S-Acylation and the control of ion channel physiology’

Protein S-acylation, the only fully reversible post-translational lipid modification of proteins, is emerging as a ubiquitous mechanism to control the properties and function of a diverse array of proteins and consequently physiological processes. S-acylation results from the enzymatic addition of long chain lipids, most typically palmitate, onto intracellular cysteine residues of soluble and transmembrane proteins via a labile thioester linkage. Ion channels represent a major class of proteins in which S-acylation can control assembly, maturation, trafficking, and regulation by other post-translational modifications. In this talk, I will discuss some of our recent work interrogating the role of S-acylation in controlling the functional diversity of calcium- and voltage- activated potassium (BK) channels in health & disease and discuss some of the major challenges and opportunities in this rapidly expanding field.
For recent review of field see: Chamberlain & Shipston (2015) Physiological Reviews 95:341-376