The intracellular dynamic of protein palmitoylation

Salaun, Christine; Greaves, Jennifer; Chamberlain, Luke H.

Palmitoylation is one of a group of lipid modifications (collectively termed lipidation) that appears on eukaryotic proteins and includes the common N-myristoyl and isoprenyl modifications. N-myristoylation describes the addition of myristic acid (C14:0) to a glycine residue with an exposed NH 2 group after cleavage of the immediately adjacent initiating methionine (Zha et al., 2000; Resh, 2006a) . This process is predominantly cotranslational, mediated by soluble enzymes, and has a strict consensus sequence (MGXXXS/T). N-myristoylation can also occur posttranslationally, notably after caspase-mediated protein cleavage during programmed cell death (Zha et al., 2000) . Prenylation is a posttranslational process also catalyzed by soluble enzymes, involving the attachment of farnesyl or geranylgeranyl isoprenoids to a C-terminal cysteine present within a defined consensus sequence (Wright and Philips, 2006) .