Deacylases —structure, function, and relationship to diseases

S-acylation is catalyzed by a group of acyltransferases, ZDHHCx, acting on various target proteins. The reverse reaction is mediated by protein acylases. The S-acylation-deacylation cycle controls the function of target proteins. Abnormal cycles can lead to various pathological conditions. Reversible S-acylation plays a pivotal role in various biological processes, modulating protein functions such as subcellular localization, protein stability/activity, and protein –protein interactions. These modifications are mediated by acyltransferases and deacylases, among which the most abundant modification is S-palmitoylation. Growing evidence has shown that this rivalrous pair of modifications, occurring in a reversible cycle, is essential for various biological fun ctions. Aberrations in this process have been associated with various diseases, including cancer, neurological disorders, and immune diseases. This underscores the importance of studying enzymes involved in acylation and deacylation to gain further insights into disease pathogenesis and provide nove l strategies for disease treatment. In this Review, we summarize our current understanding of the structure and physiological function of deacylases, highlighting their pivotal roles in pathology. Our aim is to provide insights for further clinical applications.
Source: FEBS Letters - Category: Biochemistry Authors: Tags: Review Source Type: research