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

Alkynyl-farnesol reporters for detection of protein S-prenylation in cells.
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DOI:
10.1039/c0mb00183j
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发表时间:
2011-01
影响因子:
--
通讯作者:
Hang HC
Hang HC
中科院分区:
生物3区
文献类型:
--
作者:
Charron G;Tsou LK;Maguire W;Yount JS;Hang HC

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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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