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- W1996252412 endingPage "420" @default.
- W1996252412 startingPage "410" @default.
- W1996252412 abstract "Many proteins are attached to the cell surface via a conserved post-translational modification, the glycosylphosphatidylinositol (GPI) anchor. GPI-anchored proteins are functionally diverse, but one of their most striking features is their association with lipid microdomains, which consist mainly of sphingolipids and sterols. GPI-anchored proteins modulate various biological functions when they are incorporated into these specialized domains. The biosynthesis of GPI and its attachment to proteins occurs in the endoplasmic reticulum. The lipid moieties of GPI-anchored proteins are further modified during their transport to the cell surface, and these remodeling processes are essential for the association of proteins with lipid microdomains. Recently, several genes required for GPI lipid remodeling have been identified in yeast and mammalian cells. In this review, we describe the pathways for lipid remodeling of GPI-anchored proteins in yeast and mammalian cells, and discuss how lipid remodeling affects the association of GPI-anchored proteins with microdomains in cellular events." @default.
- W1996252412 created "2016-06-24" @default.
- W1996252412 creator A5057745536 @default.
- W1996252412 creator A5082485542 @default.
- W1996252412 date "2008-03-01" @default.
- W1996252412 modified "2023-09-26" @default.
- W1996252412 title "Lipid remodeling of GPI-anchored proteins and its function" @default.
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