Abstract

Lipid modification of protein refers to the covalent attachment of lipid such as fatty acid, isoprenoid or phospholipid to protein. Protein acylation, protein prenylation and glycosylphosphatidylinositol anchor (GPI-anchor) are known as the three major lipid modifications found in the cellular proteins. The lipid-modified proteins exert their respective physiological functions by specific membrane-protein interaction and/or protein-protein interaction mediated by the lipid moiety of the protein. Because of the lack of systematic analytical methods to detect lipid modification of protein, the number of protein found to be modified with lipid is far less than the expected number. In this review, we provide a brief summary of our recent approach to establish systematic strategy to analyze lipid modification of protein by using metabolic labeling of protein. In this strategy, using cDNA as a starting material, the susceptibility of the protein to lipid modification was evaluated by metabolic labeling in an in vitro translation system or in transfected cells.

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