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Issue 1, 2011
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Alkynyl-farnesol reporters for detection ofproteinS-prenylation in cells

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Abstract

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.

Graphical abstract: Alkynyl-farnesol reporters for detection of protein S-prenylation in cells

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Supplementary files

Article information


Submitted
01 Sep 2010
Accepted
10 Nov 2010
First published
25 Nov 2010

Mol. BioSyst., 2011,7, 67-73
Article type
Paper

Alkynyl-farnesol reporters for detection of protein S-prenylation in cells

G. Charron, L. K. Tsou, W. Maguire, J. S. Yount and H. C. Hang, Mol. BioSyst., 2011, 7, 67
DOI: 10.1039/C0MB00183J

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