메뉴 건너뛰기




Volumn 459, Issue 1, 2014, Pages 15-25

Multisite phosphorylation of 14-3-3 proteins by calcium-dependent protein kinases

Author keywords

14 3 3 protein; Arabidopsis; Calcium dependent protein kinase; Kinase assay; Protein protein interaction; Tyrosine phosphorylation

Indexed keywords

ASPARTIC ACID; CALCIUM DEPENDENT PROTEIN KINASE 28; CALCIUM DEPENDENT PROTEIN KINASE 3; CALCIUM DEPENDENT PROTEIN KINASE 6; CALCIUM DEPENDENT PROTEIN KINASE 8; CALCIUM PROTEIN KINASE; NITRATE REDUCTASE; OVALBUMIN; PROTEIN 14 3 3; PROTEIN KINASE; TYROSINE; UNCLASSIFIED DRUG;

EID: 84896133428     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20130035     Document Type: Article
Times cited : (40)

References (66)
  • 1
    • 0037662761 scopus 로고    scopus 로고
    • 14-3-3 proteins find new partners in plant cell signalling
    • Roberts, M. R. (2003) 14-3-3 proteins find new partners in plant cell signalling. Trends Plant Sci. 8, 218-223
    • (2003) Trends Plant Sci. , vol.8 , pp. 218-223
    • Roberts, M.R.1
  • 2
    • 0034817007 scopus 로고    scopus 로고
    • Data mining the Arabidopsis genome reveals fifteen 14-3-3 genes. Expression is demonstrated for two out of five novel genes
    • DOI 10.1104/pp.127.1.142
    • Rosenquist, M., Alsterfjord, M., Larsson, C. and Sommarin, M. (2001) Data mining the Arabidopsis genome reveals fifteen 14-3-3 genes. Expression is demonstrated for two out of five novel genes. Plant Physiol. 127, 142-149 (Pubitemid 32930675)
    • (2001) Plant Physiology , vol.127 , Issue.1 , pp. 142-149
    • Rosenquist, M.1    Alsterfjord, M.2    Larsson, C.3    Sommarin, M.4
  • 3
    • 77950524249 scopus 로고    scopus 로고
    • Systems analysis of seed filling in Arabidopsis: Using general linear modeling to assess concordance of transcript and protein expression
    • Hajduch, M., Hearne, L. B., Miernyk, J. A., Casteel, J. E., Joshi, T., Agrawal, G. K., Song, Z., Zhou, M., Xu, D. and Thelen, J. J. (2010) Systems analysis of seed filling in Arabidopsis: using general linear modeling to assess concordance of transcript and protein expression. Plant Physiol. 152, 2078-2087
    • (2010) Plant Physiol. , vol.152 , pp. 2078-2087
    • Hajduch, M.1    Hearne, L.B.2    Miernyk, J.A.3    Casteel, J.E.4    Joshi, T.5    Agrawal, G.K.6    Song, Z.7    Zhou, M.8    Xu, D.9    Thelen, J.J.10
  • 4
    • 80053563165 scopus 로고    scopus 로고
    • Identification of 14-3-3 proteins as a target of ATL31 ubiquitin ligase, a regulator of the C/N response in Arabidopsis
    • Sato, T., Maekawa, S., Yasuda, S., Domeki, Y., Sueyoshi, K., Fujiwara, M., Fukao, Y., Goto, D. B. and Yamaguchi, J. (2011) Identification of 14-3-3 proteins as a target of ATL31 ubiquitin ligase, a regulator of the C/N response in Arabidopsis. Plant J. 68, 137-146
    • (2011) Plant J. , vol.68 , pp. 137-146
    • Sato, T.1    Maekawa, S.2    Yasuda, S.3    Domeki, Y.4    Sueyoshi, K.5    Fujiwara, M.6    Fukao, Y.7    Goto, D.B.8    Yamaguchi, J.9
  • 5
    • 67651121737 scopus 로고    scopus 로고
    • 14-3-3 and FHA domains mediate phosphoprotein interactions
    • Chevalier, D., Morris, E. R. and Walker, J. C. (2009) 14-3-3 and FHA domains mediate phosphoprotein interactions. Annu. Rev. Plant Biol. 60, 67-91
    • (2009) Annu. Rev. Plant Biol. , vol.60 , pp. 67-91
    • Chevalier, D.1    Morris, E.R.2    Walker, J.C.3
  • 9
    • 78650904589 scopus 로고    scopus 로고
    • 14-3-3 proteins fine-tune plant nutrient metabolism
    • Shin, R., Jez, J. M., Basra, A., Zhang, B. and Schachtman, D. P. (2011) 14-3-3 proteins fine-tune plant nutrient metabolism. FEBS Lett. 585, 143-147
    • (2011) FEBS Lett. , vol.585 , pp. 143-147
    • Shin, R.1    Jez, J.M.2    Basra, A.3    Zhang, B.4    Schachtman, D.P.5
  • 10
    • 33751401609 scopus 로고    scopus 로고
    • Large scale identification and quantitative profiling of phosphoproteins expressed during seed filling in oilseed rape
    • DOI 10.1074/mcp.M600084-MCP200
    • Agrawal, G. K. and Thelen, J. J. (2006) Large scale identification and quantitative profiling of phosphoproteins expressed during seed filling in oilseed rape. Mol. Cell. Proteomics 5, 2044-2059 (Pubitemid 44817017)
    • (2006) Molecular and Cellular Proteomics , vol.5 , Issue.11 , pp. 2044-2059
    • Agrawal, G.K.1    Thelen, J.J.2
  • 12
    • 66649127498 scopus 로고    scopus 로고
    • Large-scale Arabidopsis phosphoproteome profiling reveals novel chloroplast kinase substrates and phosphorylation networks
    • Reiland, S., Messerli, G., Baerenfaller, K., Gerrits, B., Endler, A., Grossmann, J., Gruissem, W. and Baginsky, S. (2009) Large-scale Arabidopsis phosphoproteome profiling reveals novel chloroplast kinase substrates and phosphorylation networks. Plant Physiol. 150, 889-903
    • (2009) Plant Physiol. , vol.150 , pp. 889-903
    • Reiland, S.1    Messerli, G.2    Baerenfaller, K.3    Gerrits, B.4    Endler, A.5    Grossmann, J.6    Gruissem, W.7    Baginsky, S.8
  • 16
    • 63049130982 scopus 로고    scopus 로고
    • Phosphoproteomic analysis of ethylene-regulated protein phosphorylation in etiolated seedlings of Arabidopsis mutant ein2 using two-dimensional separations coupled with a hybrid quadrupole time-of-flight mass spectrometer
    • Li, H., Wong, W. S., Zhu, L., Guo, H. W., Ecker, J. and Li, N. (2009) Phosphoproteomic analysis of ethylene-regulated protein phosphorylation in etiolated seedlings of Arabidopsis mutant ein2 using two-dimensional separations coupled with a hybrid quadrupole time-of-flight mass spectrometer. Proteomics 9, 1646-1661
    • (2009) Proteomics , vol.9 , pp. 1646-1661
    • Li, H.1    Wong, W.S.2    Zhu, L.3    Guo, H.W.4    Ecker, J.5    Li, N.6
  • 20
    • 0034757497 scopus 로고    scopus 로고
    • Phosphorylation of synthetic peptides by a CDPK and plant SNF1-related protein kinase. Influence of proline and basic amino acid residues at selected positions
    • Huang, J. Z. and Huber, S. C. (2001) Phosphorylation of synthetic peptides by a CDPK and plant SNF1-related protein kinase. Influence of proline and basic amino acid residues at selected positions. Plant Cell Physiol. 42, 1079-1087
    • (2001) Plant Cell Physiol. , vol.42 , pp. 1079-1087
    • Huang, J.Z.1    Huber, S.C.2
  • 21
    • 0029924885 scopus 로고    scopus 로고
    • The inhibitor protein of phosphorylated nitrate reductase from spinach (Spinacia oleracea) leaves is a 14-3-3 protein
    • DOI 10.1016/0014-5793(96)00478-4
    • Bachmann, M., Huber, J. L., Liao, P. C., Gage, D. A. and Huber, S. C. (1996) The inhibitor protein of phosphorylated nitrate reductase from spinach (Spinacia oleracea) leaves is a 14-3-3 protein. FEBS Lett. 387, 127-131 (Pubitemid 26178907)
    • (1996) FEBS Letters , vol.387 , Issue.2-3 , pp. 127-131
    • Bachmann, M.1    Huber, J.L.2    Liao, P.-C.3    Gage, D.A.4    Huber, S.C.5
  • 22
    • 0028817353 scopus 로고
    • Partial purification and characterization of a calcium-dependent protein kinase and an inhibitor protein required for inactivation of spinach leaf nitrate reductase
    • Bachmann, M., McMichael, Jr, R. W., Huber, J. L., Kaiser, W. M. and Huber, S. C. (1995) Partial purification and characterization of a calcium-dependent protein kinase and an inhibitor protein required for inactivation of spinach leaf nitrate reductase. Plant Physiol. 108, 1083-1091
    • (1995) Plant Physiol. , vol.108 , pp. 1083-1091
    • Bachmann, M.1    McMichael Jr., R.W.2    Huber, J.L.3    Kaiser, W.M.4    Huber, S.C.5
  • 23
    • 0030250857 scopus 로고    scopus 로고
    • Phosphorylated nitrate reductase from spinach leaves is inhibited by 14- 3-3 proteins and activated by fusicoccin
    • DOI 10.1016/S0960-9822(02)70677-5
    • Moorhead, G., Douglas, P., Morrice, N., Scarabel, M., Aitken, A. and MacKintosh, C. (1996) Phosphorylated nitrate reductase from spinach leaves is inhibited by 14-3-3 proteins and activated by fusicoccin. Curr. Biol. 6, 1104-1113 (Pubitemid 26368744)
    • (1996) Current Biology , vol.6 , Issue.9 , pp. 1104-1113
    • Moorhead, G.1    Douglas, P.2    Morrice, N.3    Scarabel, M.4    Aitken, A.5    MacKintosh, C.6
  • 24
    • 0028795834 scopus 로고
    • Spinach leaf sucrose-phosphate synthase and nitrate reductase are phosphorylated/inactivated by multiple protein kinases in vitro
    • McMichael, Jr, R. W., Bachmann, M. and Huber, S. C. (1995) Spinach leaf sucrose-phosphate synthase and nitrate reductase are phosphorylated/inactivated by multiple protein kinases in vitro. Plant Physiol. 108, 1077-1082
    • (1995) Plant Physiol. , vol.108 , pp. 1077-1082
    • McMichael Jr., R.W.1    Bachmann, M.2    Huber, S.C.3
  • 25
    • 0032508671 scopus 로고    scopus 로고
    • Site-specific regulatory interaction between spinach leaf sucrose-phosphate synthase and 14-3-3 proteins
    • DOI 10.1016/S0014-5793(98)01048-5, PII S0014579398010485
    • Toroser, D., Athwal, G. S. and Huber, S. C. (1998) Site-specific regulatory interaction between spinach leaf sucrose-phosphate synthase and 14-3-3 proteins. FEBS Lett. 435, 110-114 (Pubitemid 28432025)
    • (1998) FEBS Letters , vol.435 , Issue.1 , pp. 110-114
    • Toroser, D.1    Athwal, G.S.2    Huber, S.C.3
  • 26
    • 0032479463 scopus 로고    scopus 로고
    • 14-3-3 proteins activate a plant calcium-dependent protein kinase (CDPK)
    • DOI 10.1016/S0014-5793(98)00696-6, PII S0014579398006966
    • Camoni, L., Harper, J. F. and Palmgren, M. G. (1998) 14-3-3 proteins activate a plant calcium-dependent protein kinase (CDPK). FEBS Lett. 430, 381-384 (Pubitemid 28337948)
    • (1998) FEBS Letters , vol.430 , Issue.3 , pp. 381-384
    • Camoni, L.1    Harper, J.F.2    Palmgren, M.G.3
  • 28
    • 84872332376 scopus 로고    scopus 로고
    • 14-3-3-regulated Ca2+ -dependent protein kinase CPK3 is required for sphingolipid-induced cell death in Arabidopsis
    • Lachaud, C., Prigent, E., Thuleau, P., Grat, S., Da Silva, D., Briere, C., Mazars, C. and Cotelle, V. (2012) 14-3-3-regulated Ca2+ -dependent protein kinase CPK3 is required for sphingolipid-induced cell death in Arabidopsis. Cell Death Differ. 20, 209-217
    • (2012) Cell Death Differ. , vol.20 , pp. 209-217
    • Lachaud, C.1    Prigent, E.2    Thuleau, P.3    Grat, S.4    Da Silva, D.5    Briere, C.6    Mazars, C.7    Cotelle, V.8
  • 29
    • 80052475187 scopus 로고    scopus 로고
    • The 14-3-3 isoforms χ and ε differentially bind client proteins from developing Arabidopsis seed
    • Swatek, K. N., Graham, K., Agrawal, G. K. and Thelen, J. J. (2011) The 14-3-3 isoforms χ and ε differentially bind client proteins from developing Arabidopsis seed. J. Proteome Res. 10, 4075-4087
    • (2011) J. Proteome Res. , vol.10 , pp. 4075-4087
    • Swatek, K.N.1    Graham, K.2    Agrawal, G.K.3    Thelen, J.J.4
  • 30
    • 65349083749 scopus 로고    scopus 로고
    • A high-resolution two dimensional Gel- and Pro-Q DPS-based proteomics workflow for phosphoprotein identification and quantitative profiling
    • Agrawal, G. K. and Thelen, J. J. (2009) A high-resolution two dimensional Gel- and Pro-Q DPS-based proteomics workflow for phosphoprotein identification and quantitative profiling. Methods Mol. Biol. 527, 3-19
    • (2009) Methods Mol. Biol. , vol.527 , pp. 3-19
    • Agrawal, G.K.1    Thelen, J.J.2
  • 31
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 32
  • 33
    • 56149086397 scopus 로고    scopus 로고
    • Decision tree-driven tandem mass spectrometry for shotgun proteomics
    • Swaney, D. L., McAlister, G. C. and Coon, J. J. (2008) Decision tree-driven tandem mass spectrometry for shotgun proteomics. Nat. Methods 5, 959-964
    • (2008) Nat. Methods , vol.5 , pp. 959-964
    • Swaney, D.L.1    McAlister, G.C.2    Coon, J.J.3
  • 34
    • 76149132007 scopus 로고    scopus 로고
    • Comparison of database search strategies for high precursor mass accuracy MS/MS data
    • Hsieh, E. J., Hoopmann, M. R., MacLean, B. and MacCoss, M. J. (2010) Comparison of database search strategies for high precursor mass accuracy MS/MS data. J. Proteome Res. 9, 1138-1143
    • (2010) J. Proteome Res. , vol.9 , pp. 1138-1143
    • Hsieh, E.J.1    Hoopmann, M.R.2    MacLean, B.3    MacCoss, M.J.4
  • 35
    • 55849122284 scopus 로고    scopus 로고
    • Evaluation of the utility of neutral-loss-dependent MS3 strategies in large-scale phosphorylation analysis
    • Villen, J., Beausoleil, S. A. and Gygi, S. P. (2008) Evaluation of the utility of neutral-loss-dependent MS3 strategies in large-scale phosphorylation analysis. Proteomics 8, 4444-4452
    • (2008) Proteomics , vol.8 , pp. 4444-4452
    • Villen, J.1    Beausoleil, S.A.2    Gygi, S.P.3
  • 37
    • 33644872218 scopus 로고    scopus 로고
    • Gateway-compatible vectors for plant functional genomics and proteomics
    • DOI 10.1111/j.1365-313X.2005.02617.x
    • Earley, K. W., Haag, J. R., Pontes, O., Opper, K., Juehne, T., Song, K. and Pikkard, C. S. (2006) Gateway-compatible vectors for plant functional genomics and proteomics. Plant J. 45, 616-629 (Pubitemid 43373712)
    • (2006) Plant Journal , vol.45 , Issue.4 , pp. 616-629
    • Earley, K.W.1    Haag, J.R.2    Pontes, O.3    Opper, K.4    Juehne, T.5    Song, K.6    Pikaard, C.S.7
  • 38
    • 83255188814 scopus 로고    scopus 로고
    • Pathogen effectors target Arabidopsis EDS1 and alter its interactions with immune regulators
    • Bhattacharjee, S., Halane, M. K., Kim, S. H. and Gassmann, W. (2011) Pathogen effectors target Arabidopsis EDS1 and alter its interactions with immune regulators. Science 334, 1405-1408
    • (2011) Science , vol.334 , pp. 1405-1408
    • Bhattacharjee, S.1    Halane, M.K.2    Kim, S.H.3    Gassmann, W.4
  • 39
    • 79551705019 scopus 로고    scopus 로고
    • The novel cyst nematode effector protein 19C07 interacts with the Arabidopsis auxin influx transporter LAX3 to control feeding site development
    • Lee, C., Chronis, D., Kenning, C., Peret, B., Hewezi, T., Davis, E. L., Baum, T. J., Hussey, R., Bennett, M. and Mitchum, M. G. (2011) The novel cyst nematode effector protein 19C07 interacts with the Arabidopsis auxin influx transporter LAX3 to control feeding site development. Plant Physiol. 155, 866-880
    • (2011) Plant Physiol. , vol.155 , pp. 866-880
    • Lee, C.1    Chronis, D.2    Kenning, C.3    Peret, B.4    Hewezi, T.5    Davis, E.L.6    Baum, T.J.7    Hussey, R.8    Bennett, M.9    Mitchum, M.G.10
  • 40
    • 0035983609 scopus 로고    scopus 로고
    • Calcium signaling through protein kinases. The Arabidopsis calcium-dependent protein kinase gene family
    • DOI 10.1104/pp.005645
    • Cheng, S. H., Willmann, M. R., Chen, H. C. and Sheen, J. (2002) Calcium signaling through protein kinases. The Arabidopsis calcium-dependent protein kinase gene family. Plant Physiol. 129, 469-485 (Pubitemid 34689138)
    • (2002) Plant Physiology , vol.129 , Issue.2 , pp. 469-485
    • Cheng, S.-H.1    Willmann, M.R.2    Chen, H.-C.3    Sheen, J.4
  • 41
    • 0037416221 scopus 로고    scopus 로고
    • Structural view of a fungal toxin acting on a 14-3-3 regulatory complex
    • DOI 10.1093/emboj/cdg104
    • Wurtele, M., Jelich-Ottmann, C., Wittinghofer, A. and Oecking, C. (2003) Structural view of a fungal toxin acting on a 14-3-3 regulatory complex. EMBO J. 22, 987-994 (Pubitemid 36313583)
    • (2003) EMBO Journal , vol.22 , Issue.5 , pp. 987-994
    • Wurtele, M.1    Jelich-Ottmann, C.2    Wittinghofer, A.3    Oecking, C.4
  • 42
    • 0028409180 scopus 로고
    • Phosphorylation and calcium binding properties of an Arabidopsis GF14 brain protein homolog
    • Lu, G., Sehnke, P. C. and Ferl, R. J. (1994) Phosphorylation and calcium binding properties of an Arabidopsis GF14 brain protein homolog. Plant Cell 6, 501-510
    • (1994) Plant Cell , vol.6 , pp. 501-510
    • Lu, G.1    Sehnke, P.C.2    Ferl, R.J.3
  • 43
    • 0024707611 scopus 로고
    • A protein kinase from wheat germ that phosphorylates the largest subunit of RNA polymerase II
    • Guilfoyle, T. J. (1989) A protein kinase from wheat germ that phosphorylates the largest subunit of RNA polymerase II. Plant Cell 1, 827-836
    • (1989) Plant Cell , vol.1 , pp. 827-836
    • Guilfoyle, T.J.1
  • 45
    • 6044226889 scopus 로고    scopus 로고
    • Differential mass spectrometry: A label-free LC-MS method for finding significant differences in complex peptide and protein mixtures
    • DOI 10.1021/ac0493875
    • Wiener, M. C., Sachs, J. R., Deyanova, E. G. and Yates, N. A. (2004) Differential mass spectrometry: a label-free LC-MS method for finding significant differences in complex peptide and protein mixtures. Anal. Chem. 76, 6085-6096 (Pubitemid 39382956)
    • (2004) Analytical Chemistry , vol.76 , Issue.20 , pp. 6085-6096
    • Wiener, M.C.1    Sachs, J.R.2    Deyanova, E.G.3    Yates, N.A.4
  • 47
    • 58149185117 scopus 로고    scopus 로고
    • P3DB: A plant protein phosphorylation database
    • Gao, J., Agrawal, G. K., Thelen, J. J. and Xu, D. (2009) P3DB: a plant protein phosphorylation database. Nucleic Acids Res. 37, 960-962
    • (2009) Nucleic Acids Res. , vol.37 , pp. 960-962
    • Gao, J.1    Agrawal, G.K.2    Thelen, J.J.3    Xu, D.4
  • 49
    • 3242659160 scopus 로고    scopus 로고
    • +-ATPase
    • DOI 10.1055/s-2004-820933
    • Giacometti, S., Camoni, L., Albumi, C., Visconti, S., De Michelis, M. I. and Aducci, P. (2004) Tyrosine phosphorylation inhibits the interaction of 14-3-3 proteins with the plant plasma membrane H+ -ATPase. Plant Biol. (Stuttg.) 6, 422-431 (Pubitemid 38947002)
    • (2004) Plant Biology , vol.6 , Issue.4 , pp. 422-431
    • Giacometti, S.1    Camoni, L.2    Albumi, C.3    Visconti, S.4    De Michelis, M.I.5    Aducci, P.6
  • 50
    • 0033180582 scopus 로고    scopus 로고
    • Structural analysis of 14-3-3 phosphopeptide complexes identifies a dual role for the nuclear export signal of 14-3-3 in ligand binding
    • DOI 10.1016/S1097-2765(00)80363-9
    • Rittinger, K., Budman, J., Xu, J., Volinia, S., Cantley, L. C., Smerdon, S. J., Gamblin, S. J. and Yaffe, M. B. (1999) Structural analysis of 14-3-3 phosphopeptide complexes identifies a dual role for the nuclear export signal of 14-3-3 in ligand binding. Mol. Cell 4, 153-166 (Pubitemid 29456884)
    • (1999) Molecular Cell , vol.4 , Issue.2 , pp. 153-166
    • Rittinger, K.1    Budman, J.2    Xu, J.3    Volinia, S.4    Cantley, L.C.5    Smerdon, S.J.6    Gamblin, S.J.7    Yaffe, M.B.8
  • 51
    • 0036834822 scopus 로고    scopus 로고
    • +-ATPase via their typical amphipathic groove
    • +-ATPase via their typical amphipathic groove. Planta 216, 136-139
    • (2002) Planta , vol.216 , pp. 136-139
    • Jaspert, N.1    Oecking, C.2
  • 52
    • 0032191853 scopus 로고    scopus 로고
    • Biological significance of divalent metal ion binding to 14-3-3 proteins in relationship to nitrate reductase inactivation
    • Athwal, G. S., Huber, J. L. and Huber, S. C. (1998) Biological significance of divalent metal ion binding to 14-3-3 proteins in relationship to nitrate reductase inactivation. Plant Cell Physiol. 39, 1065-1072 (Pubitemid 28514898)
    • (1998) Plant and Cell Physiology , vol.39 , Issue.10 , pp. 1065-1072
    • Athwal, G.S.1    Huber, J.L.2    Huber, S.C.3
  • 53
    • 84860549883 scopus 로고    scopus 로고
    • Phosphoproteomic analysis of seed maturation in Arabidopsis, rapeseed, and soybean
    • Meyer, L. J., Gao, J., Xu, D. and Thelen, J. J. (2012) Phosphoproteomic analysis of seed maturation in Arabidopsis, rapeseed, and soybean. Plant Physiol. 158, 517-528
    • (2012) Plant Physiol. , vol.158 , pp. 517-528
    • Meyer, L.J.1    Gao, J.2    Xu, D.3    Thelen, J.J.4
  • 55
    • 84855524689 scopus 로고    scopus 로고
    • Targeted quantitative phosphoproteomics approach for the detection of phospho-tyrosine signaling in plants
    • Mithoe, S. C., Boersema, P. J., Berke, L., Snel, B., Heck, A. J. and Menke, F. L. (2012) Targeted quantitative phosphoproteomics approach for the detection of phospho-tyrosine signaling in plants. J. Proteome Res. 11, 438-448
    • (2012) J. Proteome Res. , vol.11 , pp. 438-448
    • Mithoe, S.C.1    Boersema, P.J.2    Berke, L.3    Snel, B.4    Heck, A.J.5    Menke, F.L.6
  • 56
    • 58849127342 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of the BRI1 receptor kinase emerges as a component of brassinosteroid signaling in Arabidopsis
    • Oh, M. H., Wang, X., Kota, U., Goshe, M. B., Clouse, S. D. and Huber, S. C. (2009) Tyrosine phosphorylation of the BRI1 receptor kinase emerges as a component of brassinosteroid signaling in Arabidopsis. Proc. Natl. Acad. Sci. U.S.A. 106, 658-663
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 658-663
    • Oh, M.H.1    Wang, X.2    Kota, U.3    Goshe, M.B.4    Clouse, S.D.5    Huber, S.C.6
  • 57
    • 84859164078 scopus 로고    scopus 로고
    • Nitrate and ammonium lead to distinct global dynamic phosphorylation patterns when resupplied to nitrogen-starved Arabidopsis seedlings
    • Engelsberger, W. R. and Schulze, W. X. (2012) Nitrate and ammonium lead to distinct global dynamic phosphorylation patterns when resupplied to nitrogen-starved Arabidopsis seedlings. Plant J. 69, 978-995
    • (2012) Plant J. , vol.69 , pp. 978-995
    • Engelsberger, W.R.1    Schulze, W.X.2
  • 58
    • 84869487866 scopus 로고    scopus 로고
    • CDPKs are dual-specificity protein kinases and tyrosine autophosphorylation attenuates kinase activity
    • Oh, M. H., Wu, X., Kim, H. S., Harper, J. F., Zielinski, R. E., Clouse, S. D. and Huber, S. C. (2012) CDPKs are dual-specificity protein kinases and tyrosine autophosphorylation attenuates kinase activity. FEBS Lett. 586, 4070-4075
    • (2012) FEBS Lett. , vol.586 , pp. 4070-4075
    • Oh, M.H.1    Wu, X.2    Kim, H.S.3    Harper, J.F.4    Zielinski, R.E.5    Clouse, S.D.6    Huber, S.C.7
  • 60
    • 0035206122 scopus 로고    scopus 로고
    • 14-3-3 Proteins regulate intracellular localization of the bZIP transcriptional activator RSG
    • DOI 10.1105/tpc.13.11.2483
    • Igarashi, D., Ishida, S., Fukazawa, J. and Takahashi, Y. (2001) 14-3-3 proteins regulate intracellular localization of the bZIP transcriptional activator RSG. Plant Cell 13, 2483-2497 (Pubitemid 33146111)
    • (2001) Plant Cell , vol.13 , Issue.11 , pp. 2483-2497
    • Igarashi, D.1    Ishida, S.2    Fukazawa, J.3    Takahashi, Y.4
  • 61
    • 11944253861 scopus 로고    scopus 로고
    • Involvement of 14-3-3 signaling protein binding in the functional regulation of the transcriptional activator REPRESSION of SHOOT GROWTH by gibberellins
    • DOI 10.1105/tpc.104.024604
    • Ishida, S., Fukazawa, J., Yuasa, T. and Takahashi, Y. (2004) Involvement of 14-3-3 signaling protein binding in the functional regulation of the transcriptional activator REPRESSION OF SHOOT GROWTH by gibberellins. Plant Cell 16, 2641-2651 (Pubitemid 41071352)
    • (2004) Plant Cell , vol.16 , Issue.10 , pp. 2641-2651
    • Ishida, S.1    Fukazawa, J.2    Yuasa, T.3    Takahashi, Y.4
  • 62
    • 84873885749 scopus 로고    scopus 로고
    • 14-3-3 phosphoprotein interaction networks-does isoform diversity present functional interaction speciafication
    • Paul, A. L., Denison, F. C., Schultz, E. R., Zumanska, A. K. and Ferl, R. J. (2012) 14-3-3 phosphoprotein interaction networks-does isoform diversity present functional interaction speciafication. Front. Plant Sci. 3, 190
    • (2012) Front. Plant Sci. , vol.3 , pp. 190
    • Paul, A.L.1    Denison, F.C.2    Schultz, E.R.3    Zumanska, A.K.4    Ferl, R.J.5
  • 63
    • 3242727833 scopus 로고    scopus 로고
    • 2+ signals through plant protein kinases
    • DOI 10.1146/annurev.arplant.55.031903.141627
    • Harper, J. F., Breton, G. and Harmon, A. (2004) Decoding Ca2+ signals through plant protein kinases. Annu. Rev. Plant Biol. 55, 263-288 (Pubitemid 38940933)
    • (2004) Annual Review of Plant Biology , vol.55 , pp. 263-288
    • Harper, J.R.1    Breton, G.2    Harmon, A.3
  • 64
    • 84876747163 scopus 로고    scopus 로고
    • 14-3-3 regulates 1-amincyclopropane-1-1carboxylate synthase protein turnover in Arabidopsis
    • Yoon, G. M. and Kieber, J. J. (2013) 14-3-3 regulates 1-amincyclopropane-1-1carboxylate synthase protein turnover in Arabidopsis. Plant Cell 25, 1016-1028
    • (2013) Plant Cell , vol.25 , pp. 1016-1028
    • Yoon, G.M.1    Kieber, J.J.2
  • 65
    • 2142738304 scopus 로고    scopus 로고
    • WebLogo: A sequence logo generator
    • DOI 10.1101/gr.849004
    • Crooks, G. E., Hon, G., Chandonia, J. M. and Brenner, S. E. (2004) WebLogo: a sequence logo generator. Genome Res. 14, 1188-1190 (Pubitemid 38811555)
    • (2004) Genome Research , vol.14 , Issue.6 , pp. 1188-1190
    • Crooks, G.E.1    Hon, G.2    Chandonia, J.-M.3    Brenner, S.E.4
  • 66
    • 60149087610 scopus 로고    scopus 로고
    • A structural rationale for selective stabilization of anti-tumor interactions of 14-3-3 proteins by cotylenin A
    • Ottmann, C., Weyand, M., Sassa, T., Inoue, T., Kato, N., Wittinghofer, A. and Oecking, C. (2009) A structural rationale for selective stabilization of anti-tumor interactions of 14-3-3 proteins by cotylenin A. J. Mol. Biol. 386, 913-919
    • (2009) J. Mol. Biol. , vol.386 , pp. 913-919
    • Ottmann, C.1    Weyand, M.2    Sassa, T.3    Inoue, T.4    Kato, N.5    Wittinghofer, A.6    Oecking, C.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.