*10.2. Palmitoylation*

Palmitoylation is a common post-translational modification that occurs in the Golgi where palmitoyl transferases add a fatty acid, palmitate, to a cysteine residue via a thioester linkage [255]. Palmitoylation enhances the hydrophobicity of proteins and plays an important role in subcellular trafficking of proteins between membrane compartments [256]. Proteins can be readily palmitoylated, and the modification is typically reversible. Addition and removal of palmitate can play roles in protein and membrane regulation [256]. Palmitoylated proteins can be modified by either a single palmitoyl group, or dually modified with one or more palmitoyl groups and one or more prenyl or myristoyl groups. Palmitoylated proteins can be divided into four types, (1) single palmitoyl modifications, often at the end of a protein, (2) palmitoylation near a transmembrane domain, (3) dual palmitoylation and prenylation and (4) dual palmitoylation and myristylation [255]. Viral proteins may arrange on membranes in accordance to their palmitoylation status, and it affects assembly and localization of viral oligomers [257].
