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By D.E. Vance

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And Seydel, U. (1999) Non-lamellar structure and negative charges of lipopolysaccharides required for efficient folding of outer membrane protein PhoE of Escherichia coli. J. Biol. Chem. 274, 5114-5119. , Lutterodt, L. H. (2001) Cardiolipin binds nonyl acridine orange by aggregating the dye at exposed hydrophobic domains on bilayer surfaces. FEBS Lett. 507, 187-190. Simons, K. and Ikonen, E. (2000) How cells handle cholesterol. Science 290, 1721-1726. Mileykovskaya, E. and Dowhan, W. (2000) Visualization of phospholipid domains in Escherichia coli by using the cardiolipin-specific fluorescent dye 10-N-nonyl acridine orange.

However, they have never been observed in the native state, presumably due to their small size and possibly their loose association and dynamic properties. The raft components may normally have low affinity for each other, but increase their affinity when clustering is induced by other processes. It still is not clear how glycosylphosphatidylinositol-linked proteins on the exterior of the cell interact with acylated proteins that appear to be associated with rafts on the interior surface of the membrane.

Copyright 2000 American Association for the Advancement of Science. m e m b r a n e fraction as well as phosphorylated. For example, clustering of the IgE receptor, Fc~RI, b y b i n d i n g its l i g a n d on the cell surface results in its p h o s p h o r y l a t i o n by a Src-family k i n a s e that activates a s i g n a l i n g cascade. O n l y the receptor associated with the detergent-resistant m e m b r a n e fraction is phosphorylated. The Src-family of 31 kinases is believed to localize to lipid rafts from the cytosolic side of the membrane via covalently attached fatty acids that insert into the membrane (Fig.

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