Structural remodeling of GPI anchors during biosynthesis and after attachment to proteins

FEBS Lett. 2010 May 3;584(9):1670-7. doi: 10.1016/j.febslet.2009.10.079. Epub 2009 Oct 31.


Glycosylphosphatidylinositol (GPI) anchoring of proteins is a conserved post-translational modification in eukaryotes. In mammalian cells, approximately 150 proteins on the plasma membrane are attached to the cell surface by GPI anchors, which confer specific properties on proteins, such as association with membrane microdomains. The structures of lipid and glycan moieties on GPI anchors are remodeled during biosynthesis and after attachment to proteins. The remodeling processes are critical for transport and microdomain-association of GPI-anchored proteins. Here, we describe the structural remodeling of GPI anchors and genes required for the processes in mammals, yeast, and trypanosomes.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • Glycosylphosphatidylinositols / biosynthesis*
  • Glycosylphosphatidylinositols / chemistry*
  • Glycosylphosphatidylinositols / metabolism
  • Humans
  • Lipid Metabolism / physiology
  • Mammals
  • Membrane Proteins / metabolism*
  • Models, Biological
  • Molecular Conformation
  • Peroxisomes / metabolism
  • Peroxisomes / physiology
  • Protein Binding / physiology
  • Trypanosoma
  • Yeasts


  • Glycosylphosphatidylinositols
  • Membrane Proteins