Glycosylphosphatidylinositol-anchored proteins (GPI-APs) contain a covalently linked GPI anchor located on outer cell membranes. GPI-APs are ubiquitously conserved from protozoa to vertebrates and are critical for physiological events such as development, immunity, and neurogenesis in vertebrates. Both membrane-anchored and soluble GPI-APs play a role in regulating their protein conformation and functional properties. Several pathways mediate the release of GPI-APs from the plasma membrane by vesiculation or cleavage. Phospholipases and putative substrate-specific GPI-AP-releasing enzymes, such as NOTUM, glycerophosphodiesterase 2, and angiotensin-converting enzyme, have been characterized in mammals. Here, the protein modifications resulting from the cleavage of the GPI anchor are discussed in the context of its physiological functions.
Keywords: GPIase; IZUMO1 receptor/JUNO; gene expression; genetics; glycosylphosphatidylinositol-anchored protein; glypican; membranes; phospholipases; phospholipids/phosphatidylinositol; reversion-inducing cysteine-rich protein with kazal motifs; testis-expressed gene 101.
Copyright © 2016 by the American Society for Biochemistry and Molecular Biology, Inc.