In vivo prenylation analysis of ras and rho proteins

RhoC-GTPase is a Novel Tissue Biomarker Associated with Biologically Aggressive Carcinomas of the Breast

“…Rho proteins are prenylated in order to exert their functions and to localize appropriately to the sub cytoplasmic membrane space [30][31][32][33][34]. Prenylation can be inhibited by farnesyl transferase inhibitors (FTIs) and FTIs are effective in modulating tumor growth in ras-transformed tumor cells [35][36][37][38][39].…”

Rho-Regulatory Proteins in Breast Cancer Cell Motility and Invasion

“…Like Ras, the Rho GTPases are post-translationally modified to locate them to their distinct cell compartment so they can carry out their specific function [25,84,85]. Each Rho protein contains a C-terminal CAAX domain that determines prenylation and polybasic residues in the hypervariable domain, upstream of the CAAX domain, which dictate proper membrane localization [85].…”

Dominant negative α-subunit of farnesyl- and geranylgeranyl-transferase I inhibits insulin-induced differentiation of 3T3-L1 pre-adipocytes

“…6,7 However, it has been shown that inhibition of FTase can result in geranylgeranylation of some Ras proteins. 35 Thus, using the DN FTase=GGTase I a-subunit to block both FTase and GGTase I protein activity, would prevent prenylation of Ras proteins via an alternate path. Additionally, because FTase and GGTase I share the same a-subunit, intracellular expression of a dominant negative FTase= GGTase I a-subunit would then moderate or ablate the function of both of these two prenyltransferases thereby effecting decreases in the amounts of prenylated p21Ras and RhoA.…”