...Piers A. Hemsley S-acylation is a common yet poorly understood fatty acid-based post-translational modification of proteins in all eukaryotes, including plants. While exact roles for S-acylation in protein function are largely unknown the reversibility of S-acylation indicates that it is likely...

...Mitra S. Rana; Chul-Jin Lee; Anirban Banerjee Protein S-acylation is a reversible lipidic posttranslational modification where a fatty acid chain is covalently linked to cysteine residues by a thioester linkage. A family of integral membrane enzymes known as DHHC protein acyltransferases (DHHC-PATs...

...Kimon Lemonidis; Christine Salaun; Marianna Kouskou; Cinta Diez-Ardanuy; Luke H. Chamberlain; Jennifer Greaves S-acylation is a reversible lipid modification occurring on cysteine residues mediated by a family of membrane-bound ‘zDHHC’ enzymes. S-acylation predominantly results in anchoring...

...Kimon Lemonidis; Martin W. Werno; Jennifer Greaves; Cinta Diez-Ardanuy; Maria C. Sanchez-Perez; Christine Salaun; David M. Thomson; Luke H. Chamberlain The discovery of the zDHHC family of S-acyltransferase enzymes has been one of the major breakthroughs in the S-acylation field. Now, more than...

...Jennifer Greaves; Luke H. Chamberlain A family of 23 DHHC (Asp-His-His-Cys) proteins that function as mammalian S-acyltransferases has been identified, reinvigorating the study of protein S-acylation. Recent studies have continued to reveal how S-acylation affects target proteins, and have provided...