title: Understanding Protein Palmitoylation: Biological Significance and Enzymology.
abstract: Protein palmitoylation is a widespread lipid modification in which one or more cysteine thiols on a substrate protein are modified to form a thioester with a palmitoyl group. This lipid modification is readily reversible; a feature of protein palmitoylation that allows for rapid regulation of the function of many cellular proteins. Mutations in palmitoyltransferases (PATs), the enzymes that catalyze the formation of this modification, are associated with a number of neurological diseases and cancer progression. This review summarizes the crucial role of palmitoylation in biological systems, the discovery of the DHHC protein family that catalyzes protein palmitoylation, and the development of methods for investigating the catalytic mechanism of PATs.
authors.affiliation: Departments of Chemistry and Biological Chemistry, University of Michigan, 930 N University, Ann Arbor, MI 48109-1055, USA.
authors.forename: Xiaomu
authors.initials: X
authors.lastname: Guan
authors.affiliation: Departments of Chemistry and Biological Chemistry, University of Michigan, 930 N University, Ann Arbor, MI 48109-1055, USA.
authors.forename: Carol A
authors.initials: CA
authors.lastname: Fierke
keywords: DHHC protein family; catalytic mechanism; palmitoylation assay; palmitoyltransferase (PAT); protein palmitoylation