Protein Geranylgeranyltransferase Type 1 as a Target in Cancer

Author(s): Nisar Ullah, Muhammad Mansha, Patrick J. Casey

Journal Name: Current Cancer Drug Targets

Volume 16 , Issue 7 , 2016

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The process of protein prenylation involves the covalent linkage of either farnesyl (15-carbon) or geranylgeranyl (20-carbon) isoprenoid lipds to conserved cysteine residues in the carboxyl-terminus of proteins. Protein geranylgeranyltransferase I (GGTase-I) is the enzyme that catalyzes the addition of the geranylgeranyl moiety from geranylgeranyl pyrophosphate to the target protein, which contains a Cterminal consensus sequence termed a CaaX motif. Geranylgeranylation is important to the function of a number of proteins, including the majority of Rho GTPases, G protein gamma subunits, and several other regulatory proteins. Studies over the past two decades have revealed that many of these proteins contribute to tumor development and metastasis. Blocking Rho GTPase activity through inhibition of GGTase-I in particular has been advanced as a potential strategy for disease therapy. This review will provide an overview of the CaaX prenyltransferases, the rationale for targeting GGTase-I in cancer in particular, and the current status of GGTase-I inhibitor (GGTI) development.

Keywords: Prenylation, isoprenylation, isoprenoid, CaaX protein, GGTI, FTI, geranylgeranyl, farnesyl.

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Article Details

Year: 2016
Page: [563 - 571]
Pages: 9
DOI: 10.2174/1568009616666151203224603
Price: $65

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