Abstract
The ras oncogene protein, called Ras or p21, has served as a model system for the characterization of the small (ca. 20kDa) GTPases. Among the early biochemical discoveries of Ras was the observation that this oncogene-encoded protein underwent posttranslational processing events which preceded the localization of Ras in the plasma membrane. The first specific modification identified was palmitoylation of a Cys residue somewhere near the C terminus of Ras. However, the full number and chemical nature of the modifications was not fully appreciated until recently. The steps of Ras processing (farnesylation, proteolysis, carboxyl methylation, and palmitoylation) have been reviewed extensively (for examples, see Der and Cox 1991; Gibbs 1991; Sinensky and Litz 1992), and a summary of these steps is shown in Table 1. These modifications occur in a C-terminal region that has acquired the acronym CaaX box (C, Cys; a, a usually aliphatic amino acid; X, another amino acid).
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Gibbs, J.B. (1993). Lipid Modifications of Proteins in the Ras Superfamily. In: Dickey, B.F., Birnbaumer, L. (eds) GTPases in Biology I. Handbook of Experimental Pharmacology, vol 108 / 1. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-78267-1_22
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DOI: https://doi.org/10.1007/978-3-642-78267-1_22
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