Glycosylphosphatidylinositol (pronunciation ⓘ) or glycophosphatidylinositol (GPI) is a phosphoglyceride that can be attached to the C-terminus of a protein during posttranslational modification. The resulting GPI-anchored proteins play key roles in …

The GPI anchor represents a posttranslational modification of proteins with a glycolipid and is used ubiquitously in eukaryotes and most likely in some Archaea, but not in Eubacteria. GPI-anchored proteins are the major form of cell-surface proteins in protozoa. In fungi, many GPI-anchored proteins are ultimately incorporated into the cell wall.

Feb 1, 2004 · Glycosylphosphatidylinositol (GPI)-anchored proteins are attached to the lumenal side of membranes of the secretory and endocytic pathways by a glycolipid anchor.

Jun 17, 2008 · The discovery of glycosylphosphatidylinositol (GPI) membrane anchors has had a significant impact on several areas of eukaryote cell biol. Studies of the African trypanosome, which expresses a dense surface coat of GPI-anchored variant surface glycoprotein, have played important roles in establishing the general structure of GPI membrane ...

The GPI anchor is a complex structure comprising a phosphoethanolamine linker, glycan core, and phospholipid tail. GPI-anchored proteins are structurally and functionally diverse and play vital roles in numerous biological processes.

Glycosylphosphatidylinositol anchored proteins (GPI-APs) represent a class of soluble proteins attached to the external leaflet of the plasma membrane by a post-translation modification, the GPI anchor.

From the numerous studies developed at the last quarter of the 20th century, glycosylphosphatidylinositol (GPI) anchor has been established as a unique mode of protein binding to the plasma membrane. The core structure of this anchor consists of ethanolamine phosphate, trimannoside, glucosamine and …

Feb 1, 2016 · The surface of eukaryotic cells is a multi-component fluid bilayer in which glycosylphosphatidylinositol (GPI)-anchored proteins are an abundant constituent. In this review, we discuss the complex nature of the organization and dynamics of GPI-anchored proteins at multiple spatial and temporal scales.

The functions of GPI anchors (in addition to the clear one of linking the above biopolymers to membranes) have been extensively discussed. The high lateral mobility of GPIs and GPI-anchored polymers seems to actively facilitate the selective release of molecules from the cell surface and the exchange of membrane proteins between cells.

Jul 8, 2008 · This review discusses the structural diversity of the GPI anchor and its putative cellular functions, including involvement in lipid raft partitioning, signal transduction, targeting to the apical membrane, and prion disease pathogenesis.