Site-specific chemical fatty-acylation for gain-of-function analysis of protein <i>S</i>-palmitoylation in live cells
Yumeng Li, Shushu Wang, Yanchi Chen, Manjia Li, Xiaoshu Dong, Howard C. Hang, Tao Peng
Abstract
Protein S-palmitoylation, or S-fatty-acylation, regulates many fundamental cellular processes in eukaryotes. Herein, we present a chemical fatty-acylation approach that involves site-specific incorporation of cycloalkyne-containing unnatural amino acids and subsequent bioorthogonal reactions with fatty-acyl tetrazines to install fatty-acylation mimics at target protein sites, allowing gain-of-function analysis of S-palmitoylation in live cells.
Topics & Concepts
PalmitoylationAcylationBioorthogonal chemistryChemistryMyristoylationFatty acidFunction (biology)BiochemistryProtein functionCombinatorial chemistryBiologyCell biologyCysteineEnzymeClick chemistryGeneCatalysisPhosphorylationClick Chemistry and ApplicationsChemical Synthesis and AnalysisPeptidase Inhibition and Analysis