Which lipid modification can be reversed by palmitoyl-protein thioesterase?
Palmitoylation also called S-acylation refers to attachment of 16-carbon saturated palmitate from palmitoyl-CoA to cysteine thiol via thioester bond catalyzed by membrane-bound DHHC motif palmitoyl acyltransferases containing Asp-His-His-Cys catalytic tetrad. Unlike myristoylation or prenylation irreversible thioether amide linkages, thioester is chemically labile and enzymatically reversible, providing dynamic regulation. Removal catalyzed by acyl protein thioesterases APT1 and APT2 and ABHD17 family depalmitoylases in cytosol and lysosomal palmitoyl-protein thioesterase PPT1 involved in Niem
Ref: Linder & Deschenes, Nat Rev Mol Cell Biol 2007, Palmitoylation regulation; Chamberlain & Shipston, Physiol Rev 2015.