title: Chemical and genetic probes for analysis of protein palmitoylation.
abstract: Reversible protein palmitoylation is one of the most important posttranslational modifications that has been implicated in the regulation of protein signaling, trafficking, localizing and enzymatic activities in cells and tissues. In order to achieve a precise understanding of mechanisms and functions of protein palmitoylation as well as its roles in physiological processes and disease progression, it is necessary to develop techniques that can qualitatively and quantitatively monitor the dynamic protein palmitoylation in vivo and in vitro. This review will highlight recent advances in both chemical and genetic encoded probes that have been developed for accurate analysis of protein palmitoylation, including identification and quantification of acyl moieties and palmitoylated proteins, localization of amino acid residues on which acyl moieties are attached, and imaging of cellular distributions of palmitoylated proteins. The role of major techniques of fluorescence microscopy and mass spectrometry in facilitating the analysis of protein palmitoylation will also be explored.
authors.affiliation: Key Laboratory of Pesticides and Chemical Biology, Ministry of Education, College of Chemistry, Central China Normal University, Wuhan, Hubei 430079, PR China.
authors.forename: Lun
authors.initials: L
authors.lastname: Li
authors.forename: Linjie
authors.initials: L
authors.lastname: Dong
authors.forename: Lisha
authors.initials: L
authors.lastname: Xia
authors.forename: Tingting
authors.initials: T
authors.lastname: Li
authors.forename: Hongying
authors.initials: H
authors.lastname: Zhong
mesh_terms: D000818:Animals; D036681:Fluorescence Recovery After Photobleaching / Q000379:methods*; D008401:Gas Chromatography-Mass Spectrometry / Q000379:methods*; D006801:Humans; D054878:Lipoylation; D011506:Proteins / Q000737:chemistry*; D040901:Proteomics / Q000379:methods*
chemical_list: D011506:Proteins