title: Protein S-palmitoylation in cellular differentiation.
abstract: Reversible protein S-palmitoylation confers spatiotemporal control of protein function by modulating protein stability, trafficking and activity, as well as protein-protein and membrane-protein associations. Enabled by technological advances, global studies revealed S-palmitoylation to be an important and pervasive posttranslational modification in eukaryotes with the potential to coordinate diverse biological processes as cells transition from one state to another. Here, we review the strategies and tools to analyzein vivoprotein palmitoylation and interrogate the functions of the enzymes that put on and take off palmitate from proteins. We also highlight palmitoyl proteins and palmitoylation-related enzymes that are associated with cellular differentiation and/or tissue development in yeasts, protozoa, mammals, plants and other model eukaryotes.
authors.affiliation: Metabolic Engineering Research Laboratory, Science and Engineering Institutes, Agency for Science, Technology and Research, Singapore.
authors.forename: Mingzi M
authors.initials: MM
authors.lastname: Zhang
authors.affiliation: Laboratory of Chemical Biology and Microbial Pathogenesis, The Rockefeller University, New York, NY, U.S.A. hhang@rockefeller.edu.
authors.forename: Howard C
authors.initials: HC
authors.lastname: Hang
mesh_terms: D000818:Animals; D002454:Cell Differentiation; D002623:Chemistry Techniques, Analytical / Q000379:methods; D003545:Cysteine / Q000378:metabolism*; D006801:Humans; D054878:Lipoylation; D010168:Palmitates / Q000378:metabolism*; D011499:Protein Processing, Post-Translational; D055550:Protein Stability; D015398:Signal Transduction
chemical_list: D010168:Palmitates; D003545:Cysteine
keywords: S-palmitoylation; cellular differentiation; fatty-acylation; lipidation; posttranslational modification