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. 2002 Aug 31;1564(2):473-78.
doi: 10.1016/s0005-2736(02)00497-2.

Cholesterol-dependent insertion of glycosylphosphatidylinositol-anchored enzyme

Sandrine Morandat  1 , Muriel Bortolato, Bernard Roux
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Cholesterol-dependent insertion of glycosylphosphatidylinositol-anchored enzyme

Sandrine Morandat et al. Biochim Biophys Acta. .
Free article

Abstract

Evidence is now accumulating that the plasma membrane is organized in different lipid and protein subdomains. Thus, glycosylphosphatidylinositol (GPI)-anchored proteins are proposed to be clustered in membrane microdomains enriched in cholesterol and sphingolipids, called rafts. By a detergent-mediated method, alkaline phosphatase, a GPI-anchored enzyme, was efficiently inserted into the membrane of sphingolipids- and cholesterol-rich liposomes as demonstrated by flotation in sucrose gradients. We have determined the enzyme extraluminal orientation. Using defined lipid components to assess the possible requirements for GPI-anchored protein insertion, we have demonstrated that insertion into membranes was cholesterol-dependent as the cholesterol addition increased the enzyme incorporation in simple phosphatidylcholine liposomes.

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