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- W2068034774 abstract "Covalent attachment of palmitate to proteins is a post-translational modification that exerts diverse effects on protein localization and function. The three key technical approaches required for an investigator to determine the role of palmitoylation of your favorite palmitoylated protein (YFPP) are methods to: (1) detect YFPP palmitoylation; (2) alter or inhibit palmitoylation of YFPP; (3) determine the functional significance of altered YFPP palmitoylation. Here, I describe experimental methods to address these three issues. Both radioactive (radiolabeling with [(3)H]palmitate or (125)I-IC16 palmitate) and non-radioactive (chemical labeling and mass spectrometry) methods to detect palmitoylated proteins are presented. Next, techniques to inhibit protein palmitoylation are described. These include site specific mutagenesis, and treatment of cells with inhibitors of protein palmitoylation, including 2-bromopalmitate, cerulenin, and tunicamycin. Alternative methods to replace palmitate with other fatty acids are also presented. Finally, general approaches to determining the effect of altered palmitoylation status on YFPP association with membranes and lipid rafts, as well as signal transduction, are described." @default.
- W2068034774 created "2016-06-24" @default.
- W2068034774 creator A5027044141 @default.
- W2068034774 date "2006-10-01" @default.
- W2068034774 modified "2023-09-26" @default.
- W2068034774 title "Use of analogs and inhibitors to study the functional significance of protein palmitoylation" @default.
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- W2068034774 doi "https://doi.org/10.1016/j.ymeth.2006.04.013" @default.
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