... environment of protein interactions. Among these modifications, S-acylation has emerged as a key regulator of various cellular processes, including different forms of cell death. In this mini-review, we highlight the role of S-acylation in apoptosis and its emerging contributions to necroptosis and pyroptosis...

... modification (PTM) have been identified that are added to NLRP3 to regulate its activity. Recent progress has revealed that NLRP3 is subject to a further type of PTM, S-acylation (or palmitoylation), which involves the reversible addition of long-chain fatty acids to target cysteine residues by opposing sets...

...Dale D.O. Martin; Shaun S. Sanders Protein mislocalization is a key initial step in neurodegeneration, regardless of etiology, and has been linked to changes in the dynamic addition of saturated fatty acids to proteins, a process known as S -acylation. With the advent of new techniques to study S...

... a transformative agreement with UM. cardiomyocyte exocytosis intracellular signaling palmitoylation S-acylation trafficking Cysteine palmitoylation or S-acylation is the reversible attachment of saturated fatty acids onto protein cysteine thiols that functions as a critical regulatory mechanism...

... and cell death. S-acylation, a lipid post-translational modification, is emerging as a critical regulator of several important Ca 2+ -handling proteins. S-acylation is a reversible and dynamic process involving the attachment of long-chain fatty acids (most commonly palmitate) to cysteine residues...

...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...