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Volumn 24, Issue 2, 2007, Pages 268-275

Isolation of the Arabidopsis phosphoproteome using a biotin-tagging approach

Author keywords

Arabidopsis; Biotin tagging; Mass spectrometry; Phosphoproteome; Protein phosphorylation

Indexed keywords

AVIDIN; BIOTIN; OXYGENASE; PHOSPHOPROTEOME; PROTEOME; RIBULOSEBISPHOSPHATE CARBOXYLASE; SERINE; THREONINE; UNCLASSIFIED DRUG;

EID: 36549010017     PISSN: 10168478     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (16)

References (35)
  • 1
    • 33646893240 scopus 로고    scopus 로고
    • TT8 controls its own expression in a feedback regulation involving TTG1 and homologous MYB and bHLH factors, allowing a strong and cell-specific accumulation of flavonoids in Arabidopsis thaliana
    • Baudry, A., Caboche, M., and Lepiniec, L. (2006) TT8 controls its own expression in a feedback regulation involving TTG1 and homologous MYB and bHLH factors, allowing a strong and cell-specific accumulation of flavonoids in Arabidopsis thaliana. Plant J. 46, 768-779.
    • (2006) Plant J , vol.46 , pp. 768-779
    • Baudry, A.1    Caboche, M.2    Lepiniec, L.3
  • 2
    • 0037431026 scopus 로고    scopus 로고
    • Identification of 14 new phosphoproteins involved in important plant mitochondrial processes
    • Bykova, N. V., Egsgaard, H., and Moller, I. M. (2003) Identification of 14 new phosphoproteins involved in important plant mitochondrial processes. FEBS Lett. 540, 141-146.
    • (2003) FEBS Lett , vol.540 , pp. 141-146
    • Bykova, N.V.1    Egsgaard, H.2    Moller, I.M.3
  • 3
    • 0036198435 scopus 로고    scopus 로고
    • Phosphoproteome analysis by mass spectrometry and its application to Saccharomyces cerevisiae
    • Ficarro, S. B., McCleland, M. L., Stukenberg, P. T., Burke, D. J., Ross, M. M., et al. (2002) Phosphoproteome analysis by mass spectrometry and its application to Saccharomyces cerevisiae. Nat. Biotechnol. 30, 301-305.
    • (2002) Nat. Biotechnol , vol.30 , pp. 301-305
    • Ficarro, S.B.1    McCleland, M.L.2    Stukenberg, P.T.3    Burke, D.J.4    Ross, M.M.5
  • 4
    • 0034466405 scopus 로고    scopus 로고
    • The oligomeric subunit C rotor in the fo sector of ATP synthase: Unresolved questions in our understanding of function
    • Fillingame, R. H. and Dmitriev, O. Y. (2000) The oligomeric subunit C rotor in the fo sector of ATP synthase: unresolved questions in our understanding of function. J. Bioenerg. Biomembr. 32, 433-439.
    • (2000) J. Bioenerg. Biomembr , vol.32 , pp. 433-439
    • Fillingame, R.H.1    Dmitriev, O.Y.2
  • 5
    • 0035975923 scopus 로고    scopus 로고
    • Perspectives of immobilized-metal affinity chromatography
    • Gaberc-Porekar, V. and Menart, V. (2001) Perspectives of immobilized-metal affinity chromatography. J. Biochem. Biophys. Methods 49, 335-360.
    • (2001) J. Biochem. Biophys. Methods , vol.49 , pp. 335-360
    • Gaberc-Porekar, V.1    Menart, V.2
  • 6
    • 0035356565 scopus 로고    scopus 로고
    • Phosphoprotein isotope-coded affinity tag approach for isolating and quantitating phosphopeptides in proteome-wide analyses
    • Goshe, M. B., Conrads, T. P., Panisko, E. A., Angell, N. H., Veenstra, T. D., et al. (2001) Phosphoprotein isotope-coded affinity tag approach for isolating and quantitating phosphopeptides in proteome-wide analyses. Anal. Chem. 73, 2578-2586.
    • (2001) Anal. Chem , vol.73 , pp. 2578-2586
    • Goshe, M.B.1    Conrads, T.P.2    Panisko, E.A.3    Angell, N.H.4    Veenstra, T.D.5
  • 7
    • 0036652968 scopus 로고    scopus 로고
    • A mass spectrometry-based proteomic approach for identification of serine/threonine-phosphorylated proteins by enrichment with phospho-specific antibodies: Identification of a novel protein, frigg, as a protein kinase a substrate
    • Gronborg, M., Kristiansen, T. Z., Stensballe, A., Andersen, J. S., Ohara, O., et al. (2002) A mass spectrometry-based proteomic approach for identification of serine/threonine-phosphorylated proteins by enrichment with phospho-specific antibodies: identification of a novel protein, frigg, as a protein kinase a substrate. Mol. Cell. Proteomics 1, 517-527.
    • (2002) Mol. Cell. Proteomics , vol.1 , pp. 517-527
    • Gronborg, M.1    Kristiansen, T.Z.2    Stensballe, A.3    Andersen, J.S.4    Ohara, O.5
  • 8
    • 26844507004 scopus 로고    scopus 로고
    • Rapid phosphorylation of a syntaxin during the Avr9/Cf-9-race-specific signaling pathway
    • Heese, A., Ludwig, A. A., and Jones, J. D. (2005) Rapid phosphorylation of a syntaxin during the Avr9/Cf-9-race-specific signaling pathway. Plant Physiol. 138, 2406-2416.
    • (2005) Plant Physiol , vol.138 , pp. 2406-2416
    • Heese, A.1    Ludwig, A.A.2    Jones, J.D.3
  • 9
    • 33645779078 scopus 로고    scopus 로고
    • The bifunctional dihydrofolate reductase thymidylate synthase of Tetrahymena thermophila provides a tool for molecular and biotechnology applications
    • Herrmann, L., Bockau, U., Tiedtke, A., Hartmann, M. W., and Weide, T. (2006) The bifunctional dihydrofolate reductase thymidylate synthase of Tetrahymena thermophila provides a tool for molecular and biotechnology applications. BMC Biotechnol. 20, 6-21.
    • (2006) BMC Biotechnol , vol.20 , pp. 6-21
    • Herrmann, L.1    Bockau, U.2    Tiedtke, A.3    Hartmann, M.W.4    Weide, T.5
  • 10
    • 33645218773 scopus 로고    scopus 로고
    • Nitric oxide scavenging by barley hemoglobin is facilitated by a monodehydroascorbate reductase-mediated ascorbate reduction of methemoglobin
    • Igamberdiev, A. U., Bykova, N. V., and Hill, R. D. (2006) Nitric oxide scavenging by barley hemoglobin is facilitated by a monodehydroascorbate reductase-mediated ascorbate reduction of methemoglobin. Planta 223, 1033-1040.
    • (2006) Planta , vol.223 , pp. 1033-1040
    • Igamberdiev, A.U.1    Bykova, N.V.2    Hill, R.D.3
  • 11
    • 0032603342 scopus 로고    scopus 로고
    • Sample preparation methods for mass spectrometric peptide mapping directly from 2-DE gels
    • Jensen, O. N., Wilm, M., Shevchenko, A., and Mann, M. (1999) Sample preparation methods for mass spectrometric peptide mapping directly from 2-DE gels. Meth. Mol. Biol. 112, 513-530.
    • (1999) Meth. Mol. Biol , vol.112 , pp. 513-530
    • Jensen, O.N.1    Wilm, M.2    Shevchenko, A.3    Mann, M.4
  • 12
    • 0037305895 scopus 로고    scopus 로고
    • Tackling the phosphoproteome: Tools and strategies
    • Kalume, D. E., Molina, H., and Pandey, A. (2003) Tackling the phosphoproteome: tools and strategies. Curr. Opin. Chem. Biol. 7, 64-69.
    • (2003) Curr. Opin. Chem. Biol , vol.7 , pp. 64-69
    • Kalume, D.E.1    Molina, H.2    Pandey, A.3
  • 13
    • 0034931862 scopus 로고    scopus 로고
    • Two-dimensional electrophoretic analysis of rice proteins by poly-ethylene glycol fractionation for protein arrays
    • Kim, S. T., Cho, K. S., Jang, Y. S., and Kang, K. Y. (2001) Two-dimensional electrophoretic analysis of rice proteins by poly-ethylene glycol fractionation for protein arrays. Electrophoresis 22, 2103-2109.
    • (2001) Electrophoresis , vol.22 , pp. 2103-2109
    • Kim, S.T.1    Cho, K.S.2    Jang, Y.S.3    Kang, K.Y.4
  • 14
    • 0037137219 scopus 로고    scopus 로고
    • Substrate binding and catalytic mechanism in ascorbate peroxidase: Evidence for two ascorbate binding sites
    • Lad, L., Mewies, M., and Randaven, E. L. (2002) Substrate binding and catalytic mechanism in ascorbate peroxidase: evidence for two ascorbate binding sites. Biochemistry 41, 13774-13781.
    • (2002) Biochemistry , vol.41 , pp. 13774-13781
    • Lad, L.1    Mewies, M.2    Randaven, E.L.3
  • 15
    • 0034073417 scopus 로고    scopus 로고
    • A method for application of samples to matrix-assisted laser desorption ionization time-of-flight targets that enhances peptide detection
    • Landry, F., Lombardo, C. R., and Smith, J. W. (2000) A method for application of samples to matrix-assisted laser desorption ionization time-of-flight targets that enhances peptide detection. Anal. Biochem. 279, 1-8.
    • (2000) Anal. Biochem , vol.279 , pp. 1-8
    • Landry, F.1    Lombardo, C.R.2    Smith, J.W.3
  • 16
    • 13444263450 scopus 로고    scopus 로고
    • Deciphering the plant phosphoproteome: Tools and strategies for a challenging task
    • Laugesen, S., Bergoin, A., and Rossignol, M. (2004) Deciphering the plant phosphoproteome: tools and strategies for a challenging task. Plant Physiol. Biochem. 42, 929-936.
    • (2004) Plant Physiol. Biochem , vol.42 , pp. 929-936
    • Laugesen, S.1    Bergoin, A.2    Rossignol, M.3
  • 17
    • 2942677358 scopus 로고    scopus 로고
    • Proteomic identification of annexins, calcium-dependent membrane binding proteins that mediate osmotic stress and abscisic acid signal transduction in Arabidopsis
    • Lee, S., Lee, E. J., Yang, E. J., Lee, J. E., Park, A. R., et al. (2004) Proteomic identification of annexins, calcium-dependent membrane binding proteins that mediate osmotic stress and abscisic acid signal transduction in Arabidopsis. Plant Cell 16, 1378-1391.
    • (2004) Plant Cell , vol.16 , pp. 1378-1391
    • Lee, S.1    Lee, E.J.2    Yang, E.J.3    Lee, J.E.4    Park, A.R.5
  • 18
    • 8844287599 scopus 로고    scopus 로고
    • Current chemical tagging strategies for proteome analysis by mass spectrometry
    • Leitner, A. and Lindner, W. (2004) Current chemical tagging strategies for proteome analysis by mass spectrometry. J. Chromatogr. B Analyt. Technol. Biomed. Life Sci. 813, 1-26.
    • (2004) J. Chromatogr. B Analyt. Technol. Biomed. Life Sci , vol.813 , pp. 1-26
    • Leitner, A.1    Lindner, W.2
  • 19
    • 7044222569 scopus 로고    scopus 로고
    • Chloroplast phosphoglycerate kinase from Euglena gracilis: Endosymbiotic gene replacement going against the tide
    • Nowitzki, U., Gelius-Dietrich, G., Schwieger, M., Henze, K., and Martin, W. (2004) Chloroplast phosphoglycerate kinase from Euglena gracilis: endosymbiotic gene replacement going against the tide. Eur. J. Biochem. 271, 4123-4131.
    • (2004) Eur. J. Biochem , vol.271 , pp. 4123-4131
    • Nowitzki, U.1    Gelius-Dietrich, G.2    Schwieger, M.3    Henze, K.4    Martin, W.5
  • 20
    • 11444263845 scopus 로고    scopus 로고
    • Large-scale analysis of in vivo phosphorylated membrane proteins by immobilized metal ion affinity chromatography and mass spectrometry
    • Nuhse, T. S., Stensballe, A., Jensen, O. N., and Peck, S. C. (2003) Large-scale analysis of in vivo phosphorylated membrane proteins by immobilized metal ion affinity chromatography and mass spectrometry. Mol. Cell. Proteomics 2, 1234-1243.
    • (2003) Mol. Cell. Proteomics , vol.2 , pp. 1234-1243
    • Nuhse, T.S.1    Stensballe, A.2    Jensen, O.N.3    Peck, S.C.4
  • 21
    • 4544291080 scopus 로고    scopus 로고
    • Phosphoproteomics of the Arabidopsis plasma membrane and a new phosphorylation site database
    • Nuhse, T. S., Stensballe, A., Jensen, O. N., and Peck, S. C. (2004) Phosphoproteomics of the Arabidopsis plasma membrane and a new phosphorylation site database. Plant Cell 16, 2394-2405.
    • (2004) Plant Cell , vol.16 , pp. 2394-2405
    • Nuhse, T.S.1    Stensballe, A.2    Jensen, O.N.3    Peck, S.C.4
  • 22
    • 0035067251 scopus 로고    scopus 로고
    • Enrichment analysis of phosphorylated proteins as a tool for probing the phosphoproteome
    • Oda, Y., Nagasu, T., and Chait, B. T. (2001) Enrichment analysis of phosphorylated proteins as a tool for probing the phosphoproteome. Nat. Biotechnol. 19, 379-382.
    • (2001) Nat. Biotechnol , vol.19 , pp. 379-382
    • Oda, Y.1    Nagasu, T.2    Chait, B.T.3
  • 23
    • 27444439553 scopus 로고    scopus 로고
    • Intracellular signaling for vasoconstrictor coupling factor 6: Novel function of beta-subunit of ATP synthase as receptor
    • Osanai, T., Magota, K., Tanaka, M., Shimada, M., Murakami, R., et al. (2005) Intracellular signaling for vasoconstrictor coupling factor 6: novel function of beta-subunit of ATP synthase as receptor. Hypertension 46, 1140-1146.
    • (2005) Hypertension , vol.46 , pp. 1140-1146
    • Osanai, T.1    Magota, K.2    Tanaka, M.3    Shimada, M.4    Murakami, R.5
  • 24
    • 0034602654 scopus 로고    scopus 로고
    • Analysis of receptor signaling pathways by mass spectrometry: Identification of vav-2 as a substrate of the epidermal and platelet-derived growth factor receptors
    • Pandey, A., Podtelejnikov, A. V., Blagoev, B., Bustelo, X. R., Mann, M., et al. (2000) Analysis of receptor signaling pathways by mass spectrometry: identification of vav-2 as a substrate of the epidermal and platelet-derived growth factor receptors. Proc. Natl. Acad. Sci. USA 97, 179-184.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 179-184
    • Pandey, A.1    Podtelejnikov, A.V.2    Blagoev, B.3    Bustelo, X.R.4    Mann, M.5
  • 25
    • 20444383859 scopus 로고    scopus 로고
    • Protein phosphorylation in signaling-50 years and counting
    • Pawson, T. and Scott, J. D. (2005) Protein phosphorylation in signaling-50 years and counting. Trends Biochem. Sci. 30, 286-290.
    • (2005) Trends Biochem. Sci , vol.30 , pp. 286-290
    • Pawson, T.1    Scott, J.D.2
  • 26
    • 0037458030 scopus 로고    scopus 로고
    • Profiling of tyrosine phosphorylation pathways in human cells using mass spectrometry
    • Salomon, A. R., Ficarro, S. B., Brill, L. M., Brinker, A., Phung, Q. T., et al. (2003) Profiling of tyrosine phosphorylation pathways in human cells using mass spectrometry. Proc. Natl. Acad. Sci. USA 100, 443-448.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 443-448
    • Salomon, A.R.1    Ficarro, S.B.2    Brill, L.M.3    Brinker, A.4    Phung, Q.T.5
  • 27
    • 0034284068 scopus 로고    scopus 로고
    • Functional significance of conserved residues in the phosphohydrolase module of Escherichia coli MutT protein
    • Shimokawa, H., Fujii, Y., Furuichi, M., Sekiguchi, M., and Nakabeppu, Y. (2000) Functional significance of conserved residues in the phosphohydrolase module of Escherichia coli MutT protein. Nucleic Acids Res. 28, 3240-3249.
    • (2000) Nucleic Acids Res , vol.28 , pp. 3240-3249
    • Shimokawa, H.1    Fujii, Y.2    Furuichi, M.3    Sekiguchi, M.4    Nakabeppu, Y.5
  • 28
    • 0347300317 scopus 로고    scopus 로고
    • The Arabidopsis 14-3-3 protein, GF14omega, binds to the Schizosaccharomyces pombe Cdc25 phosphatase and rescues checkpoint defects in the rad24-mutant
    • Sorrell, D. A., Marchbank, A. M., Chrimes, D. A., Dickinson, J. R., Rogers, H. J., et al. (2000) The Arabidopsis 14-3-3 protein, GF14omega, binds to the Schizosaccharomyces pombe Cdc25 phosphatase and rescues checkpoint defects in the rad24-mutant. Planta 218, 50-57.
    • (2000) Planta , vol.218 , pp. 50-57
    • Sorrell, D.A.1    Marchbank, A.M.2    Chrimes, D.A.3    Dickinson, J.R.4    Rogers, H.J.5
  • 29
    • 33845968538 scopus 로고    scopus 로고
    • Stress-induced inactivation of the c-Myb transcription factor through conjugation of SUMO-2/3 proteins
    • Sramko, M., Markus, J., Kabat, J., Wolff, L., and Bies, J. (2006) Stress-induced inactivation of the c-Myb transcription factor through conjugation of SUMO-2/3 proteins. J. Biol. Chem. 281, 40065-40075.
    • (2006) J. Biol. Chem , vol.281 , pp. 40065-40075
    • Sramko, M.1    Markus, J.2    Kabat, J.3    Wolff, L.4    Bies, J.5
  • 30
    • 0034532009 scopus 로고    scopus 로고
    • Molecular characterization of cDNA encoding oxygen evolving enhancer protein 1 increased by salt treatment in the mangrove Bruguiera gymnorrhiza
    • Sugihara, K., Hanagata, N., Dubinsky, Z., Baba, S., and Karube, I. (2000) Molecular characterization of cDNA encoding oxygen evolving enhancer protein 1 increased by salt treatment in the mangrove Bruguiera gymnorrhiza. Plant Cell Physiol. 41, 1279-1285.
    • (2000) Plant Cell Physiol , vol.41 , pp. 1279-1285
    • Sugihara, K.1    Hanagata, N.2    Dubinsky, Z.3    Baba, S.4    Karube, I.5
  • 31
    • 16544383862 scopus 로고    scopus 로고
    • Unique and overlapping expression patterns among the Arabidopsis 1-amino-cyclopropane-l-carboxylate synthase gene family members
    • Tsuchisaka, A. and Theologis, A. (2004) Unique and overlapping expression patterns among the Arabidopsis 1-amino-cyclopropane-l-carboxylate synthase gene family members. Plant Physiol. 136, 2982-3000.
    • (2004) Plant Physiol , vol.136 , pp. 2982-3000
    • Tsuchisaka, A.1    Theologis, A.2
  • 32
    • 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., and Vierstra, R. D. (2001) Mass spectrometric resolution of reversible protein phosphorylation in photosynthetic membranes of Arabidopsis thaliana. J. Biol. Chem. 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
  • 33
    • 33947366382 scopus 로고    scopus 로고
    • Identification of putative MAPK kinases in Oryza minuta and O. sativa responsive to biotic stresses
    • You, M. K., Oh, S. I., Ok, S. H., Cho, S. K., Shin, H. Y., et al. (2007) Identification of putative MAPK kinases in Oryza minuta and O. sativa responsive to biotic stresses. Mol. Cells 23, 108-114.
    • (2007) Mol. Cells , vol.23 , pp. 108-114
    • You, M.K.1    Oh, S.I.2    Ok, S.H.3    Cho, S.K.4    Shin, H.Y.5
  • 34
    • 0028144380 scopus 로고
    • Photoaffinity labeling of Arabidopsis thaliana plasma membrane vesicles by 5-azido-[7-3H] indole-3-acetic acid: Identification of a glutathione S-transferase
    • Zettl, R., Schell, J., and Palme, K. (1994) Photoaffinity labeling of Arabidopsis thaliana plasma membrane vesicles by 5-azido-[7-3H] indole-3-acetic acid: identification of a glutathione S-transferase. Proc. Natl. Acad Sci. USA 91, 689-693.
    • (1994) Proc. Natl. Acad Sci. USA , vol.91 , pp. 689-693
    • Zettl, R.1    Schell, J.2    Palme, K.3
  • 35
    • 0035072715 scopus 로고    scopus 로고
    • A systematic approach to the analysis of protein phosphorylation
    • Zhou, H., Watts, J. D., and Aebersold, R. (2001) A systematic approach to the analysis of protein phosphorylation. Nat. Biotechnol. 19, 375-378.
    • (2001) Nat. Biotechnol , vol.19 , pp. 375-378
    • Zhou, H.1    Watts, J.D.2    Aebersold, R.3


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