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Volumn 41, Issue 4, 2000, Pages 523-533

Modulation of 14-3-3 protein interactions with target polypeptides by physical and metabolic effectors

Author keywords

AMP binding; BIAcore; Hydrolytic activity; Metal binding; Protein:protein interaction; Spinacia oleracea

Indexed keywords

14 3 3 PROTEIN; ADENOSINE PHOSPHATE; ALLOSTERISM; BINDING KINETICS; ENZYME PHOSPHORYLATION; HYDROPHOBICITY; LIGAND BINDING; NITRATE REDUCTASE; PH; PROTEIN BINDING; PROTEIN PROTEIN INTERACTION; SPINACH; STEADY STATE; SURFACE PLASMON RESONANCE; SYNTHETIC PEPTIDE;

EID: 0034071769     PISSN: 00320781     EISSN: None     Source Type: Journal    
DOI: 10.1093/pcp/41.4.523     Document Type: Article
Times cited : (33)

References (43)
  • 1
    • 0032942341 scopus 로고    scopus 로고
    • Light modulation and in vivo effects of adenine nucleotides on leaf nitrate reductase activity in cucumber (Cucumis sativus)
    • Agüera, E., Poblete, L., de la Haba, P. and Maldonado, J.M. (1999) Light modulation and in vivo effects of adenine nucleotides on leaf nitrate reductase activity in cucumber (Cucumis sativus). Physiol. Plant. 105: 218-223.
    • (1999) Physiol. Plant. , vol.105 , pp. 218-223
    • Agüera, E.1    Poblete, L.2    De La Haba, P.3    Maldonado, J.M.4
  • 2
    • 0032191853 scopus 로고    scopus 로고
    • Biological significance of divalent metal ion binding to 13-3-3 proteins in relationship to nitrate reductase inactivation
    • Athwal, G.S., Huber, J.L. and Huber, S.C. (1998a) Biological significance of divalent metal ion binding to 13-3-3 proteins in relationship to nitrate reductase inactivation. Plant Cell Physiol. 39: 1065-1072.
    • (1998) Plant Cell Physiol. , vol.39 , pp. 1065-1072
    • Athwal, G.S.1    Huber, J.L.2    Huber, S.C.3
  • 3
    • 0032197397 scopus 로고    scopus 로고
    • Phosphorylated nitrate reductase and 14-3-3 proteins. Site of interaction, effects of ions, and evidence for an AMP-binding site on 14-3-3 proteins
    • Athwal, G.S., Huber, J.L. and Huber, S. (1998b) Phosphorylated nitrate reductase and 14-3-3 proteins. Site of interaction, effects of ions, and evidence for an AMP-binding site on 14-3-3 proteins. Plant Physiol. 118: 1041-1048.
    • (1998) Plant Physiol. , vol.118 , pp. 1041-1048
    • Athwal, G.S.1    Huber, J.L.2    Huber, S.3
  • 4
    • 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., McMicheal, R.W., Jr., 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    McMicheal R.W., Jr.2    Huber, J.L.3    Kaiser, W.M.4    Huber, S.C.5
  • 5
    • 0030602179 scopus 로고    scopus 로고
    • 14-3-3 proteins associated with the regulatory phosphorylation site of spinach leaf nitrate reductase in an isoform-specific manner and reduced dephosphorylation of Ser-543 by endogenous protein phosphatases
    • Bachmann, M., Huber, J.L., Athwal, G.S., Wu, K., Ferl, R.J. and Huber, S.C. (1996b) 14-3-3 proteins associated with the regulatory phosphorylation site of spinach leaf nitrate reductase in an isoform-specific manner and reduced dephosphorylation of Ser-543 by endogenous protein phosphatases. FEBS Letts. 398: 26-30.
    • (1996) FEBS Letts. , vol.398 , pp. 26-30
    • Bachmann, M.1    Huber, J.L.2    Athwal, G.S.3    Wu, K.4    Ferl, R.J.5    Huber, S.C.6
  • 6
    • 0030096855 scopus 로고    scopus 로고
    • Identification of Ser-543 as the major regulatory phosphorylation site in spinach leaf nitrate reductase
    • Bachmann, M., Shiraishi, N., Campbell, W.H., Yoo, B-C., Harmon, A.C. and Huber, S.C. (1996a) Identification of Ser-543 as the major regulatory phosphorylation site in spinach leaf nitrate reductase. Plant Cell 8: 505-517.
    • (1996) Plant Cell , vol.8 , pp. 505-517
    • Bachmann, M.1    Shiraishi, N.2    Campbell, W.H.3    Yoo, B.-C.4    Harmon, A.C.5    Huber, S.C.6
  • 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, M.M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye binding. Anal. Biochem. 72: 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 8
    • 0039441128 scopus 로고    scopus 로고
    • Nitrate reductase structure, function and regulation: Bridging the gap between biochemistry and physiology
    • Campbell, W.H. (1999) Nitrate reductase structure, function and regulation: bridging the gap between biochemistry and physiology. Annu. Rev. Plant Physiol. Plant Mol. Biol. 50: 277-303.
    • (1999) Annu. Rev. Plant Physiol. Plant Mol. Biol. , vol.50 , pp. 277-303
    • Campbell, W.H.1
  • 10
    • 0000924662 scopus 로고
    • Rapid modulation of nitrate reductase in pea roots
    • Glaab, J. and Kaiser, W.H. (1993) Rapid modulation of nitrate reductase in pea roots. Planta 191: 173-179.
    • (1993) Planta , vol.191 , pp. 173-179
    • Glaab, J.1    Kaiser, W.H.2
  • 11
    • 0027949375 scopus 로고
    • A novel cytoplasmic chaperone which functions in precursor targeting to mitochondria
    • Hachiya, N., Komiya, T., Alam, R., Iwahashi, J., Sakaguchi, M., Omura, T. and Mihara, K. (1994) A novel cytoplasmic chaperone which functions in precursor targeting to mitochondria. EMBO J. 13: 5146-5154.
    • (1994) EMBO J. , vol.13 , pp. 5146-5154
    • Hachiya, N.1    Komiya, T.2    Alam, R.3    Iwahashi, J.4    Sakaguchi, M.5    Omura, T.6    Mihara, K.7
  • 13
    • 0029137629 scopus 로고
    • Metabolic activators of spinach leaf nitrate reductase: Effects on enzymatic activity and dephosphorylation by endogenous phosphatases
    • Huber, S.C. and Huber, J.L. (1995) Metabolic activators of spinach leaf nitrate reductase: effects on enzymatic activity and dephosphorylation by endogenous phosphatases. Planta 196: 180-189.
    • (1995) Planta , vol.196 , pp. 180-189
    • Huber, S.C.1    Huber, J.L.2
  • 14
    • 0026633177 scopus 로고
    • Reversible light/dark modulation of spinach leaf nitrate reductase activity involves protein phosphorylation
    • Huber, J.L., Huber, S.C., Campbell, W.H. and Redinbaugh, M.G. (1992) Reversible light/dark modulation of spinach leaf nitrate reductase activity involves protein phosphorylation. Arch. Biochem. Biophys. 296: 58-65.
    • (1992) Arch. Biochem. Biophys. , vol.296 , pp. 58-65
    • Huber, J.L.1    Huber, S.C.2    Campbell, W.H.3    Redinbaugh, M.G.4
  • 15
    • 0030435802 scopus 로고    scopus 로고
    • 5-aminoimidazole-4-carboxamide riboside activates nitrate reductase in darkened spinach and pea leaves
    • Huber, S.C. and Kaiser, W.M. (1996) 5-aminoimidazole-4-carboxamide riboside activates nitrate reductase in darkened spinach and pea leaves. Physiol. Plant. 98: 833-837.
    • (1996) Physiol. Plant. , vol.98 , pp. 833-837
    • Huber, S.C.1    Kaiser, W.M.2
  • 17
    • 0000137376 scopus 로고
    • Rapid modulation of spinach leaf nitrate reductase by photosynthesis. II. In vitro modulation by ATP and AMP
    • Kaiser, W.M. and Spill, D. (1991) Rapid modulation of spinach leaf nitrate reductase by photosynthesis. II. In vitro modulation by ATP and AMP. Plant Physiol. 96: 368-375.
    • (1991) Plant Physiol. , vol.96 , pp. 368-375
    • Kaiser, W.M.1    Spill, D.2
  • 18
    • 34249833664 scopus 로고
    • Adenine nucleotides are apparently involved in the light-dark modulation of spinach nitrate reductase
    • Kaiser, W.H., Spill, D. and Brenble-Behnisch, E. (1992) Adenine nucleotides are apparently involved in the light-dark modulation of spinach nitrate reductase. Planta 186: 236-240.
    • (1992) Planta , vol.186 , pp. 236-240
    • Kaiser, W.H.1    Spill, D.2    Brenble-Behnisch, E.3
  • 19
    • 0032940292 scopus 로고    scopus 로고
    • Nitrate reductase in higher plants: A case study for transduction of environmental stimuli into control of catalytic activity
    • Kaiser, W.M., Weiner, H. and Huber, S.C. (1999) Nitrate reductase in higher plants: a case study for transduction of environmental stimuli into control of catalytic activity. Physiol. Plant. 105: 385-390.
    • (1999) Physiol. Plant. , vol.105 , pp. 385-390
    • Kaiser, W.M.1    Weiner, H.2    Huber, S.C.3
  • 20
    • 0031282109 scopus 로고    scopus 로고
    • Nonspecific amine immobilization of ligand can be a potential source of error in BIAcore binding experiments and may reduce binding affinities
    • Kortt, A.A., Oddie, G.W., Iliades, P., Gruen, L.C. and Hudson, P.J. (1997) Nonspecific amine immobilization of ligand can be a potential source of error in BIAcore binding experiments and may reduce binding affinities. Anal. Biochem. 253: 103-111.
    • (1997) Anal. Biochem. , vol.253 , pp. 103-111
    • Kortt, A.A.1    Oddie, G.W.2    Iliades, P.3    Gruen, L.C.4    Hudson, P.J.5
  • 21
    • 0027946119 scopus 로고
    • Recognition of mitochondria targeting signals by a cytosolic import stimulation factor
    • Komiya, T., Hachiya, N., Sakaguchi, M., Omura, T. and Mihara, K. (1994) Recognition of mitochondria targeting signals by a cytosolic import stimulation factor. J. Biol. Chem. 269: 30893-30897.
    • (1994) J. Biol. Chem. , vol.269 , pp. 30893-30897
    • Komiya, T.1    Hachiya, N.2    Sakaguchi, M.3    Omura, T.4    Mihara, K.5
  • 22
    • 0030045427 scopus 로고    scopus 로고
    • Cytoplasmic chaperones determine the targeting pathway of precursor proteins to mitochondria
    • Komiya, T., Sakaguchi, M. and Mihara, K. (1996) Cytoplasmic chaperones determine the targeting pathway of precursor proteins to mitochondria. EMBO J. 15: 399-407.
    • (1996) EMBO J. , vol.15 , pp. 399-407
    • Komiya, T.1    Sakaguchi, M.2    Mihara, K.3
  • 23
  • 25
    • 0026768507 scopus 로고
    • Regulation of spinach leaf nitrate reductase
    • Mackintosh, C. (1992) Regulation of spinach leaf nitrate reductase. Biochim. Biophys. Acta. 1137: 121-126.
    • (1992) Biochim. Biophys. Acta. , vol.1137 , pp. 121-126
    • Mackintosh, C.1
  • 26
    • 0000060738 scopus 로고    scopus 로고
    • The 14-3-3 protein binds to the nuclear matrix endonuclease and has a possible function in the control of plant senescence
    • Markiewicz, E., Wilczynski, G., Rzepecki, R., Kulma, A. and Szopa, J. (1996) The 14-3-3 protein binds to the nuclear matrix endonuclease and has a possible function in the control of plant senescence. Cell Mol. Biol. Lett. 1: 391-415.
    • (1996) Cell Mol. Biol. Lett. , vol.1 , pp. 391-415
    • Markiewicz, E.1    Wilczynski, G.2    Rzepecki, R.3    Kulma, A.4    Szopa, J.5
  • 27
    • 0033586783 scopus 로고    scopus 로고
    • Interaction of 14-3-3 with nonphosphorylated protein ligand, Exoenzyme S of Pseudomonas aeruginosa
    • Masters, S.C., Pederson, K.J., Zhang, L., Barbieri, J.T. and Fu, H. (1999) Interaction of 14-3-3 with nonphosphorylated protein ligand, Exoenzyme S of Pseudomonas aeruginosa. Biochemistry 38: 5216-5221.
    • (1999) Biochemistry , vol.38 , pp. 5216-5221
    • Masters, S.C.1    Pederson, K.J.2    Zhang, L.3    Barbieri, J.T.4    Fu, H.5
  • 28
    • 0028795834 scopus 로고
    • Spinach leaf sucrose-phosphate synthase and nitrate reductase are phosphorylated/inactivated by multiple protein kinases in vitro
    • McMichael, R.W., Jr., 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 R.W., Jr.1    Bachmann, M.2    Huber, S.C.3
  • 29
    • 0027234028 scopus 로고
    • 2+ affects the binding of ADP but not ATP to 3-phosphoglycerate kinase: Correlation between equilibrium dialysis binding and enzyme kinetic data
    • 2+ affects the binding of ADP but not ATP to 3-phosphoglycerate kinase: Correlation between equilibrium dialysis binding and enzyme kinetic data. Biochem. J. 293: 595-599.
    • (1993) Biochem. J. , vol.293 , pp. 595-599
    • Molnar, M.1    Vas, M.2
  • 30
    • 0030250857 scopus 로고    scopus 로고
    • Phosphorylated nitrate reductase from spinach leaves is inhibited by 14-3-3 proteins and activated by fusicoccin
    • 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.
    • (1996) Curr. Biol. , vol.6 , pp. 1104-1113
    • Moorhead, G.1    Douglas, P.2    Morrice, N.3    Scarabel, M.4    Aitken, A.5    Mackintosh, C.6
  • 31
    • 0029871708 scopus 로고    scopus 로고
    • Interaction of 14-3-3 with signaling proteins is mediated by the recognition of phosphoserine
    • Muslin, A.J., Tanner, J.W., Allen, P.M. and Shaw, A.S. (1996) Interaction of 14-3-3 with signaling proteins is mediated by the recognition of phosphoserine. Cell 84: 889-897.
    • (1996) Cell , vol.84 , pp. 889-897
    • Muslin, A.J.1    Tanner, J.W.2    Allen, P.M.3    Shaw, A.S.4
  • 32
    • 0033564588 scopus 로고    scopus 로고
    • The choice of refernce cell in the analysis of kinetic data using BIAcore
    • Ober, R.J. and Ward, E.S. (1999) The choice of refernce cell in the analysis of kinetic data using BIAcore. Anal. Biochem. 271: 70-80.
    • (1999) Anal. Biochem. , vol.271 , pp. 70-80
    • Ober, R.J.1    Ward, E.S.2
  • 33
    • 0032568665 scopus 로고    scopus 로고
    • 14-3-3ξ binds a phosphorylated Raf peptide and an unphosphorylated peptide via its conserved amphipathic groove
    • Petosa, C., Masters, S.C., Bankston, L.A., Pohl, J., Wang, B., Fu, H. and Liddington, R.C. (1998) 14-3-3ξ binds a phosphorylated Raf peptide and an unphosphorylated peptide via its conserved amphipathic groove. J. Biol. Chem. 273: 16305-16310.
    • (1998) J. Biol. Chem. , vol.273 , pp. 16305-16310
    • Petosa, C.1    Masters, S.C.2    Bankston, L.A.3    Pohl, J.4    Wang, B.5    Fu, H.6    Liddington, R.C.7
  • 35
    • 0026063235 scopus 로고
    • Fluorescence resonance energy transfer mapping of the fourth of six nucleotide-binding sites of chloroplast coupling factor 1
    • Shapiro, A.B., Gibson, K.D., Scheraga, H.A. and McCarty, R.E. (1991) Fluorescence resonance energy transfer mapping of the fourth of six nucleotide-binding sites of chloroplast coupling factor 1. J. Biol. Chem. 266: 17276-17285.
    • (1991) J. Biol. Chem. , vol.266 , pp. 17276-17285
    • Shapiro, A.B.1    Gibson, K.D.2    Scheraga, H.A.3    McCarty, R.E.4
  • 36
    • 0032508671 scopus 로고    scopus 로고
    • Site-specfic regulatory interaction betwn spinach leaf sucrose-phosphate synthase and 14-3-3 proteins
    • Toroser, D., Athwal, G.S. and Huber, S.C. (1998) Site-specfic regulatory interaction betwn spinach leaf sucrose-phosphate synthase and 14-3-3 proteins. FEBS Lett. 435: 110-114.
    • (1998) FEBS Lett. , vol.435 , pp. 110-114
    • Toroser, D.1    Athwal, G.S.2    Huber, S.C.3
  • 37
    • 0029815121 scopus 로고    scopus 로고
    • Molecular evolution of the 14-3-3 protein family
    • Wang, W. and Shakes, D.C. (1996) Molecular evolution of the 14-3-3 protein family. J. Mol. Evol. 43: 384-398.
    • (1996) J. Mol. Evol. , vol.43 , pp. 384-398
    • Wang, W.1    Shakes, D.C.2
  • 38
    • 0032999455 scopus 로고    scopus 로고
    • 14-3-3 proteins control proteolysis of nitrate reductase in spinach leaves
    • Weiner, H. and Kaiser, W.M. (1999) 14-3-3 proteins control proteolysis of nitrate reductase in spinach leaves. FEBS Lett. 455: 75-78.
    • (1999) FEBS Lett. , vol.455 , pp. 75-78
    • Weiner, H.1    Kaiser, W.M.2
  • 40
    • 0031106133 scopus 로고    scopus 로고
    • The heterologous interaction among plant 14-3-3 proteins and indentification of regions that are important for dimerization
    • Wu, K., Lu, G., Sehnke, P. and Ferl, R.J. (1997) The heterologous interaction among plant 14-3-3 proteins and indentification of regions that are important for dimerization. Arch. Biochem. Biophys. 339: 2-8.
    • (1997) Arch. Biochem. Biophys. , vol.339 , pp. 2-8
    • Wu, K.1    Lu, G.2    Sehnke, P.3    Ferl, R.J.4
  • 42
    • 0031451747 scopus 로고    scopus 로고
    • Intrinsic nucleotide diphosphate kinase-like activity as a novel function of 14-3-3 proteins
    • Yano, M., Mori, S., Niwa, Y., Inoue, M. and Kido, H. (1997) Intrinsic nucleotide diphosphate kinase-like activity as a novel function of 14-3-3 proteins FEBS Lett. 419: 244-248.
    • (1997) FEBS Lett. , vol.419 , pp. 244-248
    • Yano, M.1    Mori, S.2    Niwa, Y.3    Inoue, M.4    Kido, H.5
  • 43
    • 0030971096 scopus 로고    scopus 로고
    • Raf-1 kinase and exoenzyme s interact with 14-3-3ξ through a common site involving lysine 49
    • Zhang, L., Wang, H., Liu, D., Liddington, R. and Fu, H. (1997) Raf-1 kinase and exoenzyme S interact with 14-3-3ξ through a common site involving lysine 49: J. Biol. Chem. 272: 1317-13724.
    • (1997) J. Biol. Chem. , vol.272 , pp. 1317-13724
    • Zhang, L.1    Wang, H.2    Liu, D.3    Liddington, R.4    Fu, H.5


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