Biosynthesis, remodelling and functions of mammalian GPI-anchored proteins: recent progress.
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.
Kinoshita
Taroh
T
WPI Immunology Frontier Research Center, Osaka University, Osaka, Japan. tkinoshi@biken.osaka-u.ac.jp
Fujita
Morihisa
M
Maeda
Yusuke
Y
D000818:Animals; D016466:CHO Cells; D002462:Cell Membrane / Q000378:metabolism; D006224:Cricetinae; D003412:Cricetulus; D005786:Gene Expression Regulation; D017261:Glycosylphosphatidylinositols / Q000737:chemistry* / Q000502:physiology; D006801:Humans; D008055:Lipids / Q000737:chemistry; D008565:Membrane Proteins / Q000378:metabolism; D051379:Mice; D008822:Mice, Transgenic; D008954:Models, Biological; D011485:Protein Binding; D015398:Signal Transduction
D017261:Glycosylphosphatidylinositols; D008055:Lipids; D008565:Membrane Proteins