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Volumn 6, Issue 8, 2011, Pages 1127-1131

Modulation of plant HMG-CoA reductase by protein phosphatase 2A, positive and negative control at a key node of metabolism

Author keywords

HMG CoA reductase; HMGR; Isoprenoid biosynthesis; Mevalonate pathway; PP2A; Protein phosphatase 2A; Salt stress

Indexed keywords


EID: 79961182235     PISSN: 15592316     EISSN: 15592324     Source Type: Journal    
DOI: 10.4161/psb.6.8.16363     Document Type: Review
Times cited : (25)

References (65)
  • 1
    • 79961174539 scopus 로고
    • Some properties of 3-hydroxy-3-methylglutaryl coenzyme A reductase from Pisum sativum
    • Brooker JD, Russell DW. Some properties of 3-hydroxy-3-methylglutaryl coenzyme A reductase from Pisum sativum. Roy Soc New Zealand Bull 1974; 12:365-70.
    • (1974) Roy Soc New Zealand Bull , vol.12 , pp. 365-370
    • Brooker, J.D.1    Russell, D.W.2
  • 2
    • 79957689735 scopus 로고    scopus 로고
    • Multilevel control of Arabidopsis 3-hydroxy-3-methylglutaryl coenzyme A reductase by protein phosphatase 2A
    • In press
    • Leivar P, Antolín-Llovera M, Ferrero S, Closa M, Arró M, Ferrer A, et al. Multilevel control of Arabidopsis 3-hydroxy-3-methylglutaryl coenzyme A reductase by protein phosphatase 2A. Plant Cell 2011; 23; In press.
    • (2011) Plant Cell , pp. 23
    • Leivar, P.1    Antolín-Llovera, M.2    Ferrero, S.3    Closa, M.4    Arró, M.5    Ferrer, A.6
  • 4
    • 0028289750 scopus 로고
    • Regulation of HMG-CoA reductase activity in plants
    • Stermer BA, Bianchini GM, Korth KL. Regulation of HMG-CoA reductase activity in plants. J Lipid Res 1994; 35:1133-40.
    • (1994) J Lipid Res , vol.35 , pp. 1133-1140
    • Stermer, B.A.1    Bianchini, G.M.2    Korth, K.L.3
  • 5
    • 33747886506 scopus 로고    scopus 로고
    • Switching the flip: Protein phosphatase roles in signaling pathways
    • DeLong A. Switching the flip: protein phosphatase roles in signaling pathways. Curr Opin Plant Biol 2006; 9:470-7.
    • (2006) Curr Opin Plant Biol , vol.9 , pp. 470-477
    • Delong, A.1
  • 6
    • 0142057022 scopus 로고    scopus 로고
    • Protein phosphatases in plants
    • Luan S. Protein phosphatases in plants. Annu Rev Plant Biol 2003; 54:63-92.
    • (2003) Annu Rev Plant Biol , vol.54 , pp. 63-92
    • Luan, S.1
  • 7
    • 77954053558 scopus 로고    scopus 로고
    • Serine/threonine protein phosphatases type 2A and their roles in stress signaling
    • País SM, Tellez-Iñón MT, Capiati DA. Serine/threonine protein phosphatases type 2A and their roles in stress signaling. Plant Signal Behav 2009; 4:1013-5.
    • (2009) Plant Signal Behav , vol.4 , pp. 1013-1015
    • País, S.M.1    Tellez-Iñón, M.T.2    Capiati, D.A.3
  • 9
    • 0028906885 scopus 로고
    • Some new aspects of isoprenoid biosynthesis in plants-A review
    • Bach TJ. Some new aspects of isoprenoid biosynthesis in plants-A review. Lipids 1995; 30:191-202.
    • (1995) Lipids , vol.30 , pp. 191-202
    • Bach, T.J.1
  • 10
    • 0028837082 scopus 로고
    • Biochemistry and molecular biology of the isoprenoid biosynthetic pathway in plants
    • Chappell J. Biochemistry and molecular biology of the isoprenoid biosynthetic pathway in plants. Annu Rev Plant Physiol Plant Mol Biol 1995; 46:521-47.
    • (1995) Annu Rev Plant Physiol Plant Mol Biol , vol.46 , pp. 521-547
    • Chappell, J.1
  • 11
    • 43549105634 scopus 로고    scopus 로고
    • Terpenoid biomaterials
    • Bohlmann J, Keeling CI. Terpenoid biomaterials. Plant J 2008; 54:656-69.
    • (2008) Plant J , vol.54 , pp. 656-669
    • Bohlmann, J.1    Keeling, C.I.2
  • 12
    • 59049106449 scopus 로고    scopus 로고
    • Arabidopsis 3-hydroxy-3-methylglutaryl-CoA reductase is regulated at the post-translational level in response to alterations of the sphingolipid and the sterol biosynthetic pathways
    • Nieto B, Forés O, Arró M, Ferrer A. Arabidopsis 3-hydroxy-3-methylglutaryl-CoA reductase is regulated at the post-translational level in response to alterations of the sphingolipid and the sterol biosynthetic pathways. Phytochemistry 2009; 70:53-9.
    • (2009) Phytochemistry , vol.70 , pp. 53-59
    • Nieto, B.1    Forés, O.2    Arró, M.3    Ferrer, A.4
  • 13
    • 0028834801 scopus 로고
    • Bacterial expression of the catalytic domain of 3-hydroxy-3-methylglutaryl-CoA reductase (isoform HMGR1) from Arabidopsis thaliana, and its inactivation by phosphorylation at Ser577 by Brassica oleracea 3-hydroxy-3-methylglutaryl-CoA reductase kinase
    • Dale S, Arró M, Becerra B, Morrice NG, Boronat A, Hardie DG, et al. Bacterial expression of the catalytic domain of 3-hydroxy-3-methylglutaryl-CoA reductase (isoform HMGR1) from Arabidopsis thaliana, and its inactivation by phosphorylation at Ser577 by Brassica oleracea 3-hydroxy-3-methylglutaryl-CoA reductase kinase. Eur J Biochem 1995; 233:506-13.
    • (1995) Eur J Biochem , vol.233 , pp. 506-513
    • Dale, S.1    Arró, M.2    Becerra, B.3    Morrice, N.G.4    Boronat, A.5    Hardie, D.G.6
  • 14
    • 0013488609 scopus 로고
    • 2+, and posttranslational control in vivo by phytochrome and isoprenoid hormones
    • In: Randall DD, Blevins DG, Larson RL, Kagawa T, Eds, University of Missouri-Columbia
    • 2+, and posttranslational control in vivo by phytochrome and isoprenoid hormones. In: Randall DD, Blevins DG, Larson RL, Kagawa T, Eds. Current Topics in Plant Biochemistry and Physiology: University of Missouri-Columbia 1985; 191-206.
    • (1985) Current Topics in Plant Biochemistry and Physiology , pp. 191-206
    • Russell, D.W.1    Knight, J.S.2    Wilson, T.M.3
  • 15
    • 0033842934 scopus 로고    scopus 로고
    • Developmental and light-regulated post-translational control of 3-hydroxy-3-methylglutaryl-CoA reductase levels in potato
    • Korth KL, Jaggard DAW, Dixon RA. Developmental and light-regulated post-translational control of 3-hydroxy-3-methylglutaryl-CoA reductase levels in potato. Plant J 2000; 23:507-16.
    • (2000) Plant J , vol.23 , pp. 507-516
    • Korth, K.L.1    Jaggard, D.A.W.2    Dixon, R.A.3
  • 16
    • 0024869502 scopus 로고
    • Isolation and structural characterization of a cDNA encoding Arabidopsis thaliana 3-hydroxy-3-methylglutaryl coenzyme-A reductase
    • Caelles C, Ferrer A, Balcells L, Hegardt FG, Boronat A. Isolation and structural characterization of a cDNA encoding Arabidopsis thaliana 3-hydroxy-3-methylglutaryl coenzyme-A reductase. Plant MolBiol 1989; 13:627-38.
    • (1989) Plant MolBiol , vol.13 , pp. 627-638
    • Caelles, C.1    Ferrer, A.2    Balcells, L.3    Hegardt, F.G.4    Boronat, A.5
  • 17
    • 0028147680 scopus 로고
    • Arabidopsis thaliana contains two differentially expressed 3-hydroxy-3-methylglutaryl-CoA reductase genes, which encode microsomal forms of the enzyme
    • Enjuto M, Balcells L, Campos N, Caelles C, Arró M, Boronat A. Arabidopsis thaliana contains two differentially expressed 3-hydroxy-3-methylglutaryl-CoA reductase genes, which encode microsomal forms of the enzyme. Proc Natl Acad Sci USA 1994; 91:927-31.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 927-931
    • Enjuto, M.1    Balcells, L.2    Campos, N.3    Caelles, C.4    Arró, M.5    Boronat, A.6
  • 19
    • 39149144775 scopus 로고    scopus 로고
    • 3-Hydroxy-3-methylglutaryl coenzyme a reductase 1 interacts with NORK and is crucial for nodulation in Medicago truncatula
    • Kevei Z, Lougnon G, Mergaert P, Horváth GV, Kereszt A, Jayaraman D, et al. 3-Hydroxy-3-methylglutaryl coenzyme a reductase 1 interacts with NORK and is crucial for nodulation in Medicago truncatula. Plant Cell 2007; 19:3974-89.
    • (2007) Plant Cell , vol.19 , pp. 3974-3989
    • Kevei, Z.1    Lougnon, G.2    Mergaert, P.3    Horváth, G.V.4    Kereszt, A.5    Jayaraman, D.6
  • 20
    • 0029379562 scopus 로고
    • The use of an alternative promoter in the Arabidopsis thaliana HMG1 gene generates an mRNA that encodes a novel 3-hydroxy-3-methylglutaryl coenzyme A reductase isoform with an extended N-terminal region
    • Lumbreras V, Campos N, Boronat A. The use of an alternative promoter in the Arabidopsis thaliana HMG1 gene generates an mRNA that encodes a novel 3-hydroxy-3-methylglutaryl coenzyme A reductase isoform with an extended N-terminal region. Plant J 1995; 8:541-9.
    • (1995) Plant J , vol.8 , pp. 541-549
    • Lumbreras, V.1    Campos, N.2    Boronat, A.3
  • 21
    • 0029294034 scopus 로고
    • Expression of the Arabidopsis HMG2 gene, encoding 3-hydroxy-3-methylglutaryl coenzyme A reductase, is restricted to meristematic and floral tissues
    • Enjuto M, Lumbreras V, Marín C, Boronat A. Expression of the Arabidopsis HMG2 gene, encoding 3-hydroxy-3-methylglutaryl coenzyme A reductase, is restricted to meristematic and floral tissues. Plant Cell 1995; 7:517-27.
    • (1995) Plant Cell , vol.7 , pp. 517-527
    • Enjuto, M.1    Lumbreras, V.2    Marín, C.3    Boronat, A.4
  • 22
    • 35648947418 scopus 로고    scopus 로고
    • Chemical phenotypes of the hmg1 and hmg2 mutants of Arabidopsis demonstrate the In-planta role of HMG-CoA reductase in triterpene biosynthesis
    • Ohyama K, Suzuki M, Masuda K, Yoshida S, Muranaka T. Chemical phenotypes of the hmg1 and hmg2 mutants of Arabidopsis demonstrate the In-planta role of HMG-CoA reductase in triterpene biosynthesis. Chem Pharm Bull 2007; 55:1518-21.
    • (2007) Chem Pharm Bull , vol.55 , pp. 1518-1521
    • Ohyama, K.1    Suzuki, M.2    Masuda, K.3    Yoshida, S.4    Muranaka, T.5
  • 23
    • 10744224664 scopus 로고    scopus 로고
    • Loss of function of 3-hydroxy-3-methylglutaryl coenzyme A reductase 1 (HMG1) in Arabidopsis leads to dwarfing, early senescence and male sterility, and reduced sterol levels
    • Suzuki M, Kamide Y, Nagata N, Seki H, Ohyama K, Kato H, et al. Loss of function of 3-hydroxy-3-methylglutaryl coenzyme A reductase 1 (HMG1) in Arabidopsis leads to dwarfing, early senescence and male sterility, and reduced sterol levels. Plant J 2004; 37:750-61.
    • (2004) Plant J , vol.37 , pp. 750-761
    • Suzuki, M.1    Kamide, Y.2    Nagata, N.3    Seki, H.4    Ohyama, K.5    Kato, H.6
  • 24
    • 0029582822 scopus 로고
    • Targeting and topology in the membrane of plant 3-hydroxy-3-methylglutaryl coenzyme A reductase
    • Campos N, Boronat A. Targeting and topology in the membrane of plant 3-hydroxy-3-methylglutaryl coenzyme A reductase. Plant Cell 1995; 7:2163-74.
    • (1995) Plant Cell , vol.7 , pp. 2163-2174
    • Campos, N.1    Boronat, A.2
  • 27
    • 0035252894 scopus 로고    scopus 로고
    • Protein phosphatase 2A: A highly regulated family of serine/threonine phosphatases implicated in cell-growth and signalling
    • Janssens V, Goris J. Protein phosphatase 2A: a highly regulated family of serine/threonine phosphatases implicated in cell-growth and signalling. Biochem J 2001; 353:417-39.
    • (2001) Biochem J , vol.353 , pp. 417-439
    • Janssens, V.1    Goris, J.2
  • 28
    • 0035100658 scopus 로고    scopus 로고
    • Protein phosphatase 2A: The trojan horse of cellular signaling
    • Sontag E. Protein phosphatase 2A: the trojan horse of cellular signaling. Cell Signal 2001; 13:7-16.
    • (2001) Cell Signal , vol.13 , pp. 7-16
    • Sontag, E.1
  • 29
    • 0034009389 scopus 로고    scopus 로고
    • Protein phosphatase 2A: A panoply of enzymes
    • Virshup DM. Protein phosphatase 2A: a panoply of enzymes. Curr Opin Cell Biol 2000; 12:180-5.
    • (2000) Curr Opin Cell Biol , vol.12 , pp. 180-185
    • Virshup, D.M.1
  • 30
    • 79551592014 scopus 로고    scopus 로고
    • PP2A activates brassinosteroid-responsive gene expression and plant growth by dephosphorylating BZR1
    • Tang W, Yuan M, Wang R, Yang Y, Wang C, Oses-Prieto JA, et al. PP2A activates brassinosteroid-responsive gene expression and plant growth by dephosphorylating BZR1. Nat Cell Biol 2011; 13:124-31.
    • (2011) Nat Cell Biol , vol.13 , pp. 124-131
    • Tang, W.1    Yuan, M.2    Wang, R.3    Yang, Y.4    Wang, C.5    Oses-Prieto, J.A.6
  • 31
    • 0024971161 scopus 로고
    • Identification of high-levels of type 1 and type 2A protein phosphatases in higher plants
    • MacKintosh C, Cohen P. Identification of high-levels of type 1 and type 2A protein phosphatases in higher plants. Biochem J 1989; 262:335-9.
    • (1989) Biochem J , vol.262 , pp. 335-339
    • Mackintosh, C.1    Cohen, P.2
  • 32
    • 0024991575 scopus 로고
    • Sucrose-phosphate synthase is dephosphorylated by protein phosphatase 2A in spinach leaves. Evidence from the effects of okadaic acid and microcystin
    • Siegl G, Mackintosh C, Stitt M. Sucrose-phosphate synthase is dephosphorylated by protein phosphatase 2A in spinach leaves. Evidence from the effects of okadaic acid and microcystin. FEBS Lett 1990; 270:198-202.
    • (1990) FEBS Lett , vol.270 , pp. 198-202
    • Siegl, G.1    Mackintosh, C.2    Stitt, M.3
  • 33
    • 0026059954 scopus 로고
    • Plant protein phosphatases. Subcellular distribution, detection of protein phosphatase 2C and identification of protein phosphatase 2A as the major quinate dehydrogenase phosphatase
    • MacKintosh C, Coggins J, Cohen P. Plant protein phosphatases. Subcellular distribution, detection of protein phosphatase 2C and identification of protein phosphatase 2A as the major quinate dehydrogenase phosphatase. Biochem J 1991; 273:733-8.
    • (1991) Biochem J , vol.273 , pp. 733-738
    • Mackintosh, C.1    Coggins, J.2    Cohen, P.3
  • 34
    • 0026768507 scopus 로고
    • Regulation of spinach leaf nitrate reductase by reversible phosphorylation
    • MacKintosh C. Regulation of spinach leaf nitrate reductase by reversible phosphorylation. Biochim Biophys Acta 1992; 1137:121-6.
    • (1992) Biochim Biophys Acta , vol.1137 , pp. 121-126
    • Mackintosh, C.1
  • 36
    • 33645821031 scopus 로고    scopus 로고
    • A cDNA microarray approach to decipher sunflower (Helianthus annuus) responses to the necrotrophic fungus Phoma macdonaldii
    • Alignan M, Hewezi T, Petitprez M, Dechamp-Guillaume G, Gentzbittel L. A cDNA microarray approach to decipher sunflower (Helianthus annuus) responses to the necrotrophic fungus Phoma macdonaldii. New Phytol 2006; 170:523-36.
    • (2006) New Phytol , vol.170 , pp. 523-536
    • Alignan, M.1    Hewezi, T.2    Petitprez, M.3    Dechamp-Guillaume, G.4    Gentzbittel, L.5
  • 37
    • 2542584746 scopus 로고    scopus 로고
    • Silencing of subfamily I of protein phosphatase 2A catalytic subunits results in activation of plant defense responses and localized cell death
    • He XH, Anderson JC, del Pozo O, Gu YQ, Tang XY, Martin GB. Silencing of subfamily I of protein phosphatase 2A catalytic subunits results in activation of plant defense responses and localized cell death. Plant J 2004; 38:563-77.
    • (2004) Plant J , vol.38 , pp. 563-577
    • He, X.H.1    Anderson, J.C.2    del Pozo, O.3    Gu, Y.Q.4    Tang, X.Y.5    Martin, G.B.6
  • 38
    • 0036845182 scopus 로고    scopus 로고
    • Comprehensive transcript profiling of Pto- and Prf-mediated host defense responses to infection by Pseudomonas syringae pv. tomato
    • Mysore KS, Crasta OR, Tuori RP, Folkerts O, Swirsky PB, Martin GB. Comprehensive transcript profiling of Pto- and Prf-mediated host defense responses to infection by Pseudomonas syringae pv. tomato. Plant J 2002; 32:299-315.
    • (2002) Plant J , vol.32 , pp. 299-315
    • Mysore, K.S.1    Crasta, O.R.2    Tuori, R.P.3    Folkerts, O.4    Swirsky, P.B.5    Martin, G.B.6
  • 39
    • 67349099067 scopus 로고    scopus 로고
    • Characterization of potato (Solanum tuberosum) and tomato (Solanum lycopersicum) protein phosphatases type 2A catalytic subunits and their involvement in stress responses
    • País SM, González MA, Téllez-Iñón MT, Capiati DA. Characterization of potato (Solanum tuberosum) and tomato (Solanum lycopersicum) protein phosphatases type 2A catalytic subunits and their involvement in stress responses. Planta 2009; 230:13-25.
    • (2009) Planta , vol.230 , pp. 13-25
    • País, S.M.1    González, M.A.2    Téllez-Iñón, M.T.3    Capiati, D.A.4
  • 40
    • 0001091973 scopus 로고
    • Molecular cloning and characterization of genes related to chilling tolerance in rice
    • Binh LT, Oono K. Molecular cloning and characterization of genes related to chilling tolerance in rice. Plant Physiol 1992; 99:1146-50.
    • (1992) Plant Physiol , vol.99 , pp. 1146-1150
    • Binh, L.T.1    Oono, K.2
  • 41
    • 0033213260 scopus 로고    scopus 로고
    • The Arabidopsis homolog of yeast TAP42 and mammalian a4 binds to the catalytic subunit of protein phosphatase 2A and is induced by chilling
    • Harris DM, Myrick TL, Rundle SJ. The Arabidopsis homolog of yeast TAP42 and mammalian a4 binds to the catalytic subunit of protein phosphatase 2A and is induced by chilling. Plant Physiol 1999; 121:609-17.
    • (1999) Plant Physiol , vol.121 , pp. 609-617
    • Harris, D.M.1    Myrick, T.L.2    Rundle, S.J.3
  • 42
    • 0033558124 scopus 로고    scopus 로고
    • Molecular characterization of the B' regulatory subunit gene family of Arabidopsis protein phosphatase 2A
    • Haynes JG, Hartung AJ, Hendershot JD, III, Passingham RS, Rundle SJ. Molecular characterization of the B' regulatory subunit gene family of Arabidopsis protein phosphatase 2A. Eur J Biochem 1999; 260:127-36.
    • (1999) Eur J Biochem , vol.260 , pp. 127-136
    • Haynes, J.G.1    Hartung, A.J.2    Hendershot III, J.D.3    Passingham, R.S.4    Rundle, S.J.5
  • 43
    • 0030934317 scopus 로고    scopus 로고
    • Differential expression of three Arabidopsis genes encoding the B' regulatory subunit of protein phosphatase 2A
    • Latorre KA, Harris DM, Rundle SJ. Differential expression of three Arabidopsis genes encoding the B' regulatory subunit of protein phosphatase 2A. Eur J Biochem 1997; 245:156-63.
    • (1997) Eur J Biochem , vol.245 , pp. 156-163
    • Latorre, K.A.1    Harris, D.M.2    Rundle, S.J.3
  • 45
    • 34247862150 scopus 로고    scopus 로고
    • A wheat (Triticum aestivum) protein phosphatase 2A catalytic subunit gene provides enhanced drought tolerance in tobacco
    • Xu C, Jing R, Mao X, Jia X, Chang X. A wheat (Triticum aestivum) protein phosphatase 2A catalytic subunit gene provides enhanced drought tolerance in tobacco. Ann Bot 2007; 99:439-50.
    • (2007) Ann Bot , vol.99 , pp. 439-450
    • Xu, C.1    Jing, R.2    Mao, X.3    Jia, X.4    Chang, X.5
  • 46
    • 27844447043 scopus 로고    scopus 로고
    • Structure, evolution and expression of a second subfamily of protein phosphatase 2A catalytic subunit genes in the rice plant (Oryza sativa L.)
    • Yu RM, Wong MM, Jack RW, Kong RY. Structure, evolution and expression of a second subfamily of protein phosphatase 2A catalytic subunit genes in the rice plant (Oryza sativa L.). Planta 2005; 222:757-68.
    • (2005) Planta , vol.222 , pp. 757-768
    • Yu, R.M.1    Wong, M.M.2    Jack, R.W.3    Kong, R.Y.4
  • 47
    • 0037322201 scopus 로고    scopus 로고
    • Two genes encoding protein phosphatase 2A catalytic subunits are differentially expressed in rice
    • Yu RMK, Zhou Y, Xu ZF, Chye ML, Kong RYC. Two genes encoding protein phosphatase 2A catalytic subunits are differentially expressed in rice. Plant MolBiol 2003; 51:295-311.
    • (2003) Plant MolBiol , vol.51 , pp. 295-311
    • Yu, R.M.K.1    Zhou, Y.2    Xu, Z.F.3    Chye, M.L.4    Kong, R.Y.C.5
  • 48
    • 0036846816 scopus 로고    scopus 로고
    • Disruption of a guard cell-expressed protein phosphatase 2A regulatory subunit, RCN1, confers abscisic-acid insensitivity in Arabidopsis
    • Kwak JM, Moon JH, Murata Y, Kuchitsu K, Leonhardt N, Delong A, et al. Disruption of a guard cell-expressed protein phosphatase 2A regulatory subunit, RCN1, confers abscisic-acid insensitivity in Arabidopsis. Plant Cell 2002; 14:2849-61.
    • (2002) Plant Cell , vol.14 , pp. 2849-2861
    • Kwak, J.M.1    Moon, J.H.2    Murata, Y.3    Kuchitsu, K.4    Leonhardt, N.5    Delong, A.6
  • 49
    • 33646252495 scopus 로고    scopus 로고
    • AtCHIP functions as an E3 ubiquitin ligase of protein phosphatase 2A subunits and alters plant response to abscisic acid treatment
    • Luo J, Shen G, Yan J, He C, Zhang H. AtCHIP functions as an E3 ubiquitin ligase of protein phosphatase 2A subunits and alters plant response to abscisic acid treatment. Plant J 2006; 46:649-57.
    • (2006) Plant J , vol.46 , pp. 649-657
    • Luo, J.1    Shen, G.2    Yan, J.3    He, C.4    Zhang, H.5
  • 50
    • 34548131222 scopus 로고    scopus 로고
    • A protein phosphatase 2A catalytic subunit is a negative regulator of abscisic acid signalling
    • Pernas M, Garcia-Casado G, Rojo E, Solano R, Sanchez-Serrano JJ. A protein phosphatase 2A catalytic subunit is a negative regulator of abscisic acid signalling. Plant J 2007; 51:763-78.
    • (2007) Plant J , vol.51 , pp. 763-778
    • Pernas, M.1    Garcia-Casado, G.2    Rojo, E.3    Solano, R.4    Sanchez-Serrano, J.J.5
  • 51
    • 0038806442 scopus 로고    scopus 로고
    • Enhanced ethylene responsiveness in the Arabidopsis eer1 mutant results from a lossof- function mutation in the protein phosphatase 2A A regulatory subunit
    • Larsen PB, Cancel JD. Enhanced ethylene responsiveness in the Arabidopsis eer1 mutant results from a lossof- function mutation in the protein phosphatase 2A A regulatory subunit, RCN1. Plant J 2003; 34:709-18.
    • (2003) RCN1. Plant J , vol.34 , pp. 709-718
    • Larsen, P.B.1    Cancel, J.D.2
  • 52
    • 79955632307 scopus 로고    scopus 로고
    • Protein phosphatase 2A controls ethylene biosynthesis by differentially regulating the turnover of ACC synthase isoforms
    • Skottke KR, Yoon GM, Kieber JJ, Delong A. Protein phosphatase 2A controls ethylene biosynthesis by differentially regulating the turnover of ACC synthase isoforms. PLoS Genet 2011; 7:1001370.
    • (2011) PLoS Genet , vol.7 , pp. 1001370
    • Skottke, K.R.1    Yoon, G.M.2    Kieber, J.J.3    Delong, A.4
  • 53
    • 0031956098 scopus 로고    scopus 로고
    • Low-temperature signal transduction during cold acclimation: Protein phosphatase 2A as an early target for cold-inactivation
    • Monroy AF, Sangwan V, Dhindsa RS. Low-temperature signal transduction during cold acclimation: protein phosphatase 2A as an early target for cold-inactivation. Plant J 1998; 13:653-60.
    • (1998) Plant J , vol.13 , pp. 653-660
    • Monroy, A.F.1    Sangwan, V.2    Dhindsa, R.S.3
  • 54
    • 38949214828 scopus 로고    scopus 로고
    • Specificity of RCN1-mediated protein phosphatase 2A regulation in meristem organization and stress response in roots
    • Blakeslee JJ, Zhou HW, Heath JT, Skottke KR, Rodríguez-Barrios JA, Liu SY, et al. Specificity of RCN1-mediated protein phosphatase 2A regulation in meristem organization and stress response in roots. Plant Physiol 2008; 146:539-53.
    • (2008) Plant Physiol , vol.146 , pp. 539-553
    • Blakeslee, J.J.1    Zhou, H.W.2    Heath, J.T.3    Skottke, K.R.4    Rodríguez-Barrios, J.A.5    Liu, S.Y.6
  • 55
    • 1542752539 scopus 로고    scopus 로고
    • Disparate roles for the regulatory A subunit isoforms in Arabidopsis protein phosphatase 2A
    • Zhou HW, Nussbaumer C, Chao Y, DeLong A. Disparate roles for the regulatory A subunit isoforms in Arabidopsis protein phosphatase 2A. Plant Cell 2004; 16:709-22.
    • (2004) Plant Cell , vol.16 , pp. 709-722
    • Zhou, H.W.1    Nussbaumer, C.2    Chao, Y.3    Delong, A.4
  • 56
    • 0029940505 scopus 로고    scopus 로고
    • A mutation in protein phosphatase 2A regulatory subunit A affects auxin transport in Arabidopsis
    • Garbers C, DeLong A, Deruère J, Bernasconi P, Söll D. A mutation in protein phosphatase 2A regulatory subunit A affects auxin transport in Arabidopsis. EMBO J 1996; 15:2115-24.
    • (1996) EMBO J , vol.15 , pp. 2115-2124
    • Garbers, C.1    Delong, A.2    Deruère, J.3    Bernasconi, P.4    Söll, D.5
  • 57
    • 34548606390 scopus 로고    scopus 로고
    • Antagonistic regulation of PIN phosphorylation by PP2A and PINOID directs auxin flux
    • Michniewicz M, Zago MK, Abas L, Weijers D, Schweighofer A, Meskiene I, et al. Antagonistic regulation of PIN phosphorylation by PP2A and PINOID directs auxin flux. Cell 2007; 130:1044-56.
    • (2007) Cell , vol.130 , pp. 1044-1056
    • Michniewicz, M.1    Zago, M.K.2    Abas, L.3    Weijers, D.4    Schweighofer, A.5    Meskiene, I.6
  • 58
    • 77950361848 scopus 로고    scopus 로고
    • The Arabidopsis rcn1-1 mutation impairs dephosphorylation of phot2, resulting in enhanced blue light responses
    • Tseng TS, Briggs WR. The Arabidopsis rcn1-1 mutation impairs dephosphorylation of phot2, resulting in enhanced blue light responses. Plant Cell 2010; 22:392-402.
    • (2010) Plant Cell , vol.22 , pp. 392-402
    • Tseng, T.S.1    Briggs, W.R.2
  • 59
    • 0035999371 scopus 로고    scopus 로고
    • The Arabidopsis TONNEAU2 gene encodes a putative novel protein phosphatase 2A regulatory subunit essential for the control of the cortical cytoskeleton
    • Camilleri C, Azimzadeh J, Pastuglia M, Bellini C, Grandjean O, Bouchez D. The Arabidopsis TONNEAU2 gene encodes a putative novel protein phosphatase 2A regulatory subunit essential for the control of the cortical cytoskeleton. Plant Cell 2002; 14:833-45.
    • (2002) Plant Cell , vol.14 , pp. 833-845
    • Camilleri, C.1    Azimzadeh, J.2    Pastuglia, M.3    Bellini, C.4    Grandjean, O.5    Bouchez, D.6
  • 60
    • 33745198422 scopus 로고    scopus 로고
    • Calcium in plant defence-signalling pathways
    • Lecourieux D, Raneva R, Pugin A. Calcium in plant defence-signalling pathways. New Phytol 2006; 171:249-69.
    • (2006) New Phytol , vol.171 , pp. 249-269
    • Lecourieux, D.1    Raneva, R.2    Pugin, A.3
  • 62
    • 0037698100 scopus 로고    scopus 로고
    • Cross-talk between the cytosolic mevalonate and the plastidial methylerythritol phosphate pathways in tobacco Bright Yellow-2 cells
    • Hemmerlin A, Hoeffler JF, Meyer O, Tritsch D, Kagan IA, Grosdemange-Billiard C, et al. Cross-talk between the cytosolic mevalonate and the plastidial methylerythritol phosphate pathways in tobacco Bright Yellow-2 cells. J Biol Chem 2003; 278:26666-76.
    • (2003) J Biol Chem , vol.278 , pp. 26666-26676
    • Hemmerlin, A.1    Hoeffler, J.F.2    Meyer, O.3    Tritsch, D.4    Kagan, I.A.5    Grosdemange-Billiard, C.6
  • 63
    • 0026134666 scopus 로고
    • Differential activation of potato 3-hydroxy-3-methylglutaryl coenzyme A reductase genes by wounding and pathogen challenge
    • Yang ZB, Park HS, Lacy GH, Cramer CL. Differential activation of potato 3-hydroxy-3-methylglutaryl coenzyme A reductase genes by wounding and pathogen challenge. Plant Cell 1991; 3:397-405.
    • (1991) Plant Cell , vol.3 , pp. 397-405
    • Yang, Z.B.1    Park, H.S.2    Lacy, G.H.3    Cramer, C.L.4
  • 64
    • 0343384765 scopus 로고
    • Effect of auxin on the metabolism of mevalonic acid in suspension-cultured carrot cells
    • Nishi A, Tsuritani I. Effect of auxin on the metabolism of mevalonic acid in suspension-cultured carrot cells. Phytochemistry 1983; 22:399-401.
    • (1983) Phytochemistry , vol.22 , pp. 399-401
    • Nishi, A.1    Tsuritani, I.2
  • 65
    • 0020037115 scopus 로고
    • Regulation of cytosolic HMG-CoA reductase activity in pea seedlings: Contrasting responses to different hormones and hormoneproduct interaction, suggest hormonal modulation of activity
    • Russell DW, Davidson H. Regulation of cytosolic HMG-CoA reductase activity in pea seedlings: contrasting responses to different hormones and hormoneproduct interaction, suggest hormonal modulation of activity. Biochem Biophys Res Commun 1982; 104:1537-43.
    • (1982) Biochem Biophys Res Commun , vol.104 , pp. 1537-1543
    • Russell, D.W.1    Davidson, H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.