Biosynthesis, remodelling and functions of mammalian GPI-anchored proteins: recent progress
Taroh Kinoshita1, Morihisa Fujita, Yusuke Maeda
1WPI Immunology Frontier Research Center, Osaka University, Osaka, Japan. tkinoshi@biken.osaka-u.ac.jp
Abstract:
More than 100 mammalian proteins are post-translationally modified by glycosylphosphatidylinositol (GPI) at their C-termini and are anchored to the cell surface membrane via the lipid portion. GPI-anchored proteins (GPI-APs) have various functions, such as hydrolytic enzymes, receptors, adhesion molecules, complement regulatory proteins and other immunologically important proteins. GPI-anchored proteins are mainly associated with membrane microdomains or membrane rafts enriched in sphingolipids and cholesterol. It is thought that association with membrane rafts is important for GPI-APs in signal transduction and other functions. Here, we review recent progress in studies on biosynthesis, remodelling and functions of mammalian GPI-APs.
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