FEBS J. 2007 Oct;274(20):5202-10. Epub 2007 Sep 24.

Protein lipidation.

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Department of Cell Biology and Physiology, Washington University School of Medicine, St Louis, MO, USA.

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.

PMID:: 17892486; [PubMed - indexed for MEDLINE]

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