Casey PJ, Seabra MC: Protein prenyltransferases. J Biol Chem. 1996, 271: 5289-5292. 10.1074/jbc.271.10.5289. A short minireview describing protein prenyltransferases, written before the structure was known. ArticleCASPubMed Google Scholar
AceView. Alignment of expressed sequence tags and mRNAs to the human genome, showing alternative splice forms., [http://www.humangenes.org]
Andres DA, Milatovich A, Ozcelik T, Wenzlau JM, Brown MS, Goldstein JL, Francke U: cDNA cloning of the two subunits of human CAAX farnesyltransferase and chromosomal mapping of FNTA and FNTB loci and related sequences. Genomics. 1993, 18: 105-112. 10.1006/geno.1993.1432. Cloning of human FNTA and FNTB; 'related sequences' refers to processed pseudogenes. ArticleCASPubMed Google Scholar
Dhawan P, Yang E, Kumar A, Mehta KD: Genetic complexity of the human geranylgeranyltransferase I beta-subunit gene: a multigene family of pseudogenes derived from mis-spliced transcripts. Gene. 1998, 210: 9-15. 10.1016/S0378-1119(98)00042-0. The authors suggest that there are 13 GGT1B pseudogenes, but these seem to correspond to only two in the human genome. ArticleCASPubMed Google Scholar
Blatch GL, Lassle M: The tetratricopeptide repeat: a structural motif mediating protein-protein interactions. BioEssays. 1999, 21: 932-939. 10.1002/(SICI)1521-1878(199911)21:11<932::AID-BIES5>3.3.CO;2-E. Review describing the family of TPR-containing proteins. ArticleCASPubMed Google Scholar
Zhang H, Grishin NV: The alpha-subunit of protein prenyltransferases is a member of the tetratricopeptide repeat family. Protein Sci. 1999, 8: 1658-1667. Evolutionary history and relationships of the FT α subunit. ArticleCASPubMedPubMed Central Google Scholar
Liang PH, Ko TP, Wang AH: Structure, mechanism and function of prenyltransferases. Eur J Biochem. 2002, 269: 3339-3354. 10.1046/j.1432-1033.2002.03014.x. A review giving a quick overview of isoprenylpyrophosphate synthases, isoprenyl cyclases and protein prenyltransferases that share processing polyisoprene derivatives in some way with partly overlapping structures and reaction mechanisms. ArticleCASPubMed Google Scholar
Altschul SF, Madden TL, Schaffer AA, Zhang J, Zhang Z, Miller W, Lipman DJ: Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Nucleic Acids Res. 1997, 25: 3389-3402. 10.1093/nar/25.17.3389. The standard reference for the sequence similarity search tools of the BLAST suite. ArticleCASPubMedPubMed Central Google Scholar
Eddy SR: Profile hidden Markov models. Bioinformatics. 1998, 14: 755-763. 10.1093/bioinformatics/14.9.755. A sensitive alternative method to BLAST for sequence similarity searches. ArticleCAS Google Scholar
Wendt KU, Poralla K, Schulz GE: Structure and function of a squalene cyclase. Science. 1997, 277: 1811-1815. 10.1126/science.277.5333.1811. The first crystal structure of a squalene cyclase. ArticleCASPubMed Google Scholar
Nes WD, Venkatramesh M: Enzymology of phytosterol transformations. Crit Rev Biochem Mol Biol. 1999, 34: 81-93. A review on plant hormone synthesis, including the cycloartenol synthases, which are homologous to the beta subunit of protein prenyltranserases. ArticleCASPubMed Google Scholar
Sturley SL: Conservation of eukaryotic sterol homeostasis: new insights from studies in budding yeast. Biochim Biophys Acta. 2000, 1529: 155-163. 10.1016/S1388-1981(00)00145-1. A review including discussion of ergosterol synthesis in fungi. ArticleCASPubMed Google Scholar
Janowski BA, Willy PJ, Devi TR, Falck JR, Mangelsdorf DJ: An oxysterol signalling pathway mediated by the nuclear receptor LXR alpha. Nature. 1996, 383: 728-731. 10.1038/383728a0. A description of intermediate steps in steroid hormone and cholesterol synthesis. ArticleCASPubMed Google Scholar
Kim JH, Lee JN, Paik YK: Cholesterol biosynthesis from lanosterol. A concerted role for Sp1 and NF-Y-binding sites for sterol-mediated regulation of rat 7- dehydrocholesterol reductase gene expression. J Biol Chem. 2001, 276: 18153-18160. 10.1074/jbc.M101661200. Analysis of the cholesterol biosynthesis pathway, starting from lanosterol. ArticleCASPubMed Google Scholar
Bateman A, Birney E, Durbin R, Eddy SR, Howe KL, Sonnhammer EL: The Pfam protein families database. Nucleic Acids Res. 2000, 28: 263-266. 10.1093/nar/28.1.263. A protein families database automatically generated by clustering proteins into families according to similarity identified with hidden Markov models. ArticleCASPubMedPubMed Central Google Scholar
Wendt KU, Lenhart A, Schulz GE: The structure of the membrane protein squalene-hopene cyclase at 2.0 Å resolution. J Mol Biol. 1999, 286: 175-187. 10.1006/jmbi.1998.2470. High-resolution structure of squalene-hopene cyclase plus discussion of catalytic mechanism and membrane interaction surfaces. ArticleCASPubMed Google Scholar
Long SB, Casey PJ, Beese LS: The basis for K-Ras4B binding specificity to protein farnesyltransferase revealed by 2 Å resolution ternary complex structures. Structure Fold Des. 2000, 8: 209-222. 10.1016/S0969-2126(00)00096-4. The first crystal structure of FT in complex with farnesyl-pyrophosphate. ArticleCASPubMed Google Scholar
Dursina B, Thoma NH, Sidorovitch V, Niculae A, Iakovenko A, Rak A, Albert S, Ceacareanu AC, Kolling R, Herrmann C, et al: Interaction of yeast Rab geranylgeranyl transferase with its protein and lipid substrates. Biochemistry. 2002, 41: 6805-6816. 10.1021/bi016067w. Shows that immunoglobulin-like and leucine-rich repeat domains are not required for non-CaaX prenylation. ArticleCASPubMed Google Scholar
Pylypenko O, Rak A, Reents R, Niculae A, Sidorovitch V, Cioaca MD, Bessolitsyna E, Thoma NH, Waldmann H, Schlichting I, et al: Structure of rab escort protein-1 in complex with rab geranylgeranyltransferase. Mol Cell. 2003, 11: 483-494. Structure of the complex of GGT2 with REP1. ArticleCASPubMed Google Scholar
Park HW, Boduluri SR, Moomaw JF, Casey PJ, Beese LS: Crystal structure of protein farnesyltransferase at 2.25 angstrom resolution. Science. 1997, 275: 1800-1804. 10.1126/science.275.5307.1800. The first crystal structure of protein FT. ArticleCASPubMed Google Scholar
Andres DA, Goldstein JL, Ho YK, Brown MS: Mutational analysis of alpha-subunit of protein farnesyltransferase. Evidence for a catalytic role. J Biol Chem. 1993, 268: 1383-1390. The first evidence for residues of the α subunit being involved in catalysis. ArticleCASPubMed Google Scholar
Zhang H, Seabra MC, Deisenhofer J: Crystal structure of Rab geranylgeranyltransferase at 2.0 Å resolution. Structure Fold Des. 2000, 8: 241-251. 10.1016/S0969-2126(00)00102-7. The first crystal structure of GGT2. ArticleCASPubMed Google Scholar
Moores SL, Schaber MD, Mosser SD, Rands E, O'Hara MB, Garsky VM, Marshall MS, Pompliano DL, Gibbs JB: Sequence dependence of protein isoprenylation. J Biol Chem. 1991, 266: 14603-14610. Detailed analysis of the amino-acid composition of the motifs recognized by protein prenyltransferases. ArticleCASPubMed Google Scholar
Caplin BE, Hettich LA, Marshall MS: Substrate characterization of the Saccharomyces cerevisiae protein farnesyltransferase and type-I protein geranylgeranyltransferase. Biochim Biophys Acta. 1994, 1205: 39-48. 10.1016/0167-4838(94)90089-2. Characterization of substrate motifs in yeast and the cross-specificity between FT and GGT1. ArticleCASPubMed Google Scholar
Reiss Y, Goldstein JL, Seabra MC, Casey PJ, Brown MS: Inhibition of purified p21ras farnesyl:protein transferase by Cys-AAX tetrapeptides. Cell. 1990, 62: 81-88. An early biochemical analysis of FT including farnesyl-pyrophosphate binding and inhibition with CaaX tetrapeptides. ArticleCASPubMed Google Scholar
Yokoyama K, McGeady P, Gelb MH: Mammalian protein geranylgeranyltransferase-I: substrate specificity, kinetic mechanism, metal requirements, and affinity labeling. Biochemistry. 1995, 34: 1344-1354. Complete biochemical characterization of mammalian GGT1. ArticleCASPubMed Google Scholar
Saderholm MJ, Hightower KE, Fierke CA: Role of metals in the reaction catalyzed by protein farnesyltransferase. Biochemistry. 2000, 39: 12398-12405. 10.1021/bi0011781. The metal requirements of FT catalysis. ArticleCASPubMed Google Scholar
Long SB, Casey PJ, Beese LS: Reaction path of protein farnesyltransferase at atomic resolution. Nature. 2002, 419: 645-650. 10.1038/nature00986. Completion of a series of structures resembling intermediate steps of the reaction pathway of FT. Discussion of implications for all three protein prenyltransferases. ArticleCASPubMed Google Scholar
Furfine ES, Leban JJ, Landavazo A, Moomaw JF, Casey PJ: Protein farnesyltransferase: kinetics of farnesyl pyrophosphate binding and product release. Biochemistry. 1995, 34: 6857-6862. Kinetic analysis of the reaction pathway of FT. ArticleCASPubMed Google Scholar
Alexandrov K, Simon I, Yurchenko V, Iakovenko A, Rostkova E, Scheidig AJ, Goody RS: Characterization of the ternary complex between Rab7, REP-1 and Rab geranylgeranyl transferase. Eur J Biochem. 1999, 265: 160-170. 10.1046/j.1432-1327.1999.00699.x. GGT2 prenylation requires formation of complex of GGT2 with substrate and escort protein. ArticleCASPubMed Google Scholar
Alexandrov K, Horiuchi H, Steele-Mortimer O, Seabra MC, Zerial M: Rab escort protein-1 is a multifunctional protein that accompanies newly prenylated rab proteins to their target membranes. EMBO J. 1994, 13: 5262-5273. Rab escort protein is not only required for the prenylation reaction but also accompanies Rab substrates to the membrane. This article also presents its homology to the GDP dissociation inhibitor. ArticleCASPubMedPubMed Central Google Scholar
Benito-Moreno RM, Miaczynska M, Bauer BE, Schweyen RJ, Ragnini A: Mrs6p, the yeast homologue of the mammalian choroideraemia protein: immunological evidence for its function as the Ypt1p Rab escort protein. Curr Genet. 1994, 27: 23-25. Characterization of the yeast Rab/Ypt escort protein. ArticleCASPubMed Google Scholar
Haverty PM, Weng Z, Best NL, Auerbach KR, Hsiao LL, Jensen RV, Gullans SR: HugeIndex: a database with visualization tools for high-density oligonucleotide array data from normal human tissues. Nucleic Acids Res. 2002, 30: 214-217. 10.1093/nar/30.1.214. Systematic mRNA expression analysis of human tissues. ArticleCASPubMedPubMed Central Google Scholar
HuGE Index. A database of systematic mRNA expression analyses of human tissues., [http://hugeindex.org/]
Tsao KL, Waugh DS: Balancing the production of two recombinant proteins in Escherichia coli by manipulating plasmid copy number: high-level expression of heterodimeric Ras farnesyltransferase.. Protein Expr Purif. 1997, 11: 233-240. 10.1006/prep.1997.0794. The α subunit has to be downregulated when coexpressed with the β subunit in order to yield high levels of recombinant FT. ArticleCASPubMed Google Scholar
Gordon JI, Duronio RJ, Rudnick DA, Adams SP, Gokel GW: Protein _N_-myristoylation. J Biol Chem. 1991, 266: 8647-8650. Compact review on protein _N_-myristoylation. ArticleCASPubMed Google Scholar
Maurer-Stroh S, Eisenhaber B, Eisenhaber F: N-terminal _N_-myristoylation of proteins: refinement of the sequence motif and its taxon-specific differences. J Mol Biol. 2002, 317: 523-540. 10.1006/jmbi.2002.5425. A detailed update of the sequence motif for _N_-myristoylation as well as enzyme-substrate interactions. ArticleCASPubMed Google Scholar
Maurer-Stroh S, Eisenhaber B, Eisenhaber F: N-terminal _N_-myristoylation of proteins: prediction of substrate proteins from amino acid sequence. J Mol Biol. 2002, 317: 541-557. 10.1006/jmbi.2002.5426. Large-scale prediction unveils a series of new target proteins for protein _N_-myristoylation. ArticleCASPubMed Google Scholar
Morello JP, Bouvier M: Palmitoylation: a post-translational modification that regulates signalling from G-protein coupled receptors. Biochem Cell Biol. 1996, 74: 449-457. A review on the importance of palmitoylation in G-protein signaling. ArticleCASPubMed Google Scholar
Resh MD: Fatty acylation of proteins: new insights into membrane targeting of myristoylated and palmitoylated proteins. Biochim Biophys Acta. 1999, 1451: 1-16. 10.1016/S0167-4889(99)00075-0. A short review on myristoyl and palmitoyl anchors for membrane targeting. ArticleCASPubMed Google Scholar
Chatterjee S, Mayor S: The GPI-anchor and protein sorting. Cell Mol Life Sci. 2001, 58: 1969-1987. A review on glycosylphosphatidylinositol lipid anchors. ArticleCASPubMed Google Scholar
Eisenhaber B, Bork P, Eisenhaber F: Post-translational GPI lipid anchor modification of proteins in kingdoms of life: analysis of protein sequence data from complete genomes. Protein Eng. 2001, 14: 17-25. 10.1093/protein/14.1.17. Full genome analyses of GPI-anchor-containing proteins. ArticleCASPubMed Google Scholar
Sinensky M: Functional aspects of polyisoprenoid protein substituents: roles in protein-protein interaction and trafficking. Biochim Biophys Acta. 2000, 1529: 203-209. 10.1016/S1388-1981(00)00149-9. Role of farnesyl and geranylgeranyl anchors in protein-protein interactions. ArticleCASPubMed Google Scholar
Sinensky M: Recent advances in the study of prenylated proteins. Biochim Biophys Acta. 2000, 1484: 93-106. 10.1016/S1388-1981(00)00009-3. Review on enzymology and function of protein prenylation. ArticleCASPubMed Google Scholar
Trueblood CE, Boyartchuk VL, Picologlou EA, Rozema D, Poulter CD, Rine J: The CaaX proteases, Afc1p and Rce1p, have overlapping but distinct substrate specificities. Mol Cell Biol. 2000, 20: 4381-4392. 10.1128/MCB.20.12.4381-4392.2000. Characterization of endoproteases cleaving the carboxy-terminal tripeptide after prenylation of cysteine in the CaaX motif. ArticleCASPubMedPubMed Central Google Scholar
Pei J, Grishin NV: Type II CAAX prenyl endopeptidases belong to a novel superfamily of putative membrane-bound metalloproteases. Trends Biochem Sci. 2001, 26: 275-277. 10.1016/S0968-0004(01)01813-8. A description of a protein superfamily that includes CaaX prenyl endoproteases. ArticleCASPubMed Google Scholar
Bergo MO, Leung GK, Ambroziak P, Otto JC, Casey PJ, Gomes AQ, Seabra MC, Young SG: Isoprenylcysteine carboxyl methyltransferase deficiency in mice. J Biol Chem. 2001, 276: 5841-5845. 10.1074/jbc.C000831200. A description of the methyltransferase that carboxymethylates cysteines at the carboxyl terminus of prenylated proteins. ArticleCASPubMed Google Scholar
Hancock JF, Magee AI, Childs JE, Marshall CJ: All ras proteins are polyisoprenylated but only some are palmitoylated. Cell. 1989, 57: 1167-1177. Palmitoylation of Ras proteins sometimes takes place after prenylation. ArticleCASPubMed Google Scholar
Kohl NE, Omer CA, Conner MW, Anthony NJ, Davide JP, deSolms SJ, Giuliani EA, Gomez RP, Graham SL, Hamilton K, et al: Inhibition of farnesyltransferase induces regression of mammary and salivary carcinomas in ras transgenic mice. Nat Med. 1995, 1: 792-797. FT inhibition causes tumor regression in H-Ras transforming mice with minimal side-effects on the organism. ArticleCASPubMed Google Scholar
Prendergast GC, Rane N: Farnesyltransferase inhibitors: mechanism and applications. Expert Opin Investig Drugs. 2001, 10: 2105-2116. Detailed review on FTI, including their effects on non-neoplastic diseases. ArticleCASPubMed Google Scholar
Armstrong SA, Hannah VC, Goldstein JL, Brown MS: CAAX geranylgeranyl transferase transfers farnesyl as efficiently as geranylgeranyl to RhoB. J Biol Chem. 1995, 270: 7864-7868. 10.1074/jbc.270.43.25879. Reports that GGT1 can farnesylate RhoB as well as geranylgeranylating it, a surprising finding. ArticleCASPubMed Google Scholar
Yokoyama K, Zimmerman K, Scholten J, Gelb MH: Differential prenyl pyrophosphate binding to mammalian protein geranylgeranyltransferase-I and protein farnesyltransferase and its consequence on the specificity of protein prenylation. J Biol Chem. 1997, 272: 3944-3952. 10.1074/jbc.272.1.503. Detailed analysis of prenyl pyrophosphate cross-specificity of FT and GGT1. ArticleCASPubMed Google Scholar
Tamanoi F, Kato-Stankiewicz J, Jiang C, Machado I, Thapar N: Farnesylated proteins and cell cycle progression. J Cell Biochem suppl. 2001, Suppl 37: 64-70. 10.1002/jcb.10067. The involvement of farnesylated proteins in the cell cycle in the light of the effects of FT inhibition. ArticleCASPubMed Google Scholar
Ashar HR, James L, Gray K, Carr D, Black S, Armstrong L, Bishop WR, Kirschmeier P: Farnesyl transferase inhibitors block the farnesylation of CENP-E and CENP-F and alter the association of CENP-E with the microtubules. J Biol Chem. 2000, 275: 30451-30457. 10.1074/jbc.M003469200. A lack of prenylation of CENP-E affects microtubule-centromere interaction at the G2/M phase checkpoint. ArticleCASPubMed Google Scholar
Lebowitz PF, Casey PJ, Prendergast GC, Thissen JA: Farnesyltransferase inhibitors alter the prenylation and growth-stimulating function of RhoB. J Biol Chem. 1997, 272: 15591-15594. 10.1074/jbc.272.25.15591. Altering the prenylation status of RhoB alters its functions. ArticleCASPubMed Google Scholar
Tamanoi F, Gau CL, Jiang C, Edamatsu H, Kato-Stankiewicz J: Protein farnesylation in mammalian cells: effects of farnesyltransferase inhibitors on cancer cells. Cell Mol Life Sci. 2001, 58: 1636-1649. A review on cellular processes affected by FT inhibition in mammalian cancers. ArticleCASPubMed Google Scholar
Prendergast GC: Actin' up: RhoB in cancer and apoptosis. Nat Rev Cancer. 2001, 1: 162-168. 10.1038/35101096. A short review of RhoB function, including a hypothesis on the effects of FTIs. ArticleCASPubMed Google Scholar
Pereira-Leal JB, Seabra MC: Evolution of the Rab family of small GTP-binding proteins. J Mol Biol. 2001, 313: 889-901. 10.1006/jmbi.2001.5072. An extensive analysis of Rab proteins in eukaryotic genomes. ArticleCASPubMed Google Scholar
Seabra MC, Mules EH, Hume AN: Rab GTPases, intracellular traffic and disease. Trends Mol Med. 2002, 8: 23-30. 10.1016/S1471-4914(01)02227-4. An update of Rab functions and localizations, plus their involvement in disease. ArticleCASPubMed Google Scholar
Pereira-Leal JB, Hume AN, Seabra MC: Prenylation of Rab GTPases: molecular mechanisms and involvement in genetic disease. FEBS Lett. 2001, 498: 197-200. 10.1016/S0014-5793(01)02483-8. A minireview of Rab prenylation deficiency and disease. ArticleCASPubMed Google Scholar
Huizing M, Anikster Y, Gahl WA: Hermansky-Pudlak syndrome and related disorders of organelle formation. Traffic. 2000, 1: 823-835. 10.1034/j.1600-0854.2000.011103.x. A review on Hermansky-Pudlak syndrome and related disorders. ArticleCASPubMed Google Scholar
Detter JC, Zhang Q, Mules EH, Novak EK, Mishra VS, Li W, McMurtrie EB, Tchernev VT, Wallace MR, Seabra MC, et al: Rab geranylgeranyl transferase alpha mutation in the gunmetal mouse reduces Rab prenylation and platelet synthesis. Proc Natl Acad Sci USA. 2000, 97: 4144-4149. 10.1073/pnas.080517697. Genetic and molecular basis for Rab prenylation deficiency in Hermansky-Pudlak syndrome. ArticleCASPubMedPubMed Central Google Scholar
Seabra MC: New insights into the pathogenesis of choroideremia: a tale of two REPs. Ophthalmic Genet. 1996, 17: 43-46. The mechanism of choroideremia pathology involves an inability of Rab escort protein 2 to fully substitute for function of Rab escort protein 1. ArticleCASPubMed Google Scholar
van den Hurk JA, Schwartz M, van Bokhoven H, van de Pol TJ, Bogerd L, Pinckers AJ, Bleeker-Wagemakers EM, Pawlowitzki IH, Ruther K, Ropers HH, et al: Molecular basis of choroideremia (CHM): mutations involving the Rab escort protein-1 (REP-1) gene. Hum Mutat. 1997, 9: 110-117. 10.1002/(SICI)1098-1004(1997)9:2<110::AID-HUMU2>3.3.CO;2-9. A loss-of-function mutation in the CHM gene that codes for Rab escort protein 1 results in choroideremia. ArticleCASPubMed Google Scholar
Wang T, Danielson PD, Li BY, Shah PC, Kim SD, Donahoe PK: The p21(RAS) farnesyltransferase alpha subunit in TGF-beta and activin signaling. Science. 1996, 271: 1120-1122. An isoform of FT α subunit that has a non-classical function. ArticleCASPubMed Google Scholar
Cox AD, Der CJ: Farnesyltransferase inhibitors: promises and realities. Curr Opin Pharmacol. 2002, 2: 388-393. 10.1016/S1471-4892(02)00181-9. A review on the pitfalls of FT inhibition. ArticleCASPubMed Google Scholar