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Biosynthesis, remodelling and functions of mammalian GPI-anchored proteins: Recent progress

Journal

JOURNAL OF BIOCHEMISTRY
Volume 144, Issue 3, Pages 287-294

Publisher

OXFORD UNIV PRESS
DOI: 10.1093/jb/mvn090

Keywords

endoplasmic reticulum; fatty acid; glycosyltransferases; Golgi apparatus; post-translational modification

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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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