Assaying Protein S-Acylation in Plants

S-acylation is increasingly being recognized as an important posttranslational modification of proteins controlling activity, subcellular localization, microdomain residence, and stability. Heterotrimeric G-proteins and GPCRs are particularly well studied S-acylated proteins, and fast, cheap, reliable methods are required for the analysis of S-acylation states of these proteins. Various approaches have been developed to study S-acylation, but they are time consuming, expensive, frequently require radiolabels and generally only suitable for cell culture, making them impractical for work in plant systems. Here a rapid and inexpensive method is described for the analysis of the S-acylation state of AGG2 that can be performed on any cell or tissue sample using standard laboratory equipment and methods. This method is also applicable to any protein that can be detected by western blotting.