Glypiation
From Wikipedia, the free encyclopedia
Glypiation is the addition by covalent bonding of a glycosylphosphatidylinositol (GPI) anchor and is a common post-translational modification that localizes proteins to cell membranes. This special kind of glycosylation is widely detected on surface glycoproteins in eukaryotes and some Archaea.[1]
GPI anchors consist of a phosphoethanolamine linker that binds to the C-terminus of target proteins. Glycan's core structure has a phospholipid tail that anchors the structure to the membrane.
Both the lipid moiety of the tail and the sugar residues in the glycan core have considerable variation,[2][3][4][5][6][7] demonstrating vast functional diversity that includes signal transduction, cell adhesion and immune recognition.[8] GPI anchors can also be cleaved by enzymes such as phospholipase C to regulate the localization of proteins that are anchored at the plasma membrane.