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Volumn 51, Issue 3, 2004, Pages 635-647

Characterization of dual specificity protein kinase from maize seedlings

Author keywords

Dual specificity kinase; Maize; Tyrosine phosphorylation

Indexed keywords

AMINO ACID; CASEIN; ENOLASE; HEPARIN; HISTONE; MYELIN; MYELIN BASIC PROTEIN; PHOSPHOTYROSINE; POLYLYSINE; PROTEIN KINASE; PROTEIN KINASE INHIBITOR; PROTEIN TYROSINE KINASE; SERINE; STAUROSPORINE; TYROSINE;

EID: 4644279970     PISSN: 0001527X     EISSN: None     Source Type: Journal    
DOI: 10.18388/abp.2004_3549     Document Type: Article
Times cited : (8)

References (48)
  • 1
    • 0025049134 scopus 로고
    • Control of Src kinase activity by activators inhibitors and substrate chaperones
    • Abdel-Ghany M, El-Gendy K, Zhang S, Racker E. (1990) Control of Src kinase activity by activators inhibitors and substrate chaperones. Proc Natl Acad Sci USA.; 87: 7061-5.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 7061-7065
    • Abdel-Ghany, M.1    El-Gendy, K.2    Zhang, S.3    Racker, E.4
  • 3
    • 0028007154 scopus 로고
    • Cloning and biochemical characterization of a plant protein kinase that phosphorylates serine threonine and tyrosine
    • Ali N, Halfter U, Chua N-H. (1994) Cloning and biochemical characterization of a plant protein kinase that phosphorylates serine threonine and tyrosine. J Biol Chem.; 269: 31626-9.
    • (1994) J Biol Chem , vol.269 , pp. 31626-31629
    • Ali, N.1    Halfter, U.2    Chua, N.-H.3
  • 5
    • 0033010766 scopus 로고    scopus 로고
    • Evidence suggesting protein tyrosine phosphorylation in plants depends on the developmental conditions
    • Barizza E, Schiavo FL, Terzi M, Filippini F. (1999) Evidence suggesting protein tyrosine phosphorylation in plants depends on the developmental conditions. FEBS Lett.; 447: 191-4.
    • (1999) FEBS Lett , vol.447 , pp. 191-194
    • Barizza, E.1    Schiavo, F.L.2    Terzi, M.3    Filippini, F.4
  • 6
    • 0027740079 scopus 로고
    • Biochemical properties of a novel 28 kD protein tyrosine kinase partially purified from the particulate fraction of rat spleen
    • Borowski P, Medem S, Laufs R. (1993) Biochemical properties of a novel 28 kD protein tyrosine kinase partially purified from the particulate fraction of rat spleen. Biochem Biophys Res Commun.; 197: 646-53.
    • (1993) Biochem Biophys Res Commun , vol.197 , pp. 646-653
    • Borowski, P.1    Medem, S.2    Laufs, R.3
  • 7
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem.; 72: 248-54.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 8
    • 0042695811 scopus 로고    scopus 로고
    • Ethylene signaling: The MAPK module has finally landed
    • Chang C. (2003) Ethylene signaling: the MAPK module has finally landed. Trends Plant Sci.; 8: 365-8.
    • (2003) Trends Plant Sci , vol.8 , pp. 365-368
    • Chang, C.1
  • 9
    • 0020983488 scopus 로고
    • Detection and quantification of phosphotyrosine in proteins
    • Cooper JA, Sefton BM, Hunter T. (1983) Detection and quantification of phosphotyrosine in proteins. Methods Enzymol.; 99: 387-402.
    • (1983) Methods Enzymol , vol.99 , pp. 387-402
    • Cooper, J.A.1    Sefton, B.M.2    Hunter, T.3
  • 10
    • 17344362761 scopus 로고    scopus 로고
    • Signaling by dual specificity kinases
    • Dhanasekaran N, Reddy EP. (1998) Signaling by dual specificity kinases. Oncogene.; 17: 1447-55.
    • (1998) Oncogene , vol.17 , pp. 1447-1455
    • Dhanasekaran, N.1    Reddy, E.P.2
  • 11
    • 0021092862 scopus 로고
    • Influence of transformation by Rous sarcoma virus on the amount phosphorylation and enzyme kinetic properties of enolase
    • Eigenbrodt E, Fister P, Rübsamen H, Friis RR. (1983) Influence of transformation by Rous sarcoma virus on the amount phosphorylation and enzyme kinetic properties of enolase. EMBO J.; 2: 1565-70.
    • (1983) EMBO J , vol.2 , pp. 1565-1570
    • Eigenbrodt, E.1    Fister, P.2    Rübsamen, H.3    Friis, R.R.4
  • 12
    • 0021810224 scopus 로고
    • Identification of products of proteins phosphorylation in T37-transformed cells and comparison with normal cells
    • Elliot DC, Geytenbeek M. (1985) Identification of products of proteins phosphorylation in T37-transformed cells and comparison with normal cells. Biochim Biophys Acta.; 845: 317-23.
    • (1985) Biochim Biophys Acta , vol.845 , pp. 317-323
    • Elliot, D.C.1    Geytenbeek, M.2
  • 13
    • 0343621499 scopus 로고    scopus 로고
    • European Union Arabidopsis Genome Sequencing Consortium and The Cold Spring Harbor Washington University in St. Louis and PE Biosystems Arabidopsis Sequencing Consortium (1999) Nature.; 402: 769-77.
    • (1999) Nature , vol.402 , pp. 769-777
  • 14
    • 0022596409 scopus 로고
    • Detection of protein kinase activity in sodium dodecyl sulfate-polyacrylamide gels
    • Geahlen RL, Anostario M, Low PS, Harrison ML. (1986) Detection of protein kinase activity in sodium dodecyl sulfate-polyacrylamide gels. Anal Biochem.; 153: 151-8.
    • (1986) Anal Biochem , vol.153 , pp. 151-158
    • Geahlen, R.L.1    Anostario, M.2    Low, P.S.3    Harrison, M.L.4
  • 15
    • 18144447988 scopus 로고    scopus 로고
    • Profilin in Phaseolus vulgaris is encoded by two genes (only one expressed in root nodules) but multiple isoforms are generated in vivo by phosphorylation on tyrosine residues
    • Guillén G, Valdés-Lopez V, Noguez R, Olivares J, Rodriquez-Zapata LC, Pérez H, Vidali L, Villanueva MA, Sanchez F. (1999) Profilin in Phaseolus vulgaris is encoded by two genes (only one expressed in root nodules) but multiple isoforms are generated in vivo by phosphorylation on tyrosine residues. Plant J.; 19: 497-508.
    • (1999) Plant , vol.19 , pp. 497-508
    • Guillén, G.1    Valdés-Lopez, V.2    Noguez, R.3    Olivares, J.4    Rodriquez-Zapata, L.C.5    Pérez, H.6    Vidali, L.7    Villanueva, M.A.8    Sanchez, F.9
  • 16
    • 1642523244 scopus 로고    scopus 로고
    • The ethylene signaling pathway: New insights
    • Guo H, Ecker JR. (2004) The ethylene signaling pathway: new insights. Curr Opin Plant Biol.; 7: 40-9.
    • (2004) Curr Opin Plant Biol , vol.7 , pp. 40-49
    • Guo, H.1    Ecker, J.R.2
  • 17
    • 0029155492 scopus 로고
    • Histidine and tyrosine phosphorylation in pea mitochondria: Evidence for protein phosphorylation in respiratory redox signalling
    • Håkansson G, Allen JF. (1995) Histidine and tyrosine phosphorylation in pea mitochondria: evidence for protein phosphorylation in respiratory redox signalling. FEBS Lett.; 372: 238-42.
    • (1995) FEBS Lett , vol.372 , pp. 238-242
    • Håkansson, G.1    Allen, J.F.2
  • 18
    • 0026951882 scopus 로고
    • Novel protein kinase of Arabidopsis thaliana (APK1) that phosphorylates tyrosine serine and threonine
    • Hirayama T, Oka A. (1992) Novel protein kinase of Arabidopsis thaliana (APK1) that phosphorylates tyrosine serine and threonine. Plant Mol Biol.; 20: 653-62.
    • (1992) Plant Mol Biol , vol.20 , pp. 653-662
    • Hirayama, T.1    Oka, A.2
  • 20
    • 0032577051 scopus 로고    scopus 로고
    • The Croonian Lecture 1997. The phosphorylation of proteins on tyrosine: Its role in cell growth and disease
    • Hunter T. (1998) The Croonian Lecture 1997. The phosphorylation of proteins on tyrosine: its role in cell growth and disease. Philos Trans R Soc Lond Biol Sci.; 353: 583-605.
    • (1998) Philos Trans R Soc Lond Biol Sci , vol.353 , pp. 583-605
    • Hunter, T.1
  • 21
    • 0002631401 scopus 로고    scopus 로고
    • Protein phosphorylation during coconut zygotic embryo development
    • Islas-Flores I, Oropeza C, Hernández-Sotomayor T. (1998) Protein phosphorylation during coconut zygotic embryo development. Plant Physiol.; 118: 257-63.
    • (1998) Plant Physiol , vol.118 , pp. 257-263
    • Islas-Flores, I.1    Oropeza, C.2    Hernández-Sotomayor, T.3
  • 23
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature.; 227: 680-5.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 24
    • 0028010652 scopus 로고
    • Purification and differential expression of enolase from maize
    • Lal SK, Kelley PM, Elthon TE. (1994) Purification and differential expression of enolase from maize. Physiol Plant.; 91: 587-92.
    • (1994) Physiol Plant , vol.91 , pp. 587-592
    • Lal, S.K.1    Kelley, P.M.2    Elthon, T.E.3
  • 25
    • 0026555495 scopus 로고
    • Dual-specificity protein kinases: Will any hydroxyl do?
    • Lindberg RA, Quinn AM, Hunter T. (1992) Dual-specificity protein kinases: will any hydroxyl do? Trends Biochem Sci.; 17: 114-9.
    • (1992) Trends Biochem Sci , vol.17 , pp. 114-119
    • Lindberg, R.A.1    Quinn, A.M.2    Hunter, T.3
  • 26
    • 0037015047 scopus 로고    scopus 로고
    • Tyrosine phosphorylation in plant cell signaling
    • Luan S. (2002) Tyrosine phosphorylation in plant cell signaling. Proc Natl Acad Sci USA.; 99: 11567-9.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 11567-11569
    • Luan, S.1
  • 27
    • 0028357354 scopus 로고
    • Design and synthesis of two new peptide substrates for the specific and sensitive monitoring of casein kinases-1 and -2
    • Marin O, Meggio F, Pinna LA. (1994) Design and synthesis of two new peptide substrates for the specific and sensitive monitoring of casein kinases-1 and -2. Biochem Biophys Res Commun.; 198: 898-905.
    • (1994) Biochem Biophys Res Commun , vol.198 , pp. 898-905
    • Marin, O.1    Meggio, F.2    Pinna, L.A.3
  • 28
    • 0032878249 scopus 로고    scopus 로고
    • Tyrosine versus serine/threonine phosphorylation by protein kinase casein kinase-2
    • Marin O, Meggio F, Sarno S, Cesaro L, Pagano MA, Pinna LA. (1999) Tyrosine versus serine/threonine phosphorylation by protein kinase casein kinase-2 J Biol Chem.; 274: 29260-5.
    • (1999) J Biol Chem , vol.274 , pp. 29260-29265
    • Marin, O.1    Meggio, F.2    Sarno, S.3    Cesaro, L.4    Pagano, M.A.5    Pinna, L.A.6
  • 30
    • 0031472138 scopus 로고    scopus 로고
    • Cloning and characterization of MEK1 an Arabidopsis gene encoding a homologue of MAP krnase kinase
    • Morris PC, Guerrier D, Leung J, Giraudat J. (1997) Cloning and characterization of MEK1 an Arabidopsis gene encoding a homologue of MAP krnase kinase. Plant Mol Biol.; 35: 1057-64.
    • (1997) Plant Mol Biol , vol.35 , pp. 1057-1064
    • Morris, P.C.1    Guerrier, D.2    Leung, J.3    Giraudat, J.4
  • 31
    • 0024565853 scopus 로고
    • Thin-layer chromatography can resolve phosphotyrosine phosphoserine, and phosphothreonine in a protein hydrolyzate
    • Neufeld E, Goren J, Boland D. (1989) Thin-layer chromatography can resolve phosphotyrosine phosphoserine, and phosphothreonine in a protein hydrolyzate. Anal Biochem.; 177: 138-43.
    • (1989) Anal Biochem , vol.177 , pp. 138-143
    • Neufeld, E.1    Goren, J.2    Boland, D.3
  • 32
    • 0037451378 scopus 로고    scopus 로고
    • A MAPK pathway mediates ethylene signaling in plants
    • Ouaked F, Rozhon W, Lecourieux D, Hirt H. (2003) A MAPK pathway mediates ethylene signaling in plants. EMBO J.; 22: 1282-8.
    • (2003) EMBO J , vol.22 , pp. 1282-1288
    • Ouaked, F.1    Rozhon, W.2    Lecourieux, D.3    Hirt, H.4
  • 33
    • 0016711037 scopus 로고
    • High resolution two-dimensional electrophoresis of proteins
    • O'Farrell PH. (1975) High resolution two-dimensional electrophoresis of proteins. J Biol Chem.; 250: 4007-21.
    • (1975) J Biol Chem , vol.250 , pp. 4007-4021
    • O'Farrell, P.H.1
  • 34
    • 0033434080 scopus 로고    scopus 로고
    • Probability-based protein identification by searching sequence database using mass spectrometry data
    • Perkins DN, Pappin DJ, Creasy DM, Cottrell JS. (1999) Probability-based protein identification by searching sequence database using mass spectrometry data. Electrophoresis.; 20: 3551-67.
    • (1999) Electrophoresis , vol.20 , pp. 3551-3567
    • Perkins, D.N.1    Pappin, D.J.2    Creasy, D.M.3    Cottrell, J.S.4
  • 35
    • 0031574365 scopus 로고    scopus 로고
    • Staurosporine-induced conformational changes of cAMP-dependent protein kinase catalytic subunit explain inhibitory potential
    • Prade L, Engh RA, Girod A, Kinzel V, Huber R, Bossemeyer D. (1997) Staurosporine-induced conformational changes of cAMP-dependent protein kinase catalytic subunit explain inhibitory potential. Structure.; 5: 1627-37.
    • (1997) Structure , vol.5 , pp. 1627-1637
    • Prade, L.1    Engh, R.A.2    Girod, A.3    Kinzel, V.4    Huber, R.5    Bossemeyer, D.6
  • 36
    • 0030438629 scopus 로고    scopus 로고
    • The recombinant a isoform of protein kinase CK1 from Xenopus laevis can phosphorylate tyrosine in synthetic substrates
    • Pulgar V, Tapia C, Vignolo P, Santos J, Sunkel CE, Allende CG, Allende JE. (1996) The recombinant a isoform of protein kinase CK1 from Xenopus laevis can phosphorylate tyrosine in synthetic substrates. Eur J Biochem.; 242: 519-28.
    • (1996) Eur J Biochem , vol.242 , pp. 519-528
    • Pulgar, V.1    Tapia, C.2    Vignolo, P.3    Santos, J.4    Sunkel, C.E.5    Allende, C.G.6    Allende, J.E.7
  • 37
    • 0345464680 scopus 로고    scopus 로고
    • Evidence of protein-tyrosine kinase activity in Catharanthus roseus roots transformed by Agrobacterium rhizogenes
    • Rodriguez-Zapata LC, Hernández-Sotomayor T. (1998) Evidence of protein-tyrosine kinase activity in Catharanthus roseus roots transformed by Agrobacterium rhizogenes. Planta.; 204: 70-7.
    • (1998) Planta , vol.204 , pp. 70-77
    • Rodriguez-Zapata, L.C.1    Hernández-Sotomayor, T.2
  • 38
    • 0036742913 scopus 로고    scopus 로고
    • Developmentally regulated dual-specificity kinase from peanut that is induced by abiotic stresses
    • Rudrabhalta P, Rajasekharan R. (2002) Developmentally regulated dual-specificity kinase from peanut that is induced by abiotic stresses. Plant Physiology.; 130: 380-90.
    • (2002) Plant Physiology , vol.130 , pp. 380-390
    • Rudrabhalta, P.1    Rajasekharan, R.2
  • 39
    • 0037394416 scopus 로고    scopus 로고
    • Alternative splicing modulation by LAMMER kinase impinges on developmental and transcriptome expression
    • Savaldi-Goldstein S, Aviv D, Davydov O, Fluhr R. (2003) Alternative splicing modulation by LAMMER kinase impinges on developmental and transcriptome expression. Plant Cell.; 15: 926-38.
    • (2003) Plant Cell , vol.15 , pp. 926-938
    • Savaldi-Goldstein, S.1    Aviv, D.2    Davydov, O.3    Fluhr, R.4
  • 40
    • 0025221139 scopus 로고
    • Preferential inhibition of the platelet - Derived growth factor receptor tyrosine kinase by staurosporine
    • Secrist JP, Sehgal I, Powis G, Abraham RT. (1990) Preferential inhibition of the platelet - derived growth factor receptor tyrosine kinase by staurosporine. J Biol Chem.; 265: 20394-400.
    • (1990) J Biol Chem , vol.265 , pp. 20394-20400
    • Secrist, J.P.1    Sehgal, I.2    Powis, G.3    Abraham, R.T.4
  • 41
    • 0026690922 scopus 로고
    • Purification and characterization of mitogen-activated protein kinase activator(s) from epidermal growth factor - Stimulated A431 cells
    • Seger R, Ahn NG, Posade J, Munar ES, Jensen AM, Cooper JA, Cobb MH, Krebs EG. (1992) Purification and characterization of mitogen-activated protein kinase activator(s) from epidermal growth factor - stimulated A431 cells. J Biol Chem.; 267: 14373-81.
    • (1992) J Biol Chem , vol.267 , pp. 14373-14381
    • Seger, R.1    Ahn, N.G.2    Posade, J.3    Munar, E.S.4    Jensen, A.M.5    Cooper, J.A.6    Cobb, M.H.7    Krebs, E.G.8
  • 42
    • 0030331213 scopus 로고    scopus 로고
    • PK12 a plant dual-specificity protein kinase of the LAMMER family is regulated by the hormone ethylene
    • Sessa G, Raz V, Savaldi S, Fluhr R. (1996) PK12 a plant dual-specificity protein kinase of the LAMMER family is regulated by the hormone ethylene. Plant Cell.; 8: 2223-34.
    • (1996) Plant Cell , vol.8 , pp. 2223-2234
    • Sessa, G.1    Raz, V.2    Savaldi, S.3    Fluhr, R.4
  • 43
    • 0034870822 scopus 로고    scopus 로고
    • Isolation and characterization of kinase interacting protein 1 a pollen protein that interacts with the kinase domain of PRK1 a receptor-like kinase of Petunia
    • Skirpan AL, McCubbin AG, Ishimizu T, Wang X, Dowd PE, Ma H, Kao T-h. (2001) Isolation and characterization of kinase interacting protein 1 a pollen protein that interacts with the kinase domain of PRK1 a receptor-like kinase of Petunia. Plant Physiol.; 126: 1480-92.
    • (2001) Plant Physiol , vol.126 , pp. 1480-1492
    • Skirpan, A.L.1    McCubbin, A.G.2    Ishimizu, T.3    Wang, X.4    Dowd, P.E.5    Ma, H.6    Kao, T.-H.7
  • 44
    • 0023056735 scopus 로고
    • Evidence of the activity of tyrosine kinase(s) and of the presence of phosphotyrosine proteins in pea plantlets
    • Torruella M, Casano LM, Vallejos RH. (1986) Evidence of the activity of tyrosine kinase(s) and of the presence of phosphotyrosine proteins in pea plantlets. J Biol Chem.; 261: 6651-3.
    • (1986) J Biol Chem , vol.261 , pp. 6651-6653
    • Torruella, M.1    Casano, L.M.2    Vallejos, R.H.3
  • 45
    • 0040133536 scopus 로고    scopus 로고
    • Phosphorylation of plant proteins and the identification of protein-tyrosine kinase activity in maize seedlings
    • Trojanek J, Ek P, Scoble J, Muszyńska G, Engström L. (1996) Phosphorylation of plant proteins and the identification of protein-tyrosine kinase activity in maize seedlings. Eur J Biochem.; 235: 338-44.
    • (1996) Eur J Biochem , vol.235 , pp. 338-344
    • Trojanek, J.1    Ek, P.2    Scoble, J.3    Muszyńska, G.4    Engström, L.5
  • 47
    • 0030976507 scopus 로고    scopus 로고
    • Casein kinase II catalyzes tyrosine phosphorylation of the yeast nucleolar immunophilin Fpr.3
    • Wilson LK, Dhillon N, Thorner J, Martin GS. (1997) Casein kinase II catalyzes tyrosine phosphorylation of the yeast nucleolar immunophilin Fpr.3. J Biol Chem.; 272: 12961-7.
    • (1997) J Biol Chem , vol.272 , pp. 12961-12967
    • Wilson, L.K.1    Dhillon, N.2    Thorner, J.3    Martin, G.S.4
  • 48
    • 0021280154 scopus 로고
    • Purification and characterization of the major species of tyrosine protein kinase in rat liver
    • Wong TW, Goldberg AR. (1984) Purification and characterization of the major species of tyrosine protein kinase in rat liver. J Biol Chem.; 259: 8505-12.
    • (1984) J Biol Chem , vol.259 , pp. 8505-8512
    • Wong, T.W.1    Goldberg, A.R.2


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