S-Acylation is a widespread post-translational modification of cellular proteins involving the attachment of fatty acyl chains onto cysteine residues.

This project aims to understand the molecular mechanisms that control how S-acylation enzymes recognise their substrates. These lipid-modifying proteins play important roles in regulating the membrane localisation, stability, and signalling activity of many cellular proteins, but the basis of their specificity is still not well defined.

By identifying the structural and biochemical features that guide substrate selection, we will clarify how particular proteins are chosen for modification. This knowledge will provide a clearer framework for understanding how S-acylation is regulated in normal cells and how it becomes disrupted in disease.