palmitoylation

thumb|300px|right|In palmitoylation, a palmitoyl group (derived from palmitic acid, pictured above) is added. thumb|Palmitoylation of a cysteine residue thumb|Left Palmitoylation (red) anchors Ankyrin G to the plasma membrane. Right Close up. Palmityl residue in yellow. thumb|Palmitoylation of Gephyrin Controls Receptor Clustering and Plasticity of GABAergic Synapses

In molecular biology, palmitoylation is the covalent attachment of fatty acids, such as palmitic acid, to cysteine (S-palmitoylation) and less frequently to serine and threonine (O-palmitoylation) residues of proteins, which are typically membrane proteins. The precise function of palmitoylation depends on the particular protein being considered. Palmitoylation enhances the hydrophobicity of proteins and contributes to their membrane association. Palmitoylation also appears to play a significant role in subcellular trafficking of proteins between membrane compartments, as well as in modulating protein–protein interactions.