Peng, Tao Hang, Howard C. Bifunctional Fatty Acid Chemical Reporter for Analyzing S‑Palmitoylated Membrane Protein–Protein Interactions in Mammalian Cells Studying the functions of S-palmitoylated proteins in cells can be challenging due to the membrane targeting property and dynamic nature of protein S-palmitoylation. New strategies are therefore needed to specifically capture S-palmitoylated protein complexes in cellular membranes for dissecting their functions <i>in vivo</i>. Here we present a bifunctional fatty acid chemical reporter, x-alk-16, which contains an alkyne and a diazirine, for metabolic labeling of S-palmitoylated proteins and photo-cross-linking of their involved protein complexes in mammalian cells. We demonstrate that x-alk-16 can be metabolically incorporated into known S-palmitoylated proteins such as H-Ras and IFITM3, a potent antiviral protein, and induce covalent cross-linking of IFITM3 oligomerization as well as its specific interactions with other membrane proteins upon in-cell photoactivation. Moreover, integration of x-alk-16-induced photo-cross-linking with label-free quantitative proteomics allows identification of new IFITM3 interacting proteins. membrane proteins;IFITM 3;New strategies;protein complexes;acid chemical reporter;IFITM 3 oligomerization;Bifunctional Fatty;Chemical Reporter;Mammalian CellsStudying 2015-01-21
    https://acs.figshare.com/articles/dataset/Bifunctional_Fatty_Acid_Chemical_Reporter_for_Analyzing_S_Palmitoylated_Membrane_Protein_Protein_Interactions_in_Mammalian_Cells/2213836
10.1021/ja502109n.s003