메뉴 건너뛰기




Volumn 380, Issue 2, 2006, Pages 159-166

Prenylcysteine methylesterase in Arabidopsis thaliana

Author keywords

Arabidopsis thaliana; Protein methylation; Protein prenylation

Indexed keywords

CYSTEINE DERIVATIVE; ESTER DERIVATIVE; ESTERASE; PRENYLCYSTEINE ALPHA CARBOXYLMETHYL ESTERASE; PRENYLCYSTEINE METHYL ESTER; UNCLASSIFIED DRUG;

EID: 33748423737     PISSN: 03781119     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.gene.2006.05.023     Document Type: Article
Times cited : (16)

References (44)
  • 2
    • 0030801002 scopus 로고    scopus 로고
    • Gapped BLAST and PSI-BLAST: a new generation of protein database search programs
    • Altschul S.F., et al. Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Nucleic Acids Res. 25 (1997) 3389-3402
    • (1997) Nucleic Acids Res. , vol.25 , pp. 3389-3402
    • Altschul, S.F.1
  • 3
    • 0028338547 scopus 로고
    • Determination of structural requirements for the interaction of Rab6 with RabGDI and Rab geranylgeranyltransferase
    • Beranger F., et al. Determination of structural requirements for the interaction of Rab6 with RabGDI and Rab geranylgeranyltransferase. J. Biol. Chem. 269 (1994) 13637-13643
    • (1994) J. Biol. Chem. , vol.269 , pp. 13637-13643
    • Beranger, F.1
  • 4
    • 0034625181 scopus 로고    scopus 로고
    • Targeted inactivation of the isoprenylcysteine carboxyl methyltransferase gene causes mislocalization of K-Ras in mammalian cells
    • Bergo M.O., Leung G.K., Ambroziak P., Otto J.C., Casey P.J., and Young S.G. Targeted inactivation of the isoprenylcysteine carboxyl methyltransferase gene causes mislocalization of K-Ras in mammalian cells. J. Biol. Chem. 275 (2000) 17605-17610
    • (2000) J. Biol. Chem. , vol.275 , pp. 17605-17610
    • Bergo, M.O.1    Leung, G.K.2    Ambroziak, P.3    Otto, J.C.4    Casey, P.J.5    Young, S.G.6
  • 5
    • 0035937112 scopus 로고    scopus 로고
    • Isoprenylcysteine carboxyl methyltransferase deficiency in mice
    • Bergo M.O., et al. Isoprenylcysteine carboxyl methyltransferase deficiency in mice. J. Biol. Chem. 276 (2001) 5841-5845
    • (2001) J. Biol. Chem. , vol.276 , pp. 5841-5845
    • Bergo, M.O.1
  • 6
    • 0036132907 scopus 로고    scopus 로고
    • Absence of the CAAX endoprotease Rce1: effects on cell growth and transformation
    • Bergo M.O., et al. Absence of the CAAX endoprotease Rce1: effects on cell growth and transformation. Mol. Cell. Biol. 22 (2002) 171-181
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 171-181
    • Bergo, M.O.1
  • 7
    • 0036791026 scopus 로고    scopus 로고
    • Zmpste24 deficiency in mice causes spontaneous bone fractures, muscle weakness, and a prelamin A processing defect
    • Bergo M.O., et al. Zmpste24 deficiency in mice causes spontaneous bone fractures, muscle weakness, and a prelamin A processing defect. Proc. Natl. Acad. Sci. U. S. A. 99 (2002) 13049-13054
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 13049-13054
    • Bergo, M.O.1
  • 8
    • 1642326112 scopus 로고    scopus 로고
    • Inactivation of Icmt inhibits transformation by oncogenic K-Ras and B-Raf
    • Bergo M.O., et al. Inactivation of Icmt inhibits transformation by oncogenic K-Ras and B-Raf. J. Clin. Invest. 113 (2004) 539-550
    • (2004) J. Clin. Invest. , vol.113 , pp. 539-550
    • Bergo, M.O.1
  • 9
    • 1042266632 scopus 로고    scopus 로고
    • On the physiological importance of endoproteolysis of CAAX proteins: heart-specific RCE1 knockout mice develop a lethal cardiomyopathy
    • Bergo M.O., et al. On the physiological importance of endoproteolysis of CAAX proteins: heart-specific RCE1 knockout mice develop a lethal cardiomyopathy. J. Biol. Chem. 279 (2004) 4729-4736
    • (2004) J. Biol. Chem. , vol.279 , pp. 4729-4736
    • Bergo, M.O.1
  • 10
    • 0030909336 scopus 로고    scopus 로고
    • Modulation of Ras and a-factor function by carboxyl-terminal proteolysis
    • Boyartchuk V.L., Ashby M.N., and 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
  • 11
    • 0037119482 scopus 로고    scopus 로고
    • The Arabidopsis AtSTE24 is a CAAX protease with broad substrate specificity
    • Bracha K., Lavy M., and Yalovsky S. The Arabidopsis AtSTE24 is a CAAX protease with broad substrate specificity. J. Biol. Chem. 277 (2002) 29856-29864
    • (2002) J. Biol. Chem. , vol.277 , pp. 29856-29864
    • Bracha, K.1    Lavy, M.2    Yalovsky, S.3
  • 12
    • 0037444824 scopus 로고    scopus 로고
    • Identification, functional expression and enzymic analysis of two distinct CaaX proteases from Caenorhabditis elegans
    • Cadiñanos J., Schmidt W.K., Fueyo A., Varela I., López-Otín C., and Freije J.M. Identification, functional expression and enzymic analysis of two distinct CaaX proteases from Caenorhabditis elegans. Biochem. J. 370 (2003) 1047-1054
    • (2003) Biochem. J. , vol.370 , pp. 1047-1054
    • Cadiñanos, J.1    Schmidt, W.K.2    Fueyo, A.3    Varela, I.4    López-Otín, C.5    Freije, J.M.6
  • 13
    • 0142211262 scopus 로고    scopus 로고
    • AtFACE-2, a functional prenylated protein protease from Arabidopsis thaliana related to mammalian Ras-converting enzymes
    • Cadiñanos J., et al. AtFACE-2, a functional prenylated protein protease from Arabidopsis thaliana related to mammalian Ras-converting enzymes. J. Biol. Chem. 278 (2003) 42091-42097
    • (2003) J. Biol. Chem. , vol.278 , pp. 42091-42097
    • Cadiñanos, J.1
  • 14
    • 0036909347 scopus 로고    scopus 로고
    • Prenylcysteine α-carboxyl methyltransferase expression and function in Arabidopsis thaliana
    • Chary S.N., Bultema R.L., Packard C.E., and Crowell D.N. Prenylcysteine α-carboxyl methyltransferase expression and function in Arabidopsis thaliana. Plant J. 32 (2002) 735-747
    • (2002) Plant J. , vol.32 , pp. 735-747
    • Chary, S.N.1    Bultema, R.L.2    Packard, C.E.3    Crowell, D.N.4
  • 15
    • 0026735063 scopus 로고
    • Protein isoprenylation and methylation at carboxyl-terminal cysteine residues
    • Clarke 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
    • Clarke, S.1
  • 16
    • 0033735850 scopus 로고    scopus 로고
    • Functional implications of protein isoprenylation in plants
    • Crowell D.N. Functional implications of protein isoprenylation in plants. Prog. Lipid Res. 39 (2000) 393-408
    • (2000) Prog. Lipid Res. , vol.39 , pp. 393-408
    • Crowell, D.N.1
  • 17
    • 0035036576 scopus 로고    scopus 로고
    • Identification and functional expression in yeast of a prenylcysteine α-carboxyl methyltransferase gene from Arabidopsis thaliana
    • Crowell D.N., and Kennedy M. Identification and functional expression in yeast of a prenylcysteine α-carboxyl methyltransferase gene from Arabidopsis thaliana. Plant Mol. Biol. 45 (2001) 469-476
    • (2001) Plant Mol. Biol. , vol.45 , pp. 469-476
    • Crowell, D.N.1    Kennedy, M.2
  • 18
    • 0000457145 scopus 로고    scopus 로고
    • Prenylcysteine α-carboxyl methyltransferase in suspension-cultured tobacco cells
    • Crowell D.N., Sen S.E., and Randall S.K. Prenylcysteine α-carboxyl methyltransferase in suspension-cultured tobacco cells. Plant Physiol. 118 (1998) 115-123
    • (1998) Plant Physiol. , vol.118 , pp. 115-123
    • Crowell, D.N.1    Sen, S.E.2    Randall, S.K.3
  • 19
    • 0028897903 scopus 로고
    • Fractionation and characterization of protein C-terminal prenylcysteine methylesterase activities from rabbit brain
    • Dunten R.L., Wait S.J., and Backlund P.S.J. Fractionation and characterization of protein C-terminal prenylcysteine methylesterase activities from rabbit brain. Biochem. Biophys. Res. Commun. 208 (1995) 174-182
    • (1995) Biochem. Biophys. Res. Commun. , vol.208 , pp. 174-182
    • Dunten, R.L.1    Wait, S.J.2    Backlund, P.S.J.3
  • 20
    • 0025277259 scopus 로고
    • Prenyl proteins in eukaryotic cells: a new type of membrane anchor
    • Glomset J.A., Gelb M.H., and Farnsworth C.C. Prenyl proteins in eukaryotic cells: a new type of membrane anchor. Trends Biochem. Sci. 15 (1990) 139-142
    • (1990) Trends Biochem. Sci. , vol.15 , pp. 139-142
    • Glomset, J.A.1    Gelb, M.H.2    Farnsworth, C.C.3
  • 21
    • 0024465343 scopus 로고
    • Post-translational processing of p21ras is two-step and involves carboxyl-methylation and carboxy-terminal proteolysis
    • Gutierrez L., Magee A.I., Marshall C.J., and Hancock J.F. Post-translational processing of p21ras is two-step and involves carboxyl-methylation and carboxy-terminal proteolysis. EMBO J. 8 (1989) 1093-1098
    • (1989) EMBO J. , vol.8 , pp. 1093-1098
    • Gutierrez, L.1    Magee, A.I.2    Marshall, C.J.3    Hancock, J.F.4
  • 22
    • 0024406286 scopus 로고
    • All ras proteins are polyisoprenylated but only some are palmitoylated
    • Hancock J.F., Magee A.I., Childs J.E., and Marshall C.J. All ras proteins are polyisoprenylated but only some are palmitoylated. Cell 57 (1989) 1167-1177
    • (1989) Cell , vol.57 , pp. 1167-1177
    • Hancock, J.F.1    Magee, A.I.2    Childs, J.E.3    Marshall, C.J.4
  • 23
    • 0026021456 scopus 로고
    • Methylation and proteolysis are essential for efficient membrane binding of prenylated p21K-ras(B)
    • Hancock J.F., Cadwallader K., and Marshall C.J. Methylation and proteolysis are essential for efficient membrane binding of prenylated p21K-ras(B). EMBO J. 10 (1991) 641-646
    • (1991) EMBO J. , vol.10 , pp. 641-646
    • Hancock, J.F.1    Cadwallader, K.2    Marshall, C.J.3
  • 24
    • 0025764049 scopus 로고
    • The Saccharomyces cerevisiae STE14 gene encodes a methyltransferase that mediates C-terminal methylation of a-factor and RAS proteins
    • Hrycyna C.A., Sapperstein S.K., Clarke S., and Michaelis S. The Saccharomyces cerevisiae STE14 gene encodes a methyltransferase that mediates C-terminal methylation of a-factor and RAS proteins. EMBO J. 10 (1991) 1699-1709
    • (1991) EMBO J. , vol.10 , pp. 1699-1709
    • Hrycyna, C.A.1    Sapperstein, S.K.2    Clarke, S.3    Michaelis, S.4
  • 25
    • 0027430757 scopus 로고
    • Isoprenylation mediates direct protein-protein interactions between hepatitis large delta antigen and hepatitis B virus surface antigen
    • Hwang S.B., and Lai M.M. Isoprenylation mediates direct protein-protein interactions between hepatitis large delta antigen and hepatitis B virus surface antigen. J. Virol. 67 (1993) 7659-7662
    • (1993) J. Virol. , vol.67 , pp. 7659-7662
    • Hwang, S.B.1    Lai, M.M.2
  • 26
    • 0033605596 scopus 로고    scopus 로고
    • Disruption of the mouse Rce1 gene results in defective Ras processing and mislocalization of Ras within cells
    • Kim E., et al. Disruption of the mouse Rce1 gene results in defective Ras processing and mislocalization of Ras within cells. J. Biol. Chem. 274 (1999) 8383-8390
    • (1999) J. Biol. Chem. , vol.274 , pp. 8383-8390
    • Kim, E.1
  • 27
    • 0028093624 scopus 로고
    • A farnesylated domain in the G protein γ subunit is a specific determinant of receptor coupling
    • Kisselev O.G., Ermolaeva M.V., and Gautam N. A farnesylated domain in the G protein γ subunit is a specific determinant of receptor coupling. J. Biol. Chem. 269 (1994) 21399-21402
    • (1994) J. Biol. Chem. , vol.269 , pp. 21399-21402
    • Kisselev, O.G.1    Ermolaeva, M.V.2    Gautam, N.3
  • 28
    • 0027500533 scopus 로고
    • The effect of posttranslational modifications on the interaction of Ras2 with adenylyl cyclase
    • Kuroda Y., Suzuki N., and Kataoka T. The effect of posttranslational 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
  • 29
    • 27844576132 scopus 로고    scopus 로고
    • Liver prenylated methylated protein methyl esterase is an organophosphate-sensitive enzyme
    • Lamango N.S. Liver prenylated methylated protein methyl esterase is an organophosphate-sensitive enzyme. J. Biochem. Mol. Toxicol. 19 (2005) 347-357
    • (2005) J. Biochem. Mol. Toxicol. , vol.19 , pp. 347-357
    • Lamango, N.S.1
  • 30
    • 0035878127 scopus 로고    scopus 로고
    • Inactivation of AtRac1 by abscisic acid is essential for stomatal closure
    • Lemichez E., Wu Y., Sanchez J.P., Mettouchi A., Mathur J., and Chua N.H. Inactivation of AtRac1 by abscisic acid is essential for stomatal closure. Genes Dev. 15 (2001) 1808-1816
    • (2001) Genes Dev. , vol.15 , pp. 1808-1816
    • Lemichez, E.1    Wu, Y.2    Sanchez, J.P.3    Mettouchi, A.4    Mathur, J.5    Chua, N.H.6
  • 31
    • 0035800833 scopus 로고    scopus 로고
    • Biochemical studies of Zmpste24-deficient mice
    • Leung G.K., et al. Biochemical studies of Zmpste24-deficient mice. J. Biol. Chem. 276 (2001) 29051-29058
    • (2001) J. Biol. Chem. , vol.276 , pp. 29051-29058
    • Leung, G.K.1
  • 32
    • 0034973617 scopus 로고    scopus 로고
    • The Rop GTPase switch controls multiple developmental processes in Arabidopsis
    • Li H., Shen J.J., Zheng Z.L., Lin Y., and Yang Z. The Rop GTPase switch controls multiple developmental processes in Arabidopsis. Plant Physiol. 126 (2001) 670-684
    • (2001) Plant Physiol. , vol.126 , pp. 670-684
    • Li, H.1    Shen, J.J.2    Zheng, Z.L.3    Lin, Y.4    Yang, Z.5
  • 33
    • 0027284950 scopus 로고
    • Protein prenylation: a mediator of protein-protein interactions
    • Marshall C.J. Protein prenylation: a mediator of protein-protein interactions. Science 259 (1993) 1865-1866
    • (1993) Science , vol.259 , pp. 1865-1866
    • Marshall, C.J.1
  • 34
    • 16344396081 scopus 로고    scopus 로고
    • Postprenylation CAAX processing is required for proper localization of Ras but not Rho GTPases
    • Michaelson D., et al. Postprenylation CAAX processing is required for proper localization of Ras but not Rho GTPases. Mol. Biol. Cell 16 (2005) 1606-1616
    • (2005) Mol. Biol. Cell , vol.16 , pp. 1606-1616
    • Michaelson, D.1
  • 35
    • 0036578920 scopus 로고    scopus 로고
    • Defective prelamin A processing and muscular and adipocyte alterations in Zmpste24 metalloproteinase-deficient mice
    • Pendás A.M., et al. Defective prelamin A processing and muscular and adipocyte alterations in Zmpste24 metalloproteinase-deficient mice. Nat. Genet. 31 (2002) 94-99
    • (2002) Nat. Genet. , vol.31 , pp. 94-99
    • Pendás, A.M.1
  • 36
    • 0026346215 scopus 로고
    • Methylation and demethylation reactions of guanine nucleotide-binding proteins of retinal rod outer segments
    • Pérez-Sala D., Tan E.W., Cañada F.J., and Rando R.R. Methylation and demethylation reactions of guanine nucleotide-binding proteins of retinal rod outer segments. Proc. Natl. Acad. Sci. U. S. A. 88 (1991) 3043-3046
    • (1991) Proc. Natl. Acad. Sci. U. S. A. , vol.88 , pp. 3043-3046
    • Pérez-Sala, D.1    Tan, E.W.2    Cañada, F.J.3    Rando, R.R.4
  • 37
    • 0028122345 scopus 로고
    • Prenylation of Ras proteins is required for efficient hSOS1-promoted guanine nucleotide exchange
    • Porfiri E., Evans T., Chardin P., and Hancock J.F. Prenylation of Ras proteins is required for efficient hSOS1-promoted guanine nucleotide exchange. J. Biol. Chem. 269 (1994) 22672-22677
    • (1994) J. Biol. Chem. , vol.269 , pp. 22672-22677
    • Porfiri, E.1    Evans, T.2    Chardin, P.3    Hancock, J.F.4
  • 38
    • 0034490131 scopus 로고    scopus 로고
    • Carboxyl-methylation of prenylated calmodulin CaM53 is required for efficient plasma membrane targeting of the protein
    • Rodríguez-Concepción M., Toledo-Ortiz G., Yalovsky S., Caldelari D., and Gruissem W. Carboxyl-methylation of prenylated calmodulin CaM53 is required for efficient plasma membrane targeting of the protein. Plant J. 24 (2000) 775-784
    • (2000) Plant J. , vol.24 , pp. 775-784
    • Rodríguez-Concepción, M.1    Toledo-Ortiz, G.2    Yalovsky, S.3    Caldelari, D.4    Gruissem, W.5
  • 39
    • 0028125792 scopus 로고
    • Nucleotide sequence of the yeast STE14 gene, which encodes farnesylcysteine carboxyl methyltransferase, and demonstration of its essential role in a-factor export
    • Sapperstein S., Berkower C., and Michaelis S. Nucleotide sequence of the yeast STE14 gene, which encodes farnesylcysteine 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
  • 40
    • 0031874938 scopus 로고    scopus 로고
    • Dual roles for Ste24p in yeast a-factor maturation: NH2-terminal proteolysis and COOH-terminal CAAX processing
    • Tam A., Nouvet F.J., Fujimura-Kamada K., Slunt H., Sisodia S.S., and Michaelis S. Dual roles for Ste24p in yeast a-factor maturation: NH2-terminal proteolysis and COOH-terminal CAAX processing. J. Cell Biol. 142 (1998) 635-649
    • (1998) J. Cell Biol. , vol.142 , pp. 635-649
    • Tam, A.1    Nouvet, F.J.2    Fujimura-Kamada, K.3    Slunt, H.4    Sisodia, S.S.5    Michaelis, S.6
  • 41
    • 0026740602 scopus 로고
    • Identification of an isoprenylated cysteine methyl ester hydrolase activity in bovine rod outer segment membranes
    • Tan E.W., and Rando R.R. Identification of an isoprenylated cysteine methyl ester hydrolase activity in bovine rod outer segment membranes. Biochemistry 31 (1992) 5572-5578
    • (1992) Biochemistry , vol.31 , pp. 5572-5578
    • Tan, E.W.1    Rando, R.R.2
  • 42
    • 0034815797 scopus 로고    scopus 로고
    • On the occurrence of multiple isoprenylated cysteine methyl ester hydrolase activities in bovine adrenal medulla
    • Van Dessel G.A., De Busser H.M., and Lagrou A.R. On the occurrence of multiple isoprenylated cysteine methyl ester hydrolase activities in bovine adrenal medulla. Biochem. Biophys. Res. Commun. 284 (2001) 50-56
    • (2001) Biochem. Biophys. Res. Commun. , vol.284 , pp. 50-56
    • Van Dessel, G.A.1    De Busser, H.M.2    Lagrou, A.R.3
  • 43
    • 0025375466 scopus 로고
    • Brain G protein γ subunits contain an all-trans-geranylgeranylcysteine methyl ester at their carboxyl termini
    • Yamane H.K., et al. Brain G protein γ subunits contain an all-trans-geranylgeranylcysteine methyl ester at their carboxyl termini. Proc. Natl. Acad. Sci. U. S. A. 87 (1990) 5868-5872
    • (1990) Proc. Natl. Acad. Sci. U. S. A. , vol.87 , pp. 5868-5872
    • Yamane, H.K.1
  • 44
    • 0029898894 scopus 로고    scopus 로고
    • Protein prenylation: molecular mechanisms and functional consequences
    • Zhang F.L., and Casey P.J. Protein prenylation: molecular mechanisms and functional consequences. Annu. Rev. Biochem. 65 (1996) 241-269
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 241-269
    • Zhang, F.L.1    Casey, P.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.