Large-scale profiling of protein palmitoylation in mammalian cells.
S-palmitoylation is a pervasive post-translational modification required for the trafficking, compartmentalization and membrane tethering of many proteins. We demonstrate that the commercially available compound 17-octadecynoic acid (17-ODYA) can serve as a bioorthogonal, click chemistry probe for in situ labeling, identification and verification of palmitoylated proteins in human cells. We identified approximately 125 predicted palmitoylated proteins, including G proteins, receptors and a family of uncharacterized hydrolases whose plasma membrane localization depends on palmitoylation.
Martin
Brent R
BR
The Skaggs Institute of Chemical Biology and Department of Chemical Physiology, The Scripps Research Institute, 10550 N. Torrey Pines Road, La Jolla, California 92037, USA.
Cravatt
Benjamin F
BF
D005231:Fatty Acids, Unsaturated / Q000032:analysis / Q000378:metabolism*; D019204:GTP-Binding Proteins / Q000378:metabolism*; D006801:Humans; D019169:Jurkat Cells; D054878:Lipoylation; D011499:Protein Processing, Post-Translational; D040901:Proteomics / Q000379:methods*
D005231:Fatty Acids, Unsaturated; C047008:17-octadecynoic acid; D019204:GTP-Binding Proteins