The intracellular dynamic of protein palmitoylation

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

Cellular proteins undergo a vast array of dynamic and static modifications to their amino acid backbone, which can dramatically extend and regulate functional output. Some of these modifications, phosphorylation in particular, have been the subject of intensive research, and their regulation and intracellular functions are extensively characterized. In contrast, our understanding of S-palmitoylation (hereafter referred to as palmitoylation), the attachment of palmitate (C16:0) or other long chain fatty acids to cysteine residues, has lagged behind some of its more popular cousins. Indeed, enzymes that catalyze palmitoylation reactions have only recently been identified after landmark studies in yeast, settling a long-running debate as to whether this process was predominantly enzyme mediated or spontaneous (Lobo et al., 2002; Roth et al., 2002; Fukata et al., 2004; Keller et al., 2004) .