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Structural remodeling of GPI anchors during biosynthesis and after attachment to proteins
Author(s) -
Fujita Morihisa,
Kinoshita Taroh
Publication year - 2010
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2009.10.079
Subject(s) - lipid microdomain , microbiology and biotechnology , glycan , biosynthesis , membrane protein , biology , yeast , biochemistry , chemistry , gene , glycoprotein , membrane
Glycosylphosphatidylinositol (GPI) anchoring of proteins is a conserved post‐translational modification in eukaryotes. In mammalian cells, approximately 150 proteins on the plasma membrane are attached to the cell surface by GPI anchors, which confer specific properties on proteins, such as association with membrane microdomains. The structures of lipid and glycan moieties on GPI anchors are remodeled during biosynthesis and after attachment to proteins. The remodeling processes are critical for transport and microdomain‐association of GPI‐anchored proteins. Here, we describe the structural remodeling of GPI anchors and genes required for the processes in mammals, yeast, and trypanosomes.