Abstract
Posttranslational prenylation of proteins in mammalian cells involves the formation of a thioether linkage between a 15-carbon farnesyl or a 20-carbon geranylgeranyl moiety and one or more cysteine residues, at or near the carboxyl terminus of the polypeptide. The prenyl groups are donated by farnesyl pyrophosphate or geranylgeranyl pyrophosphate, which, in turn, are derived from a common precursor, mevalonate (1,2). Prenylation ranks among the most common lipid modifications of proteins in mammalian cells, with one estimate suggesting that 2% (by mass) of all cellular proteins may be modified in this way (3). A few of the known farnesylated or geranylgeranylated proteins include nuclear lamin B (4), H-, and K-Ras proteins (5,6), the γ-subunits of heterotrimeric G proteins (7,8), and Ras-related GTP-binding proteins belonging to the Rac (9), Rap (2,10), Ral (9), Rho (11,12), and Rab (13–15) families. The characterization of several protein:prenyltransferases (16–19) has led to rapid advances in knowledge concerning the enzymology of protein prenylation. However, much remains to be learned about the significance of the prenyl modification for the function of individual proteins in living cells.
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Overmeyer, J.H., Erdman, R.A., Maltese, W.A. (1998). Membrane Targeting via Protein Prenylation. In: Clegg, R.A. (eds) Protein Targeting Protocols. Methods in Molecular Biology™, vol 88. Humana Press. https://doi.org/10.1385/0-89603-487-9:249
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DOI: https://doi.org/10.1385/0-89603-487-9:249
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