Abstract
Lipid modifications of proteins are widespread and functionally important in eukaryotic cells. Intracellular proteins such as the signal-transducing heterotrimeric GTP-binding proteins (G proteins) and the Ras superfamily of G proteins are modified by 14- or 16-carbon fatty acids and/or 15- or 20-carbon isoprenoids. Numerous cell surface glycoproteins such as acetylcholinesterase and the folate receptor are modified at their C-terminus by a structurally complex glycosylphosphatidylinositol (GPI) anchor. Even some secreted protein ligands are lipid modified: the morphogen Hedgehog has a covalently attached cholesterol moiety at its C-terminus and an amide-linked C16 fatty acid at its N-terminus. In most cases, the lipid moiety is crucial to protein function as it can regulate the interaction of an otherwise water-soluble protein with membranes. In some instances, the covalent lipid acts as a functional switch resulting in membrane association of certain protein conformations but not of others. The lipid moiety also aids in the sorting of the protein to membrane domains that promote lateral and transbilayer protein-protein interactions that are critical for cell function.
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