Journal
MOLECULAR BIOSYSTEMS
Volume 7, Issue 1, Pages 67-73Publisher
ROYAL SOC CHEMISTRY
DOI: 10.1039/c0mb00183j
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Funding
- Cancer Research Institute
- Ellison Medical Foundation
- NIH/NIGMS [1R01 GM087544-01A2]
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [T32GM007739, R01GM087544] Funding Source: NIH RePORTER
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Protein S-prenylation is a lipid modification that regulates membrane-protein and protein-protein interactions in cell signaling. Though sites of protein S-prenylation can be predicted based upon conserved C-terminal CaaX or CC/CXC motifs, biochemical detection of protein S-prenylation in cells is still challenging. Herein, we report an alkynyl-isoprenol chemical reporter (alk-FOH) as an efficient substrate for prenyltransferases in mammalian cells that enables sensitive detection of S-farnesylated and S-geranylgeranylated proteins using bioorthogonal ligation methods. Fluorescent detection alleviates the need to deplete cellular isoprenoids for biochemical analysis of S-prenylated proteins and enables robust characterization of S-prenylated proteins, such as effectors that are injected into host cells by bacterial pathogens. This alkynyl-prenylation reporter provides a sensitive tool for biochemical analysis and rapid profiling of prenylated proteins in cells.
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