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Updated: Jan 24, 2026

Deacetylation Assays to Unravel the Interplay between Sirtuins SIRT2 and Specific Protein-substrates
Published on: February 27, 2016
Global Profiling of Sirtuin Deacylase Substrates Using a Chemical Proteomic Strategy and Validation by Fluorescent
Shuai Zhang1, Nicole A Spiegelman1, Hening Lin2
1Department of Chemistry and Chemical Biology, Cornell University, Ithaca, NY, USA.
Abstract:
Protein fatty-acylation is an important posttranslational modification (PTM) and has been associated with many fundamental biological processes. Sirtuins, the nicotinamide adenine dinucleotide (NAD)-dependent class of histone deacetylases have been reported to possess lysine defatty-acylase activity. Comprehensive substrate profiling of sirtuins will help to establish the function of both protein lysine fatty acylation and its regulation by sirtuins. Here, we describe a chemical proteomic strategy to globally profile sirtuin defatty-acylation substrates and a fluorescent labeling method to validate sirtuin substrates.
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