cells. Trends in Plant Science 15: 656–663.

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Germain, Véronique, Perraki, Artemis, and Mongrand, Sébastien(Sep 2012) Lipid Rafts. In: eLS. John Wiley & Sons Ltd, Chichester. [doi: 10.1002/9780470015902.a0023727]