Cholesterol-dependent insertion of glycosylphosphatidylinositol-anchored enzyme |
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Authors: | Morandat Sandrine Bortolato Muriel Roux Bernard |
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Affiliation: | Laboratoire de Physico-Chimie Biologique, UMR-CNRS 5013, Batiment Chevreul, Université Claude Bernard Lyon I, 43, boulevard du 11 novembre 1918, F-69622 Villeurbanne Cedex, France. |
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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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