S-palmitoylation and the regulation of NCX1

Investigations into reversible cysteine acylation (S-palmitoylation) have enjoyed a renaissance recently, thanks to numerous techniques that have improved the sensitivity of detection above the traditional use of 3H-palmitate. Often considered a largely static modifi-cation necessary only for traffic of membrane proteins through the secretory pathway, an appreciation is now growing that S-almitoylation dynamically regulates the landscape of the cell surface in unexpected ways, including the formation and endocytosis of protein/lipid domains, as well as directly modulating ion channel and transporter function.