Journal
FEBS JOURNAL
Volume 274, Issue 20, Pages 5202-5210Publisher
WILEY
DOI: 10.1111/j.1742-4658.2007.06056.x
Keywords
DHHC-CRD; fatty acylation; myristoylation; palmitoylation; prenylation; protein acyltransferase; protein lipidation; S-palmitoylation; Ras; ZDHHC
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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.
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