title: Protein lipidation.
abstract: Proteins are covalently modified with a variety of lipids, including fatty acids, isoprenoids, and cholesterol. Lipid modifications play important roles in the localization and function of proteins. The focus of this review is S-palmitoylation, the reversible addition of palmitate and other long-chain fatty acids to proteins at cysteine residues in a variety of sequence contexts. The functional consequences of palmitoylation are diverse. Palmitoylation facilitates the association of proteins with membranes, mediates protein trafficking, and more recently has been appreciated as a regulator of protein stability. Members of a family of integral membrane proteins that harbor a DHHC cysteine-rich domain mediate most cellular palmitoylation events. Here we focus on DHHC proteins that modify Ras proteins in yeast and mammalian cells.
authors: Department of Cell Biology and Physiology, Washington University School of Medicine, St Louis, MO, USA.
authors: Marissa J
authors: MJ
authors: Nadolski
authors: Maurine E
authors: ME
authors: Linder
mesh_terms: D000217:Acyltransferases / Q000378:metabolism* / Q000502:physiology; D000818:Animals; D000077614:Golgi Matrix Proteins; D006801:Humans; D054878:Lipoylation; D008565:Membrane Proteins / Q000378:metabolism*; D019308:Palmitic Acid / Q000378:metabolism*
chemical_list: C480862:GOLGA7 protein, human; D000077614:Golgi Matrix Proteins; D008565:Membrane Proteins; D019308:Palmitic Acid; D000217:Acyltransferases; C504825:ZDHHC9 protein, human