Glycosylphosphatidylinositol (GPI)-anchored proteins are a class of lipid-anchored membrane proteins that are ubiquitously expressed at the surface of eukaryotic cells. GPI proteins represent roughly 1% of all proteins encoded by eukaryotic genomes. They differ from traditional membrane proteins in that they rely on a complex glycolipid, GPI, rather than a hydrophobic transmembrane sequence for their association with membranes. GPI anchors are found on a variety of functionally diverse proteins (as well as glycoconjugates) including cell-surface receptors (folate receptor, CD14), cell adhesion molecules (neural cell adhesion molecule isoforms and carcinoembryonic antigen variants), cell surface hydrolases (5'-nucleotidase, acetylcholinesterase), complement regulatory proteins (decay accelerating factor), and protozoal surface molecules (Trypanosoma brucei variant surface glycoprotein, Leishmania lipophosphoglycan). Along with serving to attach proteins to the cell surface, GPI-anchored proteins appear to be markers and major constituents of detergent-resistant lipid rafts, the sphingolipid- and sterol-rich domains in membranes that are postulated to play an important role in the activation of signaling cascades.
CITATION STYLE
Menon, A. K. (2013). Glycosylphosphatidylinositol Anchors. In Encyclopedia of Biological Chemistry: Second Edition (pp. 476–478). Elsevier Inc. https://doi.org/10.1016/B978-0-12-378630-2.00211-5
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