Palmitoylation has emerged as an important post translational modification regulating protein function, intracellular trafficking and protein-protein as well as protein-lipid interactions. In particular it has generated much interest in the cardiovascular research community since it has been shown to regulate the function of key proteins that contribute to normal Ca²⁺ cycling and therefore myocyte contraction, as well as G-protein coupled receptors, important modulators of myocardial contractility. 

Palmitoylation is the covalent attachment of a 16-carbon saturated fatty acid to a cysteine residue within a protein through the formation of a thioester or S-acyl bond.  The process is mediated by a set of enzymes referred to as palmitoyl acyl transferases (PATs) together with the fatty acid donor palmitoyl CoA. There are 24 PAT enzymes which are characterised by a canonical zinc binding motif Asp-His-His-Cys (zDHHC). Furthermore, over 8000 palmitoylated proteins have been identified (a database of these proteins can be found at http://swisspalm.epfl.ch/ ). Palmitoylation can be constitutive in some instances, but can also be dynamic and reversible, in a manner analogous to phosphorylation – the palmitate group being removed by the activity of acyl palmitoyl thioesterases (APTs).