Abstract
A number of proteins on the plasma membrane are modified by the glycolipid, glycosylphosphatidylinositol (GPI). These proteins are called GPI-anchored proteins (GPI-APs) and approximately 150 proteins exist as GPI-anchored forms in mammals. Characteristics of GPI-APs include: 1) forming membrane domains with specific lipids such as sphingolipids and cholesterol on the cell membrane and 2) cleavage at the GPI moiety to release the protein from the cell surface. Since complete structures of GPI anchors were determined in 1988, genes involved in biosynthetic pathways and structural remodeling of GPI anchors have been identified. In recent years, structural remodeling of GPI has been shown to regulate quality control, transport and localization of GPI-APs. In addition, particular GPI-cleaving enzymes cause shedding of GPI-APs from the cell surface. Here, I introduce recent progress about the structural chemistry and cleaving mechanisms of GPI-anchors.
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