Abstract
The posttranslational modification of proteins by the covalent attachment of farnesyl and geranylgeranyl groups to cysteine residues at or near the C-terminus via a thioether bond is now well established in mammalian cells (1–6). Most isoprenylated proteins are thought to serve as regulators of cell signaling and membrane trafficking. Farnesylation and geranylgeranylation of the cysteinyl residues have been shown to promote both protein-protein and protein-membrane interactions (6–8). Isoprenylation, and, in some cases, the subsequent palmitoylation, provide a mechanism for the membrane association of polypeptides, which lack a transmembrane domain, and appear to be prerequisite for their in vivo activity (6,9,10).
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Andres, D.A., Crick, D.C., Finlin, B.S., Waechter, C.J. (1998). Rapid Identification of Cysteine-Linked Isoprenyl Groups by Metabolic Labeling with [3H]Farnesol and [3H]Geranylgeraniol. In: Gelb, M.H. (eds) Protein Lipidation Protocols. Methods in Molecular Biology, vol 116. Humana Press. https://doi.org/10.1385/1-59259-264-3:107
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DOI: https://doi.org/10.1385/1-59259-264-3:107
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