S-palmitoylation

S-palmitoylation, in its most specific sense, refers to the process whereby a peptide is modified by the formation of a thioester linkage between palmitic acid and a cysteine moiety on the native chain. S-palmitoylation can also refer to the general process of protein acylation by fatty acids.

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Because S-palmitoylation is a dynamic, post-translational process, it is believed to be employed by the cell to alter the subcellular localization, protein-protein interactions, or binding capacities of a protein.

The palmitoylation cycles of a wide array of enzymes have been characterized in the past few years, including H-Ras, Gsα, the β2-adrenergic receptor, and endothelial nitric oxide synthase (eNOS).

References

Smotrys J and Linder A. (2004) "Palmitoylation of Intracellular Signaling Proteins: Regulation and Function". Annu Rev Biochem 73:559-87.

Resh, M. (2006) "Palmitoylation of Ligands, Receptors, and Intracellular Signaling Molecules". Sci STK. 359 October 31.

Linder M and Deschenes R. (2007) Palmitoylation: policing protein stability and traffic. Nature 8: 74-84.