Journal
NATURE METHODS
Volume 6, Issue 2, Pages 135-138Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/NMETH.1293
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- Skaggs Institute for Chemical Biology [F32NS060559, CA087660]
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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 similar to 125 predicted palmitoylated proteins, including G proteins, receptors and a family of uncharacterized hydrolases whose plasma membrane localization depends on palmitoylation.
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