메뉴 건너뛰기




Volumn 11, Issue 12, 1999, Pages 2393-2405

Novel protein kinases associated with calcineurin B-like calcium sensors in Arabidopsis

Author keywords

[No Author keywords available]

Indexed keywords

ARABIDOPSIS;

EID: 0033388972     PISSN: 10404651     EISSN: None     Source Type: Journal    
DOI: 10.1105/tpc.11.12.2393     Document Type: Article
Times cited : (291)

References (62)
  • 1
    • 0025936416 scopus 로고
    • Complementation of snf1, a mutation affecting global regulation of carbon metabolism in yeast, by a plant protein kinase complementary DNA
    • Alderson, A., Sabelli, P.A., Dickinson, J.R., Cole, D., Richardson, M., Kreis, M., Shewry, P.R., and Halford, N.G. (1991). Complementation of snf1, a mutation affecting global regulation of carbon metabolism in yeast, by a plant protein kinase complementary DNA. Proc. Natl. Acad. Sci. USA 88, 8602-8605.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 8602-8605
    • Alderson, A.1    Sabelli, P.A.2    Dickinson, J.R.3    Cole, D.4    Richardson, M.5    Kreis, M.6    Shewry, P.R.7    Halford, N.G.8
  • 2
    • 0028831029 scopus 로고
    • 2+-permeable slow vacuolar ion channel of stomatal guard cells
    • 2+-permeable slow vacuolar ion channel of stomatal guard cells. Plant Cell 7, 1473-1483.
    • (1995) Plant Cell , vol.7 , pp. 1473-1483
    • Allen, G.J.1    Sanders, D.2
  • 4
    • 0032031455 scopus 로고    scopus 로고
    • Characterization of a sorghum bicolor gene family encoding putative protein kinases with a high similarity to the yeast SNF1 protein kinase
    • Annen, F., and Stockhaus, J. (1998). Characterization of a Sorghum bicolor gene family encoding putative protein kinases with a high similarity to the yeast SNF1 protein kinase. Plant Mol. Biol. 36, 529-539.
    • (1998) Plant Mol. Biol. , vol.36 , pp. 529-539
    • Annen, F.1    Stockhaus, J.2
  • 5
    • 0030803832 scopus 로고    scopus 로고
    • Reversible protein phosphorylation regulates the activity of the slow-vacuolar ion channel
    • Bethke, P.C., and Jones, R.L. (1997). Reversible protein phosphorylation regulates the activity of the slow-vacuolar ion channel. Plant J. 11, 1227-1235.
    • (1997) Plant J. , vol.11 , pp. 1227-1235
    • Bethke, P.C.1    Jones, R.L.2
  • 6
    • 0032895315 scopus 로고    scopus 로고
    • Intracellular neuronal calcium sensor proteins: A family of EF-hand calcium binding proteins in search of a function
    • Braunewell, K.-H., and Gundelfinger, E.D. (1999). Intracellular neuronal calcium sensor proteins: A family of EF-hand calcium binding proteins in search of a function. Cell Tissue Res. 295, 1-12.
    • (1999) Cell Tissue Res. , vol.295 , pp. 1-12
    • Braunewell, K.-H.1    Gundelfinger, E.D.2
  • 8
    • 0028825379 scopus 로고
    • Rhodopsin kinase inhibition by recoverin: Function of recoverin myristoylation
    • Calvert, P.D., Klenchin, V.A., and Bownds, M.D. (1995). Rhodopsin kinase inhibition by recoverin: Function of recoverin myristoylation. J. Biol. Chem. 270, 24127-24129.
    • (1995) J. Biol. Chem. , vol.270 , pp. 24127-24129
    • Calvert, P.D.1    Klenchin, V.A.2    Bownds, M.D.3
  • 10
    • 0025940629 scopus 로고
    • The two-hybrid system: A method to identify and clone genes for proteins that interact with a protein of interest
    • Chien, C.-T., Bartel, P.L., Sternglanz, R., and Fields, S. (1991). The two-hybrid system: A method to identify and clone genes for proteins that interact with a protein of interest. Proc. Natl. Acad. Sci. USA 88, 9578-9582.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 9578-9582
    • Chien, C.-T.1    Bartel, P.L.2    Sternglanz, R.3    Fields, S.4
  • 12
    • 0029149085 scopus 로고
    • Molecular and structural basis of target recognition by calmodulin
    • Crivici, A., and Ikura, M. (1995). Molecular and structural basis of target recognition by calmodulin. Annu. Rev. Biophys. Biomol. Struct. 24, 85-116.
    • (1995) Annu. Rev. Biophys. Biomol. Struct. , vol.24 , pp. 85-116
    • Crivici, A.1    Ikura, M.2
  • 13
    • 0032580202 scopus 로고    scopus 로고
    • Calcium oscillations increase the efficiency and specificity of gene expression
    • Dolmetsch, R.E., Xu, K., and Lewis, R.S. (1998). Calcium oscillations increase the efficiency and specificity of gene expression. Nature 392, 933-936.
    • (1998) Nature , vol.392 , pp. 933-936
    • Dolmetsch, R.E.1    Xu, K.2    Lewis, R.S.3
  • 15
    • 0029895156 scopus 로고    scopus 로고
    • Calcium spiking in plant root hairs responding to rhizobium nodulation signals
    • Ehrhardt, D.W., Wais, R., and Long, S.R. (1996). Calcium spiking in plant root hairs responding to rhizobium nodulation signals. Cell 85, 673-681.
    • (1996) Cell , vol.85 , pp. 673-681
    • Ehrhardt, D.W.1    Wais, R.2    Long, S.R.3
  • 16
    • 0031426195 scopus 로고    scopus 로고
    • 2+-selective microelectrode tests and fura-dextran ratio imaging
    • 2+-selective microelectrode tests and fura-dextran ratio imaging. Plant Physiol. 114, 39-45.
    • (1997) Plant Physiol. , vol.114 , pp. 39-45
    • Felle, H.H.1    Hepler, P.K.2
  • 17
    • 0029832826 scopus 로고    scopus 로고
    • Growth of pollen tubes of Papaver rhoeas is regulated by a slow-moving calcium wave propagated by inositol 1,4,5-trisphosphate
    • Franklin-Tong, V.E., Drobak, B.K., Allan, A.C., Watkins, P.A.C., and Trewavas, A.J. (1996). Growth of pollen tubes of Papaver rhoeas is regulated by a slow-moving calcium wave propagated by inositol 1,4,5-trisphosphate. Plant Cell 8, 1305-1321.
    • (1996) Plant Cell , vol.8 , pp. 1305-1321
    • Franklin-Tong, V.E.1    Drobak, B.K.2    Allan, A.C.3    Watkins, P.A.C.4    Trewavas, A.J.5
  • 19
    • 0032409540 scopus 로고    scopus 로고
    • Identification of a dual-specificity protein phosphatase that inactivates MAP kinase from Arabidopsis
    • Gupta, R., Huang, Y., Kieber, J.J., and Luan, S. (1998). Identification of a dual-specificity protein phosphatase that inactivates MAP kinase from Arabidopsis. Plant J. 16, 581-590.
    • (1998) Plant J. , vol.16 , pp. 581-590
    • Gupta, R.1    Huang, Y.2    Kieber, J.J.3    Luan, S.4
  • 20
    • 0031007065 scopus 로고    scopus 로고
    • The AMP-activated protein kinase: Fuel gauge of the mammalian cell?
    • Hardie, D.G., and Carling, D. (1997). The AMP-activated protein kinase: Fuel gauge of the mammalian cell? Eur. J. Biochem. 246, 259-273.
    • (1997) Eur. J. Biochem. , vol.246 , pp. 259-273
    • Hardie, D.G.1    Carling, D.2
  • 21
    • 0031717105 scopus 로고    scopus 로고
    • The AMP-activated/SNF1 protein kinase subfamily: Metabolic sensors of the eukaryotic cells?
    • Hardie, D.G., Carling, D., and Carlson, M. (1998). The AMP-activated/SNF1 protein kinase subfamily: Metabolic sensors of the eukaryotic cells? Annu. Rev. Biochem. 67, 821-855.
    • (1998) Annu. Rev. Biochem. , vol.67 , pp. 821-855
    • Hardie, D.G.1    Carling, D.2    Carlson, M.3
  • 22
    • 0031412197 scopus 로고    scopus 로고
    • Pollen tube growth and the intracellular cytosolic calcium gradient oscillate in phase while extracellular calcium influx is delayed
    • Holdaway-Clarke, T.L., Feijo, J.A., Hackett, G.R., Kunkel, J.G., and Hepler, P.K. (1997). Pollen tube growth and the intracellular cytosolic calcium gradient oscillate in phase while extracellular calcium influx is delayed. Plant Cell 9, 1999-2010.
    • (1997) Plant Cell , vol.9 , pp. 1999-2010
    • Holdaway-Clarke, T.L.1    Feijo, J.A.2    Hackett, G.R.3    Kunkel, J.G.4    Hepler, P.K.5
  • 23
    • 0028095626 scopus 로고
    • Biochemical properties of the autophosphorylation of RLK5, a receptor-like protein kinase from Arabidopsis thaliana
    • Horn, M.A., and Walker, J.C. (1994). Biochemical properties of the autophosphorylation of RLK5, a receptor-like protein kinase from Arabidopsis thaliana. Biochim. Biophys. Acta 1208, 65-74.
    • (1994) Biochim. Biophys. Acta , vol.1208 , pp. 65-74
    • Horn, M.A.1    Walker, J.C.2
  • 24
    • 0031470701 scopus 로고    scopus 로고
    • Arabidopsis NPH1: A protein kinase with a putative redox-sensing domain
    • Huala, E., Oeller, P.W., Liscum, E., Han, I.-S., Larsen, E., and Briggs, W.R. (1997). Arabidopsis NPH1: A protein kinase with a putative redox-sensing domain. Science 278, 2120-2123.
    • (1997) Science , vol.278 , pp. 2120-2123
    • Huala, E.1    Oeller, P.W.2    Liscum, E.3    Han, I.-S.4    Larsen, E.5    Briggs, W.R.6
  • 25
    • 0032928915 scopus 로고    scopus 로고
    • Regulation of G-protein-coupled receptor kinase subtypes by calcium sensor proteins
    • Iacovelli, L., Sallese, M., Mariggio, S., and De Blasi, A. (1999). Regulation of G-protein-coupled receptor kinase subtypes by calcium sensor proteins. FASEB J. 13, 1-8.
    • (1999) FASEB J. , vol.13 , pp. 1-8
    • Iacovelli, L.1    Sallese, M.2    Mariggio, S.3    De Blasi, A.4
  • 26
    • 0020529962 scopus 로고
    • Transformation of intact yeast (Saccharomyces cerevisiae) cells treated with alkali cations
    • Ito, H., Fukuda, Y., Murata, K., and Kimura, A. (1983). Transformation of intact yeast (Saccharomyces cerevisiae) cells treated with alkali cations. J. Bacteriol. 153, 163-168.
    • (1983) J. Bacteriol. , vol.153 , pp. 163-168
    • Ito, H.1    Fukuda, Y.2    Murata, K.3    Kimura, A.4
  • 27
    • 0027483936 scopus 로고
    • Optimization of the resolution of phosphoamino acids by one-dimensional thin-layer electro-phoresis
    • Jelinek, T., and Weber, M.J. (1993). Optimization of the resolution of phosphoamino acids by one-dimensional thin-layer electro-phoresis. BioTechniques 15, 629-630.
    • (1993) Biotechniques , vol.15 , pp. 629-630
    • Jelinek, T.1    Weber, M.J.2
  • 28
    • 0030671551 scopus 로고    scopus 로고
    • Protein-protein interactions among the AUX/IAA proteins
    • Kim, J., Harter, K., and Theologis, A. (1997). Protein-protein interactions among the AUX/IAA proteins. Proc. Natl. Acad. Sci. USA 94, 11786-11791.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 11786-11791
    • Kim, J.1    Harter, K.2    Theologis, A.3
  • 29
    • 0028848524 scopus 로고
    • Crystal structures of human calcineurin and the human FKBP12-FK506-calcineurin complex
    • Kissinger, C.R., et al. (1995). Crystal structures of human calcineurin and the human FKBP12-FK506-calcineurin complex. Nature 378, 641-644.
    • (1995) Nature , vol.378 , pp. 641-644
    • Kissinger, C.R.1
  • 31
    • 0032577483 scopus 로고    scopus 로고
    • Regulation of calmodulin-stimulated protein phosphatase, calcineurin
    • Klee, C.B., Ren, H., and Wang, X. (1998). Regulation of calmodulin-stimulated protein phosphatase, calcineurin. J. Biol. Chem. 273, 13367-13370.
    • (1998) J. Biol. Chem. , vol.273 , pp. 13367-13370
    • Klee, C.B.1    Ren, H.2    Wang, X.3
  • 32
    • 0030096580 scopus 로고    scopus 로고
    • Cold calcium signaling in Arabidopsis involves two cellular pools and a change in calcium signature after acclimation
    • Knight, H., Trewavas, A.J., and Knight, M.R. (1996). Cold calcium signaling in Arabidopsis involves two cellular pools and a change in calcium signature after acclimation. Plant Cell 8, 489-503.
    • (1996) Plant Cell , vol.8 , pp. 489-503
    • Knight, H.1    Trewavas, A.J.2    Knight, M.R.3
  • 33
    • 0031279985 scopus 로고    scopus 로고
    • Calcium signaling in Arabidopsis thaliana responding to drought and salinity
    • Knight, H., Trewavas, A.J., and Knight, M.R. (1997). Calcium signaling in Arabidopsis thaliana responding to drought and salinity. Plant J. 12, 1067-1078.
    • (1997) Plant J. , vol.12 , pp. 1067-1078
    • Knight, H.1    Trewavas, A.J.2    Knight, M.R.3
  • 34
    • 0026419945 scopus 로고
    • Transgenic plant aequorin reports the effects of touch and cold-shock and elicitors on cytoplasmic calcium
    • Knight, M.R., Campbell, A.K., Smith, S.M., and Trewavas, A.J. (1991). Transgenic plant aequorin reports the effects of touch and cold-shock and elicitors on cytoplasmic calcium. Nature 352, 524-526.
    • (1991) Nature , vol.352 , pp. 524-526
    • Knight, M.R.1    Campbell, A.K.2    Smith, S.M.3    Trewavas, A.J.4
  • 35
    • 0033551073 scopus 로고    scopus 로고
    • Genes encoding calcineurin B-like protein in Arabidopsis are differentially regulated by stress signals
    • Kudla, J., Xu, Q., Gruissem, W., and Luan, S. (1999). Genes encoding calcineurin B-like protein in Arabidopsis are differentially regulated by stress signals. Proc. Natl. Acad. Sci. USA 96, 4718-4723.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 4718-4723
    • Kudla, J.1    Xu, Q.2    Gruissem, W.3    Luan, S.4
  • 37
    • 0032546821 scopus 로고    scopus 로고
    • A calcium sensor homolog required for plant salt tolerance
    • Liu, J., and Zhu, J.-K. (1998). A calcium sensor homolog required for plant salt tolerance. Science 280, 1943-1945.
    • (1998) Science , vol.280 , pp. 1943-1945
    • Liu, J.1    Zhu, J.-K.2
  • 39
    • 0030911771 scopus 로고    scopus 로고
    • Calcium ions as second messengers in guard cell signal transduction
    • McAinsh, M.R., Brownlee, C., and Hetherington, A.M. (1997). Calcium ions as second messengers in guard cell signal transduction. Physiol. Plant. 100, 16-29.
    • (1997) Physiol. Plant. , vol.100 , pp. 16-29
    • McAinsh, M.R.1    Brownlee, C.2    Hetherington, A.M.3
  • 40
    • 0032531742 scopus 로고    scopus 로고
    • Calcium regulation of Ndr protein kinase mediated by S100 calcium-binding proteins
    • Millward, T.A., Heizmann, C.W., Schafer, B.W., and Hemmings, B.A. (1998). Calcium regulation of Ndr protein kinase mediated by S100 calcium-binding proteins. EMBO J. 17, 5913-5922.
    • (1998) EMBO J. , vol.17 , pp. 5913-5922
    • Millward, T.A.1    Heizmann, C.W.2    Schafer, B.W.3    Hemmings, B.A.4
  • 41
    • 0028274294 scopus 로고
    • Characterization of tobacco protein kinase NPK5, a homolog of Saccharomyces cerevisiae SNF1 that constitutively activates expression of the glucose-repressible SUC2 gene for a secreted invertase of S. cerevisiae
    • Muranaka, T., Banno, H., and Machida, Y. (1994). Characterization of tobacco protein kinase NPK5, a homolog of Saccharomyces cerevisiae SNF1 that constitutively activates expression of the glucose-repressible SUC2 gene for a secreted invertase of S. cerevisiae. Mol. Cell. Biol. 14, 2958-2965.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 2958-2965
    • Muranaka, T.1    Banno, H.2    Machida, Y.3
  • 42
    • 0027156395 scopus 로고
    • Calcium-calmodulin-dependent and independent phytochrome signal transduction pathways
    • Neuhaus, G., Bowler, C., Kern, R., and Chua, N.-H. (1993). Calcium-calmodulin-dependent and independent phytochrome signal transduction pathways. Cell 73, 937-952.
    • (1993) Cell , vol.73 , pp. 937-952
    • Neuhaus, G.1    Bowler, C.2    Kern, R.3    Chua, N.-H.4
  • 45
    • 11944252555 scopus 로고
    • Calcium-modulated proteins targets of intracellular calcium signals in higher plants
    • Roberts, D.M., and Harmon, A.C. (1992). Calcium-modulated proteins targets of intracellular calcium signals in higher plants. Annu. Rev. Plant Physiol. Plant Mol. Biol. 43, 375-414.
    • (1992) Annu. Rev. Plant Physiol. Plant Mol. Biol. , vol.43 , pp. 375-414
    • Roberts, D.M.1    Harmon, A.C.2
  • 46
    • 0029915683 scopus 로고    scopus 로고
    • Calcium-bound recoverin targets rhodopsin kinase to membranes to inhibit rhodopsin phosphorylation
    • Sanada, K., Shimizu, F., Kameyama, K., Haga, K., Haga, T., and Fukada, Y. (1996). Calcium-bound recoverin targets rhodopsin kinase to membranes to inhibit rhodopsin phosphorylation. FEBS Lett. 384, 227-230.
    • (1996) FEBS Lett. , vol.384 , pp. 227-230
    • Sanada, K.1    Shimizu, F.2    Kameyama, K.3    Haga, K.4    Haga, T.5    Fukada, Y.6
  • 47
    • 0028213889 scopus 로고
    • Light and nutritional regulation of transcripts encoding a wheat protein kinase homolog is mediated by cytokinins
    • Sano, H., and Youssefian, S. (1994). Light and nutritional regulation of transcripts encoding a wheat protein kinase homolog is mediated by cytokinins. Proc. Natl. Acad. Sci. USA 91, 2582-2586.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 2582-2586
    • Sano, H.1    Youssefian, S.2
  • 49
    • 0024799254 scopus 로고
    • High efficiency transformation of intact yeast cells using single stranded nucleic acids as a carrier
    • Schiestl, R.H., and Gietz, R.D. (1989). High efficiency transformation of intact yeast cells using single stranded nucleic acids as a carrier. Curr. Genet. 16, 339-346.
    • (1989) Curr. Genet. , vol.16 , pp. 339-346
    • Schiestl, R.H.1    Gietz, R.D.2
  • 50
    • 0030657770 scopus 로고    scopus 로고
    • Cloning and characterization of a human STE20-like protein kinase with unusual cofactor requirements
    • Schinkmann, K., and Blenis, J. (1997). Cloning and characterization of a human STE20-like protein kinase with unusual cofactor requirements. J. Biol. Chem. 272, 28695-28703.
    • (1997) J. Biol. Chem. , vol.272 , pp. 28695-28703
    • Schinkmann, K.1    Blenis, J.2
  • 51
    • 0030874691 scopus 로고    scopus 로고
    • Biochemical evidence that the Saccharomyces cerevisiae YGR262C gene, required for normal growth, encodes a novel Ser-Thr-specific protein kinase
    • Stocchetto, S., Marin, O., Carignani, G., and Pinna, L.A. (1997). Biochemical evidence that the Saccharomyces cerevisiae YGR262C gene, required for normal growth, encodes a novel Ser-Thr-specific protein kinase. FEBS Lett. 414, 171-175.
    • (1997) FEBS Lett. , vol.414 , pp. 171-175
    • Stocchetto, S.1    Marin, O.2    Carignani, G.3    Pinna, L.A.4
  • 52
    • 0029310678 scopus 로고
    • Plant protein kinase families and signal transduction
    • Stone, J.M., and Walker, J.C. (1995). Plant protein kinase families and signal transduction. Plant Physiol. 108, 451-457.
    • (1995) Plant Physiol. , vol.108 , pp. 451-457
    • Stone, J.M.1    Walker, J.C.2
  • 53
    • 15844383337 scopus 로고    scopus 로고
    • Cloning and characterization of a novel serine-threonine protein kinase expressed in early Xenopus embryos
    • Su, J.-Y., Erikson, E., and Maller, J.L. (1996). Cloning and characterization of a novel serine-threonine protein kinase expressed in early Xenopus embryos. J. Biol. Chem. 271, 14430-14437.
    • (1996) J. Biol. Chem. , vol.271 , pp. 14430-14437
    • Su, J.-Y.1    Erikson, E.2    Maller, J.L.3
  • 55
    • 0028724539 scopus 로고
    • Mechanical signaling, calcium and plant form
    • Trewavas, A., and Knight, M. (1994). Mechanical signaling, calcium and plant form. Plant Mol. Biol. 26, 1329-1341.
    • (1994) Plant Mol. Biol. , vol.26 , pp. 1329-1341
    • Trewavas, A.1    Knight, M.2
  • 56
    • 0028506122 scopus 로고
    • Calmodulin: A versatile calcium mediator protein
    • Vogel, H.J. (1994). Calmodulin: A versatile calcium mediator protein. Biochem. Cell Biol. 72, 357-376.
    • (1994) Biochem. Cell Biol. , vol.72 , pp. 357-376
    • Vogel, H.J.1
  • 58
    • 0031213767 scopus 로고    scopus 로고
    • Cytoplasmic free calcium distributions during the development of root hairs of Arabidopsis thaliana
    • Wymer, C.L., Bibikova, T.N., and Gilroy, S. (1997). Cytoplasmic free calcium distributions during the development of root hairs of Arabidopsis thaliana. Plant J. 12, 427-439.
    • (1997) Plant J. , vol.12 , pp. 427-439
    • Wymer, C.L.1    Bibikova, T.N.2    Gilroy, S.3
  • 59
    • 0032076827 scopus 로고    scopus 로고
    • Identification of a stress-responsive protein tyrosine phosphatase
    • Xu, Q., Fu, H., and Luan, S. (1998a). Identification of a stress-responsive protein tyrosine phosphatase. Plant Cell 10, 849-858.
    • (1998) Plant Cell , vol.10 , pp. 849-858
    • Xu, Q.1    Fu, H.2    Luan, S.3
  • 60
    • 0032143086 scopus 로고    scopus 로고
    • A novel FKBP12 that does not mediate action of immunosuppressive drugs FK506 and rapamycin
    • Xu, Q., Kudla, J., and Luan, S. (1998b). A novel FKBP12 that does not mediate action of immunosuppressive drugs FK506 and rapamycin. Plant J. 15, 511-519.
    • (1998) Plant J. , vol.15 , pp. 511-519
    • Xu, Q.1    Kudla, J.2    Luan, S.3
  • 61
    • 0032029230 scopus 로고    scopus 로고
    • Activation of the tobacco SIP kinase by both a cell wall-derived carbohydrate elicitor and purified proteinaceous elicitins from Phytophthora spp.
    • Zhang, S., Du, H., and Klessig, D.F. (1998). Activation of the tobacco SIP kinase by both a cell wall-derived carbohydrate elicitor and purified proteinaceous elicitins from Phytophthora spp. Plant Cell 10, 435-449.
    • (1998) Plant Cell , vol.10 , pp. 435-449
    • Zhang, S.1    Du, H.2    Klessig, D.F.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.