Getting stuck in: protein palmitoylation in Plasmodium

Abstract

Palmitoylation is the reversible post-translational addition of a lipid moiety to cysteine residues on targeted proteins. The recent use of proteomic-scale techniques to study protein palmitoylation in multiple organisms has radically changed our understanding of the diversity of proteins and signaling pathways that are affected by palmitoylation. These experiments have made clear that, similarly to phosphorylation, palmitoylation is a regulatory tool that has an impact upon a wide range of essential eukaryotic processes. A recent proteome-level analysis of protein palmitoylation in Plasmodium has revealed the importance of palmitoylation in parasite biology and has raised new and exciting questions about several Plasmodium-specific and virulence-associated processes.