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Volumn 11, Issue 2, 2012, Pages 1228-1239

Phosphoproteome exploration reveals a reformatting of cellular processes in response to low sterol biosynthetic capacity in Arabidopsis

Author keywords

Arabidopsis thaliana; growth; HMGR; phosphoproteomics; regulation; sterol

Indexed keywords

ACYL COENZYME A; HYDROXYMETHYLGLUTARYL COENZYME A REDUCTASE; PHOSPHOPEPTIDE; PHOSPHOPROTEOME; PHYTOSTEROL; PROTEOME; STEROL; UNCLASSIFIED DRUG;

EID: 84863052507     PISSN: 15353893     EISSN: 15353907     Source Type: Journal    
DOI: 10.1021/pr201127u     Document Type: Article
Times cited : (10)

References (79)
  • 1
    • 77954308993 scopus 로고    scopus 로고
    • Increased leaf size: Different means to an end
    • Gonzalez, N. Increased leaf size: different means to an end Plant Physiol. 2010, 153, 1261-1279
    • (2010) Plant Physiol. , vol.153 , pp. 1261-1279
    • Gonzalez, N.1
  • 2
    • 77953199770 scopus 로고    scopus 로고
    • High-affinity manganese uptake by the metal transporter NRAMP1 is essential for Arabidopsis growth in low manganese conditions
    • Cailliatte, R.; Schikora, A.; Briat, J. F.; Mari, S.; Curie, C. High-affinity manganese uptake by the metal transporter NRAMP1 is essential for Arabidopsis growth in low manganese conditions Plant Cell 2010, 22, 904-917
    • (2010) Plant Cell , vol.22 , pp. 904-917
    • Cailliatte, R.1    Schikora, A.2    Briat, J.F.3    Mari, S.4    Curie, C.5
  • 3
    • 0028505013 scopus 로고
    • The terpenoid theory of the origin of cellular life: The evolution of terpenoids to cholesterol
    • Ourisson, G.; Nakatani, Y. The terpenoid theory of the origin of cellular life: the evolution of terpenoids to cholesterol Chem. Biol. 1994, 1, 11-23
    • (1994) Chem. Biol. , vol.1 , pp. 11-23
    • Ourisson, G.1    Nakatani, Y.2
  • 5
    • 42949147070 scopus 로고    scopus 로고
    • Allelic mutant series reveal distinct functions for Arabidopsis cycloartenol synthase 1 in cell viability and plastid biogenesis
    • Babiychuk, E. Allelic mutant series reveal distinct functions for Arabidopsis cycloartenol synthase 1 in cell viability and plastid biogenesis Proc. Natl. Acad. Sci. U.S.A. 2008, 105, 3163-3168
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 3163-3168
    • Babiychuk, E.1
  • 6
    • 0034028486 scopus 로고    scopus 로고
    • 7-reductase gene of Arabidopsis cause dwarfism due to a block in brassinosteroid biosynthesis
    • 7-reductase gene of Arabidopsis cause dwarfism due to a block in brassinosteroid biosynthesis Plant J. 2000, 21, 431-443
    • (2000) Plant J. , vol.21 , pp. 431-443
    • Choe, S.1
  • 7
    • 4644225477 scopus 로고    scopus 로고
    • Rescue of defective auxin-mediated gene expression and root meristem function by inhibition of ethylene signalling in sterol biosynthesis mutants of Arabidopsis
    • Souter, M. A.; Pullen, M. L.; Topping, J. F.; Zhang, X.; Lindsey, K. Rescue of defective auxin-mediated gene expression and root meristem function by inhibition of ethylene signalling in sterol biosynthesis mutants of Arabidopsis Planta 2004, 219, 773-783
    • (2004) Planta , vol.219 , pp. 773-783
    • Souter, M.A.1    Pullen, M.L.2    Topping, J.F.3    Zhang, X.4    Lindsey, K.5
  • 8
  • 9
    • 0842334768 scopus 로고    scopus 로고
    • Distinct light-mediated pathways regulate the biosynthesis and exchange of isoprenoid precursors during Arabidopsis seedling development
    • Rodríguez-Concepción, M. Distinct light-mediated pathways regulate the biosynthesis and exchange of isoprenoid precursors during Arabidopsis seedling development Plant Cell 2004, 16, 144-156
    • (2004) Plant Cell , vol.16 , pp. 144-156
    • Rodríguez-Concepción, M.1
  • 10
    • 0030088045 scopus 로고    scopus 로고
    • Light suppresses 3-hydroxy-3-methyl-glutaryl-coenzyme A reductase gene expression in Arabidopsis thaliana
    • Learned, R. M. Light suppresses 3-hydroxy-3-methyl-glutaryl-coenzyme A reductase gene expression in Arabidopsis thaliana Plant Physiol. 1996, 110, 645-655
    • (1996) Plant Physiol. , vol.110 , pp. 645-655
    • Learned, R.M.1
  • 11
    • 34249811510 scopus 로고    scopus 로고
    • Plant sterols in 'rafts': A better way to regulate membrane thermal shocks
    • Beck, J. G.; Mathieu, D.; Loudet, C.; Buchoux, S.; Dufourc, E. J. Plant sterols in 'rafts': a better way to regulate membrane thermal shocks FASEB J. 2007, 21, 1714-1723
    • (2007) FASEB J. , vol.21 , pp. 1714-1723
    • Beck, J.G.1    Mathieu, D.2    Loudet, C.3    Buchoux, S.4    Dufourc, E.J.5
  • 12
    • 56449097008 scopus 로고    scopus 로고
    • Insig regulates HMG-CoA reductase by controlling enzyme phosphorylation in fission yeast
    • Burg, J. S.; Powell, D. W.; Chai, R.; Hughes, A. L.; Link, A. J.; Espenshade, P. J. Insig regulates HMG-CoA reductase by controlling enzyme phosphorylation in fission yeast Cell Metab. 2008, 8, 522-531
    • (2008) Cell Metab. , vol.8 , pp. 522-531
    • Burg, J.S.1    Powell, D.W.2    Chai, R.3    Hughes, A.L.4    Link, A.J.5    Espenshade, P.J.6
  • 13
    • 79960983285 scopus 로고    scopus 로고
    • Glucose Controls Phosphoregulation of Hydroxymethylglutaryl Coenzyme A Reductase through the Protein Phosphatase 2A-related Phosphatase Protein, Ppe1, and Insig in Fission Yeast
    • Burg, J. S.; Espenshade, P. J. Glucose Controls Phosphoregulation of Hydroxymethylglutaryl Coenzyme A Reductase through the Protein Phosphatase 2A-related Phosphatase Protein, Ppe1, and Insig in Fission Yeast J. Biol. Chem. 2011, 286, 27139-27146
    • (2011) J. Biol. Chem. , vol.286 , pp. 27139-27146
    • Burg, J.S.1    Espenshade, P.J.2
  • 14
    • 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. 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, 506-513
    • (1995) Eur. J. Biochem. , vol.233 , pp. 506-513
    • Dale, S.1
  • 15
    • 0036740929 scopus 로고    scopus 로고
    • Inhibition of squalene synthase and squalene epoxidase in tobacco cells triggers an up-regulation of 3-hydroxy-3-methylglutaryl coenzyme a reductase
    • Wentzinger, L. F.; Bach, T. J.; Hartmann, M. A. Inhibition of squalene synthase and squalene epoxidase in tobacco cells triggers an up-regulation of 3-hydroxy-3-methylglutaryl coenzyme a reductase Plant Physiol. 2002, 130, 334-346
    • (2002) Plant Physiol. , vol.130 , pp. 334-346
    • Wentzinger, L.F.1    Bach, T.J.2    Hartmann, M.A.3
  • 16
    • 61449116914 scopus 로고    scopus 로고
    • Ortho-proteogenomics: Multiple proteomes investigation through orthology and a new MS-based protocol
    • Gallien, S. Ortho-proteogenomics: multiple proteomes investigation through orthology and a new MS-based protocol Genome Res. 2009, 19, 128-135
    • (2009) Genome Res. , vol.19 , pp. 128-135
    • Gallien, S.1
  • 17
    • 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. 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, 750-761
    • (2004) Plant J. , vol.37 , pp. 750-761
    • Suzuki, M.1
  • 18
    • 1842504609 scopus 로고    scopus 로고
    • A novel high efficiency, low maintenance, hydroponic system for synchronous growth and flowering of Arabidopsis thaliana
    • Tocquin, P. A novel high efficiency, low maintenance, hydroponic system for synchronous growth and flowering of Arabidopsis thaliana BMC Plant Biol. 2003, 30, 3(2)
    • (2003) BMC Plant Biol. , vol.30 , pp. 32
    • Tocquin, P.1
  • 19
    • 79952450613 scopus 로고    scopus 로고
    • Driving biochemical discovery with quantitative proteomics
    • Washburn, M. Driving biochemical discovery with quantitative proteomics Trends Biochem. Sci. 2011, 36, 170-177
    • (2011) Trends Biochem. Sci. , vol.36 , pp. 170-177
    • Washburn, M.1
  • 20
    • 84988119829 scopus 로고
    • Quantitation of microgram amounts of protein in two-dimensional polyacrylamide gel electrophoresis sample buffer
    • Ramagli, L. S.; Rodriguez, L. V. Quantitation of microgram amounts of protein in two-dimensional polyacrylamide gel electrophoresis sample buffer Electrophoresis 1985, 6, 559-563
    • (1985) Electrophoresis , vol.6 , pp. 559-563
    • Ramagli, L.S.1    Rodriguez, L.V.2
  • 21
    • 2342518184 scopus 로고    scopus 로고
    • An efficient protocol for the identification of protein phosphorylation in a seedless plant, sensitive enough to detect members of signalling cascades
    • Heintz, D. An efficient protocol for the identification of protein phosphorylation in a seedless plant, sensitive enough to detect members of signalling cascades Electrophoresis 2004, 25, 1149-1159
    • (2004) Electrophoresis , vol.25 , pp. 1149-1159
    • Heintz, D.1
  • 22
    • 33748301955 scopus 로고    scopus 로고
    • Rapid alteration of the phosphoproteome in the moss Physcomitrella patens after cytokinin treatment
    • Heintz, D. Rapid alteration of the phosphoproteome in the moss Physcomitrella patens after cytokinin treatment J. Proteome Res. 2006, 5, 2283-2293
    • (2006) J. Proteome Res. , vol.5 , pp. 2283-2293
    • Heintz, D.1
  • 23
    • 33845757588 scopus 로고    scopus 로고
    • Global metabolic changes following loss of a feedback loop reveal dynamic steady states of the yeast metabolome
    • Lu, P.; Rangan, A.; Chan, S. Y.; Appling, D. R.; Hoffman, D. W.; Marcotte, E. M. Global metabolic changes following loss of a feedback loop reveal dynamic steady states of the yeast metabolome Metab. Eng. 2007, 9, 8-20
    • (2007) Metab. Eng. , vol.9 , pp. 8-20
    • Lu, P.1    Rangan, A.2    Chan, S.Y.3    Appling, D.R.4    Hoffman, D.W.5    Marcotte, E.M.6
  • 24
    • 33846165487 scopus 로고    scopus 로고
    • Absolute protein expression profiling estimates the relative contributions of transcriptional and translational regulation
    • Lu, P.; Vogel, C.; Wang, R.; Yao, X.; Marcotte, E. M. Absolute protein expression profiling estimates the relative contributions of transcriptional and translational regulation Nat. Biotechnol. 2007b, 25, 117-124
    • (2007) Nat. Biotechnol. , vol.25 , pp. 117-124
    • Lu, P.1    Vogel, C.2    Wang, R.3    Yao, X.4    Marcotte, E.M.5
  • 25
    • 44449097260 scopus 로고    scopus 로고
    • The proteomic response of Mycobacterium smegmatis to anti-tuberculosis drugs suggests targeted pathways
    • Wang, R.; Marcotte, E. M. The proteomic response of Mycobacterium smegmatis to anti-tuberculosis drugs suggests targeted pathways J. Proteome Res. 2008, 7, 855-865
    • (2008) J. Proteome Res. , vol.7 , pp. 855-865
    • Wang, R.1    Marcotte, E.M.2
  • 26
    • 70449579978 scopus 로고    scopus 로고
    • Differential membrane proteome analysis reveals novel proteins involved in the degradation of aromatic compounds in Geobacter metallireducens
    • Heintz, D. Differential membrane proteome analysis reveals novel proteins involved in the degradation of aromatic compounds in Geobacter metallireducens Mol. Cell. Proteomics 2009, 8, 2159-2169
    • (2009) Mol. Cell. Proteomics , vol.8 , pp. 2159-2169
    • Heintz, D.1
  • 27
    • 66249123951 scopus 로고    scopus 로고
    • Complete blockage of the mevalonate pathway results in male gametophyte lethality
    • Suzuki, M. Complete blockage of the mevalonate pathway results in male gametophyte lethality J. Exp. Bot. 2009, 60, 2055-2064
    • (2009) J. Exp. Bot. , vol.60 , pp. 2055-2064
    • Suzuki, M.1
  • 28
    • 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. (Tokyo) 2007, 55, 1518-1521
    • (2007) Chem. Pharm. Bull. (Tokyo) , vol.55 , pp. 1518-1521
    • Ohyama, K.1    Suzuki, M.2    Masuda, K.3    Yoshida, S.4    Muranaka, T.5
  • 29
    • 58149299336 scopus 로고    scopus 로고
    • Significance analysis of spectral count data in label-free shotgun proteomics
    • Choi, H.; Fermin, D.; Nesvizhskii, A. I. Significance analysis of spectral count data in label-free shotgun proteomics Mol. Cell. Proteomics 2008, 7, 2373-238
    • (2008) Mol. Cell. Proteomics , vol.7 , pp. 2373-238
    • Choi, H.1    Fermin, D.2    Nesvizhskii, A.I.3
  • 30
    • 79956149039 scopus 로고    scopus 로고
    • Quantitative label-free phosphoproteomics strategy for multifaceted experimental designs
    • Soderblom, E. J.; Phillip, M.; Thomson, J. W.; Caron, M. G.; Moseley, M. A. Quantitative label-free phosphoproteomics strategy for multifaceted experimental designs Anal. Chem. 2011, 83, 3758-3764
    • (2011) Anal. Chem. , vol.83 , pp. 3758-3764
    • Soderblom, E.J.1    Phillip, M.2    Thomson, J.W.3    Caron, M.G.4    Moseley, M.A.5
  • 31
    • 66649127498 scopus 로고    scopus 로고
    • Large-scale Arabidopsis phosphoproteome profiling reveals novel chloroplast kinase substrates and phosphorylation networks
    • Reiland, S. Large-scale Arabidopsis phosphoproteome profiling reveals novel chloroplast kinase substrates and phosphorylation networks Plant Physiol. 2009, 150, 889-903
    • (2009) Plant Physiol. , vol.150 , pp. 889-903
    • Reiland, S.1
  • 32
    • 33845500104 scopus 로고    scopus 로고
    • Quantitative proteomics analysis of the secretorypathway
    • Gilchrist, A. Quantitative proteomics analysis of the secretorypathway Cell 2006, 127, 1265-1281
    • (2006) Cell , vol.127 , pp. 1265-1281
    • Gilchrist, A.1
  • 33
    • 32544450674 scopus 로고    scopus 로고
    • Structural mechanism of plant aquaporin gating
    • Törnroth-Horsefield, S. Structural mechanism of plant aquaporin gating Nature 2006, 439, 688-694
    • (2006) Nature , vol.439 , pp. 688-694
    • Törnroth-Horsefield, S.1
  • 34
    • 46749099449 scopus 로고    scopus 로고
    • Multiple phosphorylations in the C-terminal tail of plant plasma membrane aquaporins: Role in subcellular trafficking of AtPIP2;1 in response to salt stress
    • Prak, S. Multiple phosphorylations in the C-terminal tail of plant plasma membrane aquaporins: role in subcellular trafficking of AtPIP2;1 in response to salt stress Mol. Cell. Proteomics 2008, 7, 1019-1030
    • (2008) Mol. Cell. Proteomics , vol.7 , pp. 1019-1030
    • Prak, S.1
  • 35
    • 77957682118 scopus 로고    scopus 로고
    • In planta changes in protein phosphorylation induced by the plant hormone abscisic acid
    • Kline, K. G.; Barrett-Wilt, G. A.; Sussman, M. R. In planta changes in protein phosphorylation induced by the plant hormone abscisic acid Proc. Natl. Acad. Sci. U.S.A. 2010, 107, 15986-15991
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 15986-15991
    • Kline, K.G.1    Barrett-Wilt, G.A.2    Sussman, M.R.3
  • 36
    • 35648996970 scopus 로고    scopus 로고
    • Temporal analysis of sucrose-induced phosphorylation changes in plasma membrane proteins of Arabidopsis
    • Niittylä, T.; Fuglsang, A. T.; Palmgren, M. G.; Frommer, W. B.; Schulze, W. X. Temporal analysis of sucrose-induced phosphorylation changes in plasma membrane proteins of Arabidopsis Mol. Cell. Proteomics 2007, 6, 1711-1726
    • (2007) Mol. Cell. Proteomics , vol.6 , pp. 1711-1726
    • Niittylä, T.1    Fuglsang, A.T.2    Palmgren, M.G.3    Frommer, W.B.4    Schulze, W.X.5
  • 37
    • 70249134972 scopus 로고    scopus 로고
    • CHL1 functions as a nitrate sensor in plants
    • Ho, C. H.; Lin, S. H.; Hu, H. C.; Tsay, Y. F. CHL1 functions as a nitrate sensor in plants Cell 2009, 138, 1184-1194
    • (2009) Cell , vol.138 , pp. 1184-1194
    • Ho, C.H.1    Lin, S.H.2    Hu, H.C.3    Tsay, Y.F.4
  • 38
    • 0037416191 scopus 로고    scopus 로고
    • Switching between the two action modes of the dual-affinity nitrate transporter CHL1 by phosphorylation
    • Liu, K. H.; Tsay, Y. F. Switching between the two action modes of the dual-affinity nitrate transporter CHL1 by phosphorylation EMBO J. 2003, 22, 1005-1013
    • (2003) EMBO J. , vol.22 , pp. 1005-1013
    • Liu, K.H.1    Tsay, Y.F.2
  • 39
    • 34848831773 scopus 로고    scopus 로고
    • Novel subsets of the Arabidopsis plasmalemma phosphoproteome identify phosphorylation sites in secondary active transporters
    • Hem, S.; Rofidal, V.; Sommerer, N.; Rossignol, M. Novel subsets of the Arabidopsis plasmalemma phosphoproteome identify phosphorylation sites in secondary active transporters Biochem. Biophys. Res. Commun. 2007, 363, 375-380
    • (2007) Biochem. Biophys. Res. Commun. , vol.363 , pp. 375-380
    • Hem, S.1    Rofidal, V.2    Sommerer, N.3    Rossignol, M.4
  • 40
    • 34248193815 scopus 로고    scopus 로고
    • Nitrate transporters and peptide transporters
    • Tsay, Y. F. Nitrate transporters and peptide transporters FEBS Lett. 2007, 581, 2290-2300
    • (2007) FEBS Lett. , vol.581 , pp. 2290-2300
    • Tsay, Y.F.1
  • 41
    • 77954396706 scopus 로고    scopus 로고
    • The Arabidopsis nitrate transporter NRT1.8 functions in nitrate removal from the xylem sap and mediates cadmium tolerance
    • Li, J. Y. The Arabidopsis nitrate transporter NRT1.8 functions in nitrate removal from the xylem sap and mediates cadmium tolerance Plant Cell 2010, 22, 1633-1646
    • (2010) Plant Cell , vol.22 , pp. 1633-1646
    • Li, J.Y.1
  • 42
    • 33750546025 scopus 로고    scopus 로고
    • Additive contribution of AMT1;1 and AMT1;3 to high-affinity ammonium uptake across the plasma membrane of nitrogen-deficient Arabidopsis roots
    • Loqué, D. Additive contribution of AMT1;1 and AMT1;3 to high-affinity ammonium uptake across the plasma membrane of nitrogen-deficient Arabidopsis roots Plant J. 2006, 48, 522-534
    • (2006) Plant J. , vol.48 , pp. 522-534
    • Loqué, D.1
  • 43
    • 73249131234 scopus 로고    scopus 로고
    • Feedback inhibition of ammonium uptake by a phospho-dependent allosteric mechanism in Arabidopsis
    • Lanquar, V. Feedback inhibition of ammonium uptake by a phospho-dependent allosteric mechanism in Arabidopsis Plant Cell 2009, 11, 3610-3622
    • (2009) Plant Cell , vol.11 , pp. 3610-3622
    • Lanquar, V.1
  • 44
    • 77954291457 scopus 로고    scopus 로고
    • The acidic A-domain of Arabidopsis TOC159 occurs as a hyperphosphorylated protein
    • Agne, B. The acidic A-domain of Arabidopsis TOC159 occurs as a hyperphosphorylated protein Plant Physiol. 2010, 15, 1016-1030
    • (2010) Plant Physiol. , vol.15 , pp. 1016-1030
    • Agne, B.1
  • 46
    • 77952916753 scopus 로고    scopus 로고
    • Molecular characterization of mutant Arabidopsis plants with reduced plasma membrane proton pump activity
    • Haruta, M. Molecular characterization of mutant Arabidopsis plants with reduced plasma membrane proton pump activity J. Biol. Chem. 2010, 285, 17918-17929
    • (2010) J. Biol. Chem. , vol.285 , pp. 17918-17929
    • Haruta, M.1
  • 48
    • 71449105949 scopus 로고    scopus 로고
    • 2+-ATPase of Arabidopsis thaliana, generate partially deregulated pumps
    • 2+-ATPase of Arabidopsis thaliana, generate partially deregulated pumps J. Biol. Chem. 2009, 284, 30881-30888
    • (2009) J. Biol. Chem. , vol.284 , pp. 30881-30888
    • Fusca, T.1
  • 49
    • 34250183058 scopus 로고    scopus 로고
    • Phototropin blue-light receptors
    • Christie, J. M. Phototropin blue-light receptors Annu. Rev. Plant Biol. 2007, 58, 21-45
    • (2007) Annu. Rev. Plant Biol. , vol.58 , pp. 21-45
    • Christie, J.M.1
  • 50
    • 54349124106 scopus 로고    scopus 로고
    • Molecular basis of the functional specificities of phototropin 1 and 2
    • Aihara, Y.; Tabata, R.; Suzuki, T.; Shimazaki, K.; Nagatani, A. Molecular basis of the functional specificities of phototropin 1 and 2 Plant J. 2008, 56, 364-375
    • (2008) Plant J. , vol.56 , pp. 364-375
    • Aihara, Y.1    Tabata, R.2    Suzuki, T.3    Shimazaki, K.4    Nagatani, A.5
  • 51
    • 47849128479 scopus 로고    scopus 로고
    • In vivo phosphorylation site mapping and functional characterization of Arabidopsis phototropin 1
    • Sullivan, S.; Thomson, C. E.; Lamont, D. J.; Jones, M. A.; Christie, J. M. In vivo phosphorylation site mapping and functional characterization of Arabidopsis phototropin 1 Mol.r Plant 2008, 1, 178-194
    • (2008) Mol.r Plant , vol.1 , pp. 178-194
    • Sullivan, S.1    Thomson, C.E.2    Lamont, D.J.3    Jones, M.A.4    Christie, J.M.5
  • 52
    • 44449166482 scopus 로고    scopus 로고
    • Blue light-induced autophosphorylation of phototropin is a primary step for signaling
    • Inoue, S. Blue light-induced autophosphorylation of phototropin is a primary step for signaling Proc. Natl. Acad. Sci. U.S.A. 2008, 105, 5626-5631
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 5626-5631
    • Inoue, S.1
  • 54
    • 0032125091 scopus 로고    scopus 로고
    • Role of a COP1 interactive protein in mediating light-regulated gene expression in Arabidopsis
    • Yamamoto, Y.; Matsui, M.; Ang, L. H.; Deng, X. W. Role of a COP1 interactive protein in mediating light-regulated gene expression in Arabidopsis Plant Cell 1998, 10, 1083-1091
    • (1998) Plant Cell , vol.10 , pp. 1083-1091
    • Yamamoto, Y.1    Matsui, M.2    Ang, L.H.3    Deng, X.W.4
  • 55
    • 54049112625 scopus 로고    scopus 로고
    • A novel protein phosphatase indirectly regulates phytochrome-interacting factor 3 via phytochrome
    • Phee, B. K. A novel protein phosphatase indirectly regulates phytochrome-interacting factor 3 via phytochrome Biochem. J. 2008, 415, 247-255
    • (2008) Biochem. J. , vol.415 , pp. 247-255
    • Phee, B.K.1
  • 56
    • 79957689735 scopus 로고    scopus 로고
    • Multilevel control of Arabidopsis 3-hydroxy-3-methymglutarylCoenzyme A reductase by Phosphatase 2A
    • Leivar, P. Multilevel control of Arabidopsis 3-hydroxy-3- methymglutarylCoenzyme A reductase by Phosphatase 2A Plant Cell 2011, 23, 1494-1511
    • (2011) Plant Cell , vol.23 , pp. 1494-1511
    • Leivar, P.1
  • 57
    • 0035542782 scopus 로고    scopus 로고
    • Cryptochrome 1, cryptochrome 2, and phytochrome a co-activate the chloroplast psbD blue light-responsive promoter
    • Thum, K. E.; Kim, M.; Christopher, D. A.; Mullet, J. E. Cryptochrome 1, cryptochrome 2, and phytochrome a co-activate the chloroplast psbD blue light-responsive promoter Plant Cell 2001, 13, 2747-2760
    • (2001) Plant Cell , vol.13 , pp. 2747-2760
    • Thum, K.E.1    Kim, M.2    Christopher, D.A.3    Mullet, J.E.4
  • 58
    • 0031587034 scopus 로고    scopus 로고
    • Stabilization of photosystem two dimers by phosphorylation: Implication for the regulation of the turnover of D1 protein
    • Kruse, O.; Zheleva, D.; Barber, J. Stabilization of photosystem two dimers by phosphorylation: implication for the regulation of the turnover of D1 protein FEBS Lett. 1997, 408, 276-280
    • (1997) FEBS Lett. , vol.408 , pp. 276-280
    • Kruse, O.1    Zheleva, D.2    Barber, J.3
  • 59
    • 0035831456 scopus 로고    scopus 로고
    • Mass spectrometric resolution of reversible protein phosphorylation in photosynthetic membranes of Arabidopsis thaliana
    • Vener, A. V.; Harms, A.; Sussman, M. R.; Vierstra, R. D. Mass spectrometric resolution of reversible protein phosphorylation in photosynthetic membranes of Arabidopsis thaliana J. Biol. Chem. 2001, 276, 6959-6966
    • (2001) J. Biol. Chem. , vol.276 , pp. 6959-6966
    • Vener, A.V.1    Harms, A.2    Sussman, M.R.3    Vierstra, R.D.4
  • 60
    • 1842546738 scopus 로고    scopus 로고
    • Identification of three previously unknown in vivo protein phosphorylation sites in thylakoid membranes of Arabidopsis thaliana
    • Hansson, M.; Vener, A. V. Identification of three previously unknown in vivo protein phosphorylation sites in thylakoid membranes of Arabidopsis thaliana Mol. Cell. Proteomics 2003, 2, 550-559
    • (2003) Mol. Cell. Proteomics , vol.2 , pp. 550-559
    • Hansson, M.1    Vener, A.V.2
  • 61
    • 0032792264 scopus 로고    scopus 로고
    • Characterization of mutants with alterations of the phosphorylation site in the D2 photosystem II polypeptide of chlamydomonas reinhardtii
    • Fleischmann, M. M.; Rochaix, J. D. Characterization of mutants with alterations of the phosphorylation site in the D2 photosystem II polypeptide of chlamydomonas reinhardtii Plant Physiol. 1999, 19, 1557-1566
    • (1999) Plant Physiol. , vol.19 , pp. 1557-1566
    • Fleischmann, M.M.1    Rochaix, J.D.2
  • 62
    • 17544404364 scopus 로고    scopus 로고
    • Evaluation and classification of RING-finger domains encoded by the Arabidopsis genome
    • (RESEARCH0016
    • Kosarev, P.; Mayer, K. F.; Hardtke, C. S. Evaluation and classification of RING-finger domains encoded by the Arabidopsis genome Genome Biol. 2002, 3 (4 RESEARCH0016
    • (2002) Genome Biol. , vol.3 , Issue.4
    • Kosarev, P.1    Mayer, K.F.2    Hardtke, C.S.3
  • 63
    • 0038377588 scopus 로고    scopus 로고
    • The Arabidopsis CDPK-SnRK superfamily of protein kinases
    • Hrabak, E. M. The Arabidopsis CDPK-SnRK superfamily of protein kinases Plant Physiol. 2003, 132, 666-680
    • (2003) Plant Physiol. , vol.132 , pp. 666-680
    • Hrabak, E.M.1
  • 64
    • 16744362946 scopus 로고    scopus 로고
    • Using mutant alleles to determine the structure and function of leucine-rich repeat receptor-like kinases
    • Dievart, A.; Clark, S. E. Using mutant alleles to determine the structure and function of leucine-rich repeat receptor-like kinases Curr. Opin. Plant Biol. 2003, 6, 507-516
    • (2003) Curr. Opin. Plant Biol. , vol.6 , pp. 507-516
    • Dievart, A.1    Clark, S.E.2
  • 66
    • 41049083912 scopus 로고    scopus 로고
    • Over-expression of an arabidopsis family A sucrose phosphate synthase (SPS) gene alters plant growth and fibre development
    • Park, J. Y.; Canam, T.; Kang, K. Y.; Ellis, D. D.; Mansfield, S. D. Over-expression of an arabidopsis family A sucrose phosphate synthase (SPS) gene alters plant growth and fibre development Transgenic Res. 2008, 17, 181-192
    • (2008) Transgenic Res. , vol.17 , pp. 181-192
    • Park, J.Y.1    Canam, T.2    Kang, K.Y.3    Ellis, D.D.4    Mansfield, S.D.5
  • 67
    • 0026090386 scopus 로고
    • In vitro phosphorylation and inactivation of spinach leaf sucrose-phosphate synthase by an endogenous protein kinase
    • Huber, S. C.; Huber, J. L. In vitro phosphorylation and inactivation of spinach leaf sucrose-phosphate synthase by an endogenous protein kinase Biochim. Biophys. Acta: Mol. Cell Res. 1991, 1091, 393-400
    • (1991) Biochim. Biophys. Acta: Mol. Cell Res. , vol.1091 , pp. 393-400
    • Huber, S.C.1    Huber, J.L.2
  • 68
    • 29144521559 scopus 로고    scopus 로고
    • An integrated strategy for identification and relative quantification of site-specific protein phosphorylation using liquid chromatography coupled to MS(2)/MS(3)
    • Wolschin, F.; Lehmann, U.; Glinski, M.; Weckwerth, W. An integrated strategy for identification and relative quantification of site-specific protein phosphorylation using liquid chromatography coupled to MS(2)/MS(3) Rapid Commun. Mass Spectrom. 2005, 19, 3626-3623
    • (2005) Rapid Commun. Mass Spectrom. , vol.19 , pp. 3626-3623
    • Wolschin, F.1    Lehmann, U.2    Glinski, M.3    Weckwerth, W.4
  • 69
    • 0033134243 scopus 로고    scopus 로고
    • Two SNF1-related protein kinases from spinach leaf phosphorylate and inactivate 3-hydroxy-3-methylglutaryl-coenzyme A reductase, nitrate reductase, and sucrose phosphate synthase in vitro
    • Sugden, C.; Donaghy, P. G.; Halford, N. G.; Grahame Hardie, D. Two SNF1-related protein kinases from spinach leaf phosphorylate and inactivate 3-hydroxy-3-methylglutaryl-coenzyme A reductase, nitrate reductase, and sucrose phosphate synthase in vitro Plant Physiol. 1999, 120, 257-274
    • (1999) Plant Physiol. , vol.120 , pp. 257-274
    • Sugden, C.1    Donaghy, P.G.2    Halford, N.G.3    Grahame Hardie, D.4
  • 70
    • 78049243938 scopus 로고    scopus 로고
    • Mutations of cellulose synthase (CESA1) phosphorylation sites modulate anisotropic cell expansion and bidirectional mobility of cellulose synthase
    • Chen, S.; Ehrhardt, D. W.; Somerville, C. R. Mutations of cellulose synthase (CESA1) phosphorylation sites modulate anisotropic cell expansion and bidirectional mobility of cellulose synthase Proc. Natl. Acad Sci. U.S.A. 2010, 107, 17188-17193
    • (2010) Proc. Natl. Acad Sci. U.S.A. , vol.107 , pp. 17188-17193
    • Chen, S.1    Ehrhardt, D.W.2    Somerville, C.R.3
  • 71
    • 0033197621 scopus 로고    scopus 로고
    • The gain-of-function Arabidopsis acd6 mutant reveals novel regulation and function of the salicylic acid signaling pathway in controlling cell death, defenses, and cell growth
    • Rate, D. N.; Cuenca, J. V.; Bowman, G. R.; Guttman, D. S.; Greenberg, J. T. The gain-of-function Arabidopsis acd6 mutant reveals novel regulation and function of the salicylic acid signaling pathway in controlling cell death, defenses, and cell growth Plant Cell 1999, 11, 1695-1708
    • (1999) Plant Cell , vol.11 , pp. 1695-1708
    • Rate, D.N.1    Cuenca, J.V.2    Bowman, G.R.3    Guttman, D.S.4    Greenberg, J.T.5
  • 72
    • 33644846447 scopus 로고    scopus 로고
    • Structure-function analysis of the plasma membrane- localized Arabidopsis defense component ACD6
    • Lu, H.; Liu, Y.; Greenberg, J. T. Structure-function analysis of the plasma membrane- localized Arabidopsis defense component ACD6 Plant J. 2005, 44, 798-809
    • (2005) Plant J. , vol.44 , pp. 798-809
    • Lu, H.1    Liu, Y.2    Greenberg, J.T.3
  • 73
    • 77953198418 scopus 로고    scopus 로고
    • Natural allelic variation underlying a major fitness trade-off in Arabidopsis thaliana
    • Todesco, M. Natural allelic variation underlying a major fitness trade-off in Arabidopsis thaliana Nature 2010, 465, 632-636
    • (2010) Nature , vol.465 , pp. 632-636
    • Todesco, M.1
  • 74
    • 34249821366 scopus 로고    scopus 로고
    • Arabidopsis KAM2/GRV2 is required for proper endosome formation and functions in vacuolar sorting and determination of the embryo growth axis
    • Tamura, K. Arabidopsis KAM2/GRV2 is required for proper endosome formation and functions in vacuolar sorting and determination of the embryo growth axis Plant Cell 2007, 19, 320-332
    • (2007) Plant Cell , vol.19 , pp. 320-332
    • Tamura, K.1
  • 75
    • 28844489072 scopus 로고    scopus 로고
    • The DnaJ-domain protein RME-8 functions in endosomal trafficking
    • Girard, M.; Poupon, V.; Blondeau, F.; McPherson, P. S. The DnaJ-domain protein RME-8 functions in endosomal trafficking J. Biol. Chem. 2005, 280, 40135-40143
    • (2005) J. Biol. Chem. , vol.280 , pp. 40135-40143
    • Girard, M.1    Poupon, V.2    Blondeau, F.3    McPherson, P.S.4
  • 76
    • 0034760311 scopus 로고    scopus 로고
    • Identification of a signal that distinguishes between the chloroplast outer envelope membrane and the endomembrane system in vivo
    • Lee, Y. J.; Kim, D. H.; Kim, Y. W.; Hwang, I. Identification of a signal that distinguishes between the chloroplast outer envelope membrane and the endomembrane system in vivo Plant Cell 2001, 13, 2175-2190
    • (2001) Plant Cell , vol.13 , pp. 2175-2190
    • Lee, Y.J.1    Kim, D.H.2    Kim, Y.W.3    Hwang, I.4
  • 77
    • 0029868470 scopus 로고    scopus 로고
    • Phosphorylation of the transit sequence of chloroplast precursor proteins
    • Waegemann, K.; Soll, J. Phosphorylation of the transit sequence of chloroplast precursor proteins J. Biol. Chem. 1996, 271, 6545-6554
    • (1996) J. Biol. Chem. , vol.271 , pp. 6545-6554
    • Waegemann, K.1    Soll, J.2
  • 78
    • 30344486984 scopus 로고    scopus 로고
    • Flotillin-1 defines a clathrin-independent endocytic pathway in mammalian cells
    • Glebov, O. O.; Bright, N. A.; Nichols, B. J. Flotillin-1 defines a clathrin-independent endocytic pathway in mammalian cells Nat. Cell Biol. 2006, 8, 46-54
    • (2006) Nat. Cell Biol. , vol.8 , pp. 46-54
    • Glebov, O.O.1    Bright, N.A.2    Nichols, B.J.3
  • 79
    • 78651268139 scopus 로고    scopus 로고
    • Separating parental environment from seed size effects on next generation growth and development in Arabidopsis
    • Elwell, A. L.; Gronwall, D. S.; Miller, N. D.; Spalding, E. P.; Durham Brooks, T. L. Separating parental environment from seed size effects on next generation growth and development in Arabidopsis Plant Cell Environ. 2011, 34, 291-301
    • (2011) Plant Cell Environ. , vol.34 , pp. 291-301
    • Elwell, A.L.1    Gronwall, D.S.2    Miller, N.D.3    Spalding, E.P.4    Durham Brooks, T.L.5


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