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Sci. STKE, 31 October 2006
Vol. 2006, Issue 359, p. re14
[DOI: 10.1126/stke.3592006re14]

REVIEWS

Palmitoylation of Ligands, Receptors, and Intracellular Signaling Molecules

Marilyn D. Resh*

Cell Biology Program, Memorial Sloan-Kettering Cancer Center, 1275 York Avenue, Box 143, New York, NY 10021, USA.

Gloss: Many proteins contain covalently attached fatty acids. Two types of fatty acids can be linked to proteins: myristate, a 14-carbon fatty acid, or palmitate, a 16-carbon fatty acid. Some proteins contain both fatty acids. This Review focuses on the various ways that modification of proteins by palmitate regulates protein structure and function. Attachment of palmitate to intracellular signaling proteins can help target these proteins to specific membranes where their action is needed for signal transduction. Palmitoylation is often a dynamic reaction: Removal of the bound palmitate results in dissociation of the depalmitoylated protein from the membrane. Palmitate can also be attached to transmembrane proteins, which helps the modified proteins to traffic through the cell, to become enriched in specialized membrane domains (termed rafts), and to signal effectively. Surprisingly, even secreted proteins can be palmitoylated. In this case, palmitoylation modulates the ability of these proteins to signal close to and far away from the producing cell. Moreover, palmitoylation can regulate enzyme activity as well as protein-protein interactions. Thus, modification of ligands, receptors, and intracellular signaling proteins by palmitate has multiple effects on their localization and signaling functions.

*Corresponding author. E-mail, m-resh{at}ski.mskcc.org

Citation: M. D. Resh, Palmitoylation of Ligands, Receptors, and Intracellular Signaling Molecules. Sci. STKE 2006, re14 (2006).

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