A facile assay for zDHHC palmitoyl transferase activation elucidates effects of mutation and modification

• Published in: Journal of lipid research Vol. 66; no. 2; p. 100743
• Main Authors: Adachi, Naoko, Hess, Douglas T., Ueyama, Takehiko
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 01.02.2025; Elsevier
• Subjects: acyltransferase; Acyltransferases - genetics; Acyltransferases - metabolism; cancer mutations; cell signaling; Enzyme Activation; Enzyme Assays - methods; enzymology-enzyme regulation; fatty acyl-CoA; HEK293 Cells; Humans; lipid signaling; Lipoylation; Mutation; palmitoylation; Protein Processing, Post-Translational; tumor cell biology; zinc finger; acyl-CoA; cancer mutations; cell signaling; fatty acyl-CoA; tumor cell biology; zinc finger; enzymology-enzyme regulation; lipid signaling; palmitoylation; acyltransferase

At least 10% of proteins constituting the human proteome are subject to S-acylation by a long-chain fatty acid, thioesterified to a Cys thiol side chain. Fatty S-acylation (prototypically, S-palmitoylation) operates across eukaryotic phylogeny and cell type. S-palmitoylation is carried out in mammal...