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

J Biochem. 2008 Sep;144(3):287-94. doi: 10.1093/jb/mvn090. Epub 2008 Jul 17.

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.

Publication types

  • Review

MeSH terms

  • Animals
  • CHO Cells
  • Cell Membrane / metabolism
  • Cricetinae
  • Cricetulus
  • Gene Expression Regulation*
  • Glycosylphosphatidylinositols / chemistry*
  • Glycosylphosphatidylinositols / physiology
  • Humans
  • Lipids / chemistry
  • Membrane Proteins / metabolism
  • Mice
  • Mice, Transgenic
  • Models, Biological
  • Protein Binding
  • Signal Transduction

Substances

  • Glycosylphosphatidylinositols
  • Lipids
  • Membrane Proteins