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Determination of glycosyl‐phosphatidylinositol membrane protein anchorage
Author(s) -
Hooper Nigel M.
Publication year - 2001
Publication title -
proteomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/1615-9861(200106)1:6<748::aid-prot748>3.0.co;2-t
Subject(s) - lipid raft , phosphatidylinositol , biochemistry , membrane protein , membrane , phospholipase , chemistry , raft , glycan , biology , signal transduction , enzyme , glycoprotein , organic chemistry , copolymer , polymer
A diverse range of proteins are modified by the post‐translational covalent attachment of a glycosyl‐phosphatidylinositol (GPI) membrane anchor. Hydropathy plots and other computer algorithms can be used to predict the presence of a GPI anchor attachment signal in the nascent polypeptide chain. However, the presence of a GPI anchor on the mature protein requires experimental evidence, including sensitivity of the protein to release from cells or membranes with bacterial phosphatidylinositol‐specific phospholipase C, recognition by anti‐cross‐reacting determinant antibodies, or metabolic labelling with components of the anchor. GPI‐anchored proteins are resistant to solubilisation with detergents such as Triton X‐100 due to their association with cholesterol and glycosphingolipids in membrane domains known as lipid rafts. This detergent insolubility can be used to provide evidence for the presence of a GPI anchor on a protein and to isolate lipid rafts.