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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. [2] The precise function of palmitoylation depends on the particular protein being ...
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The protein palmitoylation is a reversible process. The addition of palmitoyl group increase the membrane association of the substrate protein while the removal by palmitoyl thioesterase decreases the membrane association.
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Some members of the family such as ZDHHC3 and ZDHHC7 enhance palmitoylation of proteins such as PSD-95, SNAP-25, GAP43, Gαs. Others such as ZDHHC9 showed specificity only toward the H-Ras protein. [3] However, a recent study questions the involvement of classical enzyme-substrate recognition and specificity in the palmitoylation reaction. [4]
One function is thought to cluster proteins to increase the efficiency of protein-protein interactions and facilitate biological processes. In the opposite scenario palmitate mediated localization sequesters proteins away from a non-localized molecule.
S-Acylation is the process of chemically linking a molecule to another molecule via a thioester bond. [1] Protein S-acylation is a sub-type of S-acylation where the first of those molecules is a protein, and connected to the second through a cysteine amino acid. [1]
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