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Biochim Biophys Acta. 2008 Mar;1780(3):410-20. Epub 2007 Aug 25.

Lipid remodeling of GPI-anchored proteins and its function.

Author information

1
Research Institute for Cell Engineering, National Institute of Advanced Industrial Science and Technology, Tsukuba, Ibaraki 305-8566, Japan.

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.

PMID:
17913366
DOI:
10.1016/j.bbagen.2007.08.009
[Indexed for MEDLINE]

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