In: Biochemical Society Symposia, 2007, vol. 74, p. 199-209
The mature sphingolipids of yeast consist of IPCs (inositolphosphorylceramides) and glycosylated derivatives thereof. Beyond being an abundant membrane constituent in the organelles of the secretory pathway, IPCs are also used to constitute the lipid moiety of the majority of GPI (glycosylphosphatidylinositol) proteins, while a minority of GPI proteins contain PI (phosphatidylinositol). Thus...
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In: Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids, 2007, vol. 1771, no. 3, p. 405-420
Like most other eukaryotes, Saccharomyces cerevisiae harbors a GPI anchoring machinery and uses it to attach proteins to membranes. While a few GPI proteins reside permanently at the plasma membrane, a majority of them gets further processed and is integrated into the cell wall by a covalent attachment to cell wall glucans. The GPI biosynthetic pathway is necessary for growth and survival...
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In: Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids, 2005, vol. 1735(1), p. 79
Homologues of Gpi8p, Gaa1p, Gpi16p, Gpi17p, and Cdc91p are essential components of the GPI transamidase complex that adds glycosylphosphatidylinositols (GPIs 1) to newly synthesized proteins in the ER. In mammalian cells, these five subunits remain stably associated with each other in detergent. In yeast, we find no stable stoichiometric association of Gpi17p with the Gpi8p–Gpi16p–Gaa1p core...
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