Protein Prenyltransferases

Supporting information

Protein prenyltransferases are enzymes that transfer isoprenoid lipids (such as farnesyl or geranylgeranyl groups) to acceptor molecules. The attachment of these groups is known as prenylation. Farnesyltransferase (FTase) and geranylgeranyltransferase type 1 (GGTase 1) catalyze this modification, which takes place at a conserved cysteine residue in a CaaX motif in the protein substrate (in which 'C' is cysteine, 'a' is an aliphatic amino acid, and 'X' is variable). The attachment of a farnesyl group or a geranyl group permits membrane localization of proteins lacking a transmembrane domain, and occurs post-translationally.

FTase and GGTase 1 are heterodimeric enzymes that share a common α-subunit and different β-subunits. Target proteins include Ras, which is suggestive of a role for prenylation in tumor development. Ras requires farnesylation for malignant activity, and many of the downstream proteins it targets are also subject to farnesylation or geranylgeranylation in order to mediate the growth, survival and migration of tumor cells. Prenyltransferase inhibitors are therefore of interest in the development of cancer therapeutics. Farnesyltransferase inhibitors (FTIs) exhibit antitumor effects by inducing apoptosis and cell cycle arrest, and inhibiting cell proliferation, migration and angiogenesis. Geranylgeranyltransferase type 1 inhibitors (GGTIs) also induce apoptosis and inhibit the growth of tumor cells.

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Gene Species Gene Symbol Gene Accession No. Protein Accession No.
Farnesyl-transferase (α subunit) Human FNTA NM_002027 P49354
Mouse Fnta NM_008033 Q61239
Rat Fnta NM_012847 Q04631
Farnesyl-transferase (β subunit) Human FNTB NM_002028   P49356
Mouse Fntb NM_145927 Q8K2I1
Rat Fntb NM_172034 Q02293
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Literature for Protein Prenyltransferases

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