Meeting background

Post-translational modifications play a major role in controlling protein function. Palmitoylation, which generally involves the attachment of palmitic acid groups onto cysteine residues, has emerged as a dynamic and versatile protein regulator. This modification impacts protein trafficking, membrane micro-localisation, protein-protein interactions, and protein stability. A diverse array of proteins are modified by palmitoylation, including neurotransmitter receptors, ion channels, G proteins and G protein-coupled receptors, kinases, secreted signalling proteins and a variety of other signalling molecules. The study of palmitoylation is rapidly advancing, driven by key methodological developments, proteomic profiling of the cellular palmitoylome, and the identification of two families of palmitoylating enzymes: the large ‘DHHC’ family and the ‘MBOAT’ family. This meeting will bring together leading scientists in the field to highlight the most recent breakthroughs in palmitoylation research.