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Volumn 2, Issue 5, 1999, Pages 388-392

Protein farnesylation in plants: A greasy tale

Author keywords

[No Author keywords available]

Indexed keywords

ARABIDOPSIS;

EID: 0033214738     PISSN: 13695266     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1369-5266(99)00010-2     Document Type: Review
Times cited : (37)

References (39)
  • 1
    • 0026757391 scopus 로고
    • Structure and biological effects of lipid modifications on proteins
    • Chow M, Der CJ, Buss JE Structure and biological effects of lipid modifications on proteins. Curr Opin Cell Biol. 4:1992;629-636.
    • (1992) Curr Opin Cell Biol , vol.4 , pp. 629-636
    • Chow, M.1    Der, C.J.2    Buss, J.E.3
  • 2
    • 0027076554 scopus 로고
    • Protein prenylation: Genes, enzymes, targets, and functions
    • Schafer WR, Rine J Protein prenylation: genes, enzymes, targets, and functions. Anuu Rev Genet. 26:1992;209-237.
    • (1992) Anuu Rev Genet , vol.26 , pp. 209-237
    • Schafer, W.R.1    Rine, J.2
  • 3
    • 0026735063 scopus 로고
    • Protein isoprenylation and methylation at carboxyl-terminal cysteine residues
    • Clark S Protein isoprenylation and methylation at carboxyl-terminal cysteine residues. Annu Rev Biochem. 61:1992;355-386.
    • (1992) Annu Rev Biochem , vol.61 , pp. 355-386
    • Clark, S.1
  • 4
    • 0029966304 scopus 로고    scopus 로고
    • Protein prenyltransferases
    • Casey PJ, Seabra MC Protein prenyltransferases. J Biol Chem. 271:1996;5289-5292.
    • (1996) J Biol Chem , vol.271 , pp. 5289-5292
    • Casey, P.J.1    Seabra, M.C.2
  • 5
    • 0027284950 scopus 로고
    • Protein prenylation: A mediator of protein-protein interactions
    • Marshall CJ Protein prenylation: a mediator of protein-protein interactions. Science. 259:1993;1865-1866.
    • (1993) Science , vol.259 , pp. 1865-1866
    • Marshall, C.J.1
  • 6
    • 0027500533 scopus 로고
    • The effect of post-translational modifications on the interaction of, RAS2 with adenylyl cyclase
    • Kuroda Y, Suzuki N, Kataoka T The effect of post-translational modifications on the interaction of, RAS2 with adenylyl cyclase. Science. 259:1993;683-686.
    • (1993) Science , vol.259 , pp. 683-686
    • Kuroda, Y.1    Suzuki, N.2    Kataoka, T.3
  • 7
    • 0027239583 scopus 로고
    • Isoprenylation of the plant molecular chaperone ANJ1 facilitates membrane association and function at high temperature
    • Zhu JK, Bressan RA, Hasegawa PM Isoprenylation of the plant molecular chaperone ANJ1 facilitates membrane association and function at high temperature. Proc Natl Acad Sci USA. 90:1993;8557-8561.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 8557-8561
    • Zhu, J.K.1    Bressan, R.A.2    Hasegawa, P.M.3
  • 8
    • 0027586925 scopus 로고
    • Protein isoprenylation in suspension-cultured tobacco cells
    • Randall SK, Marshall MS, Crowell DN Protein isoprenylation in suspension-cultured tobacco cells. Plant Cell. 5:1993;433-442.
    • (1993) Plant Cell , vol.5 , pp. 433-442
    • Randall, S.K.1    Marshall, M.S.2    Crowell, D.N.3
  • 9
    • 0030266778 scopus 로고    scopus 로고
    • Molecular and biochemical characterization of tomato farnesyl-protein transferase
    • Schmitt D, Callan K, Grussem W Molecular and biochemical characterization of tomato farnesyl-protein transferase. Plant Physiol. 112:1996;767-777.
    • (1996) Plant Physiol , vol.112 , pp. 767-777
    • Schmitt, D.1    Callan, K.2    Grussem, W.3
  • 10
    • 0028836231 scopus 로고
    • Changes in protein isoprenylation during the growth of suspension-cultured tobacco cells
    • Morehead TA, Biermann BJ, Crowell DN, Randall SK Changes in protein isoprenylation during the growth of suspension-cultured tobacco cells. Plant Physiol. 109:1995;277-284.
    • (1995) Plant Physiol , vol.109 , pp. 277-284
    • Morehead, T.A.1    Biermann, B.J.2    Crowell, D.N.3    Randall, S.K.4
  • 11
    • 0029585503 scopus 로고
    • Identification of spinach farnesyltransferase-dithiothreitol as an acceptor in vitro
    • Parmryd I, Shipton CA, Swiezewska E, Anderson B, Dallner G Identification of spinach farnesyltransferase-dithiothreitol as an acceptor in vitro. Eur J Biochem. 234:1995;723-731.
    • (1995) Eur J Biochem , vol.234 , pp. 723-731
    • Parmryd, I.1    Shipton, C.A.2    Swiezewska, E.3    Anderson, B.4    Dallner, G.5
  • 14
    • 0030909336 scopus 로고    scopus 로고
    • Modulation of Ras and a-factor function by carboxyl-terminal proteolysis
    • Boyartchuk VL, Ashby MN, Rine J Modulation of Ras and a-factor function by carboxyl-terminal proteolysis. Science. 275:1997;1796-1800.
    • (1997) Science , vol.275 , pp. 1796-1800
    • Boyartchuk, V.L.1    Ashby, M.N.2    Rine, J.3
  • 15
    • 0033605743 scopus 로고    scopus 로고
    • Cloning and characterization of a mammalian prenyl protein-specific protease
    • Otto JC, Kim E, Young SG, Casey PJ Cloning and characterization of a mammalian prenyl protein-specific protease. J Biol Chem. 274:1999;8379-8382.
    • (1999) J Biol Chem , vol.274 , pp. 8379-8382
    • Otto, J.C.1    Kim, E.2    Young, S.G.3    Casey, P.J.4
  • 16
    • 0028125792 scopus 로고
    • Nucleotide sequence of the yeast STE14 gene, which encodesfarnesylcysteine carboxyl methyltransferase, and demonstration of its essential role in a-factor export
    • Sapperstein S, Berkower C, Michaelis S Nucleotide sequence of the yeast STE14 gene, which encodesfarnesylcysteine carboxyl methyltransferase, and demonstration of its essential role in a-factor export. Mol Cell Biol. 14:1994;1438-1449.
    • (1994) Mol Cell Biol , vol.14 , pp. 1438-1449
    • Sapperstein, S.1    Berkower, C.2    Michaelis, S.3
  • 17
    • 0031020235 scopus 로고    scopus 로고
    • Genes encoding farnesyl cysteine carboxyl methyltransferase in Schizosaccharomyces pombe and Xenopus laevis
    • Imai Y, Davey J, Kawagishi-Kobayashi M, Yamamoto M Genes encoding farnesyl cysteine carboxyl methyltransferase in Schizosaccharomyces pombe and Xenopus laevis. Mol Cell Biol. 17:1997;1543-1551.
    • (1997) Mol Cell Biol , vol.17 , pp. 1543-1551
    • Imai, Y.1    Davey, J.2    Kawagishi-Kobayashi, M.3    Yamamoto, M.4
  • 18
    • 0000457145 scopus 로고    scopus 로고
    • Prenylcysteine a-carboxyl methyltransferase in suspension-cultured tobacco cells
    • This paper demonstrated for the first time an enzyme activity of carboxyl methylation of prenylated cysteines in plants. It also shows that methylation of both geranylgeranyled and farnesylated targets is catalyzed by the same enzyme.
    • Crowell DN, Sen SE, Randall SK Prenylcysteine a-carboxyl methyltransferase in suspension-cultured tobacco cells. Plant Physiol. 118:1998;115-123. This paper demonstrated for the first time an enzyme activity of carboxyl methylation of prenylated cysteines in plants. It also shows that methylation of both geranylgeranyled and farnesylated targets is catalyzed by the same enzyme.
    • (1998) Plant Physiol , vol.118 , pp. 115-123
    • Crowell, D.N.1    Sen, S.E.2    Randall, S.K.3
  • 19
    • 0027539011 scopus 로고
    • Protein farnesyltransferase in plants. Molecular cloning and expression of a homolog of the β subunit from the garden pea
    • Yang Z, Cramer CL, Watson JC Protein farnesyltransferase in plants. Molecular cloning and expression of a homolog of the β subunit from the garden pea. Plant Physiol. 101:1993;667-674.
    • (1993) Plant Physiol , vol.101 , pp. 667-674
    • Yang, Z.1    Cramer, C.L.2    Watson, J.C.3
  • 20
    • 0030344706 scopus 로고    scopus 로고
    • Protein prenylation in plants: Molecular characterization and involvement in cell cycle control
    • Qian D, Zhou D, Ju R, Cramer CL, Yang Z Protein prenylation in plants: molecular characterization and involvement in cell cycle control. Plant Cell. 8:1996;2381-2394.
    • (1996) Plant Cell , vol.8 , pp. 2381-2394
    • Qian, D.1    Zhou, D.2    Ju, R.3    Cramer, C.L.4    Yang, Z.5
  • 22
    • 0029839761 scopus 로고    scopus 로고
    • A protein farnesyl transferase involved abscisic acid signal transduction in Arabidopsis
    • Cutler S, Ghassemian M, Bonetta D, Cooney S, McCourt P A protein farnesyl transferase involved abscisic acid signal transduction in Arabidopsis. Science. 273:1996;1239-1241.
    • (1996) Science , vol.273 , pp. 1239-1241
    • Cutler, S.1    Ghassemian, M.2    Bonetta, D.3    Cooney, S.4    McCourt, P.5
  • 23
    • 0007282498 scopus 로고    scopus 로고
    • A cDNA clone encoding the beta subunit of protein farnesyltransferase from Nicotiana glutinosa
    • Zhou D, Yang Z, Cramer CL A cDNA clone encoding the beta subunit of protein farnesyltransferase from Nicotiana glutinosa. Plant Physiol. 112:1996;1398-1399.
    • (1996) Plant Physiol , vol.112 , pp. 1398-1399
    • Zhou, D.1    Yang, Z.2    Cramer, C.L.3
  • 24
    • 0031259857 scopus 로고    scopus 로고
    • Developmental and environmental regulation of tissue- And cell-specific expression of a pea protein farnesyltransferase
    • Zhou D, Qian D, Cramer CL, Yang Z Developmental and environmental regulation of tissue- and cell-specific expression of a pea protein farnesyltransferase. Plant J. 12:1997;921-930.
    • (1997) Plant J , vol.12 , pp. 921-930
    • Zhou, D.1    Qian, D.2    Cramer, C.L.3    Yang, Z.4
  • 25
    • 0031434108 scopus 로고    scopus 로고
    • Induction of the cholesterol metabolic pathway regulates the farnesylation of RAS in embryonic chick heart cells: A new role for ras in regulating the expression of muscarinic receptors and G proteins
    • Gadbut AP, Wu L, Tang D, Papageorge A, Watson JA, Galper JB Induction of the cholesterol metabolic pathway regulates the farnesylation of RAS in embryonic chick heart cells: a new role for ras in regulating the expression of muscarinic receptors and G proteins. EMBO J. 15:1997;7250-7260.
    • (1997) EMBO J , vol.15 , pp. 7250-7260
    • Gadbut, A.P.1    Wu, L.2    Tang, D.3    Papageorge, A.4    Watson, J.A.5    Galper, J.B.6
  • 26
    • 0025845750 scopus 로고
    • The CaaX motif is required for isoprenylation, carboxyl methylation, and nuclear membrane association of lamin B2
    • Kitten GT, Nigg EA The CaaX motif is required for isoprenylation, carboxyl methylation, and nuclear membrane association of lamin B2. J Cell Biol. 113:1991;13-23.
    • (1991) J Cell Biol , vol.113 , pp. 13-23
    • Kitten, G.T.1    Nigg, E.A.2
  • 27
    • 0032578008 scopus 로고    scopus 로고
    • C-Nap1, a novel centrosomal coiled-coil protein and candidate substrate of the cell cycle-regulated protein kinase Nek2
    • Fry AM, Mayor T, Meraldi P, Stierhof YD, Tanaka K, Nigg EA C-Nap1, a novel centrosomal coiled-coil protein and candidate substrate of the cell cycle-regulated protein kinase Nek2. J Cell Biol. 141:1998;1563-1574.
    • (1998) J Cell Biol , vol.141 , pp. 1563-1574
    • Fry, A.M.1    Mayor, T.2    Meraldi, P.3    Stierhof, Y.D.4    Tanaka, K.5    Nigg, E.A.6
  • 28
    • 0027183972 scopus 로고
    • CSE1 and CSE2, two new genes required for accurate mitotic chromosome segregation in Saccharomyces cerevisiae
    • Xiao Z, McGrew JT, Schroeder AJ, Fitzgerald-Hayes M CSE1 and CSE2, two new genes required for accurate mitotic chromosome segregation in Saccharomyces cerevisiae. Mol Cell Biol. 13:1993;4691-4702.
    • (1993) Mol Cell Biol , vol.13 , pp. 4691-4702
    • Xiao, Z.1    McGrew, J.T.2    Schroeder, A.J.3    Fitzgerald-Hayes, M.4
  • 29
    • 0032473350 scopus 로고    scopus 로고
    • The mitotic peptidyl-prolyl isomerase, Pin1, interacts with Cdc25 and Plx1
    • Crenshaw DG, Yang J, Means AR, Kornbluth S The mitotic peptidyl-prolyl isomerase, Pin1, interacts with Cdc25 and Plx1. EMBO J. 17:1998;1315-1327.
    • (1998) EMBO J , vol.17 , pp. 1315-1327
    • Crenshaw, D.G.1    Yang, J.2    Means, A.R.3    Kornbluth, S.4
  • 30
    • 0030163073 scopus 로고    scopus 로고
    • The Arabidopsis XET-related gene family: Environmental and hormonal regulation of expression
    • Xu W, Campbell P, Vargheese AK, Braam J The Arabidopsis XET-related gene family: environmental and hormonal regulation of expression. Plant J. 9:1996;879-889.
    • (1996) Plant J , vol.9 , pp. 879-889
    • Xu, W.1    Campbell, P.2    Vargheese, A.K.3    Braam, J.4
  • 31
    • 0032500887 scopus 로고    scopus 로고
    • Role of farnesyltransferase in ABA regulation of guard cell anion channels and plant water loss
    • The era1 mutants were originally isolated by the inability to germinate in the presence of low concentration of exogenous ABA. This paper demonstrated the first evidence for a role of ERA1 in ABA-mediated stomatal closure and drought avoidance in Arabidopsis.
    • Pei ZM, Ghassemian M, Kwak CM, McCourt P, Schroeder JI Role of farnesyltransferase in ABA regulation of guard cell anion channels and plant water loss. Science. 282:1998;287-290. The era1 mutants were originally isolated by the inability to germinate in the presence of low concentration of exogenous ABA. This paper demonstrated the first evidence for a role of ERA1 in ABA-mediated stomatal closure and drought avoidance in Arabidopsis.
    • (1998) Science , vol.282 , pp. 287-290
    • Pei, Z.M.1    Ghassemian, M.2    Kwak, C.M.3    McCourt, P.4    Schroeder, J.I.5
  • 32
    • 0032102380 scopus 로고    scopus 로고
    • Genetic analysis of ABA signal transduction pathways
    • Bonetta D, McCourt P Genetic analysis of ABA signal transduction pathways. Trends Plant Sci. 3:1998;231-235.
    • (1998) Trends Plant Sci , vol.3 , pp. 231-235
    • Bonetta, D.1    McCourt, P.2
  • 33
    • 0028339956 scopus 로고
    • Arabidopsis ABA response gene ABI1: Features of a calcium-modulated protein phosphatase
    • Leung J, Bouvier-Durand M, Morris PC, Guerrier D, Chefdor F, Giraudat J Arabidopsis ABA response gene ABI1: features of a calcium-modulated protein phosphatase. Science. 264:1994;1448-1452.
    • (1994) Science , vol.264 , pp. 1448-1452
    • Leung, J.1    Bouvier-Durand, M.2    Morris, P.C.3    Guerrier, D.4    Chefdor, F.5    Giraudat, J.6
  • 34
    • 0031131635 scopus 로고    scopus 로고
    • The Arabidopsis ABSCISIC ACID-INSENSITIVE2 (ABI2) and ABI1 genes encode homologous protein phosphatases 2C involved in abscisic acid signal transduction
    • Leung J, Merlot S, Giraudat J The Arabidopsis ABSCISIC ACID-INSENSITIVE2 (ABI2) and ABI1 genes encode homologous protein phosphatases 2C involved in abscisic acid signal transduction. Plant Cell. 9:1997;759-771.
    • (1997) Plant Cell , vol.9 , pp. 759-771
    • Leung, J.1    Merlot, S.2    Giraudat, J.3
  • 36
    • 0030916369 scopus 로고    scopus 로고
    • Farnesyltransferase inhibitors alter the prenylation and growth-stimulating function of RhoB
    • Lebowitz PF, Casey PJ, Prendergast GC, Thissen JA Farnesyltransferase inhibitors alter the prenylation and growth-stimulating function of RhoB. J Biol Chem. 272:1997;15591-15594.
    • (1997) J Biol Chem , vol.272 , pp. 15591-15594
    • Lebowitz, P.F.1    Casey, P.J.2    Prendergast, G.C.3    Thissen, J.A.4
  • 37
    • 0028178790 scopus 로고
    • Regulation of the Arabidopsis floral homeotic gene APETALA1
    • Gustafson-Brown C, Savidge B, Yanofsky MF Regulation of the Arabidopsis floral homeotic gene APETALA1. Cell. 76:1994;131-143.
    • (1994) Cell , vol.76 , pp. 131-143
    • Gustafson-Brown, C.1    Savidge, B.2    Yanofsky, M.F.3
  • 38
    • 0028956983 scopus 로고
    • Molecular basis of the cauliflower phenotype in Arabidopsis
    • Kempin SA, Savidge B, Yanofsky MF Molecular basis of the cauliflower phenotype in Arabidopsis. Science. 267:1995;522-525.
    • (1995) Science , vol.267 , pp. 522-525
    • Kempin, S.A.1    Savidge, B.2    Yanofsky, M.F.3
  • 39


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