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Volumn 3, Issue 8, 1998, Pages 299-304

Calmodulin, calmodulin-related proteins and plant responses to the environment

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EID: 0031926552     PISSN: 13601385     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1360-1385(98)01284-9     Document Type: Review
Times cited : (208)

References (41)
  • 1
    • 0027223245 scopus 로고
    • Imaging calcium dynamics in living plant cells and tissues
    • Read N.D.et al. Imaging calcium dynamics in living plant cells and tissues. Cell Biol. Int. 17:1993;111-125.
    • (1993) Cell Biol. Int. , vol.17 , pp. 111-125
    • Read, N.D.1
  • 3
    • 0028534876 scopus 로고
    • Emerging themes of plant signal transduction
    • Bowler C., Chua N.-H. Emerging themes of plant signal transduction. Plant Cell. 6:1994;1529-1541.
    • (1994) Plant Cell , vol.6 , pp. 1529-1541
    • Bowler, C.1    Chua, N.-H.2
  • 4
    • 51249167396 scopus 로고
    • 35S-labeled recombinant calmodulin as a probe
    • 35S-labeled recombinant calmodulin as a probe. Plant Mol. Biol. Rep. 10:1992;199-206.
    • (1992) Plant Mol. Biol. Rep. , vol.10 , pp. 199-206
    • Fromm, H.1    Chua, N-H.2
  • 5
    • 0024396312 scopus 로고
    • Crystal structure of the helix-loop-helix calcium-binding proteins
    • Natalie C., Strynadka J., James M.N.G. Crystal structure of the helix-loop-helix calcium-binding proteins. Annu. Rev. Biochem. 58:1989;951-958.
    • (1989) Annu. Rev. Biochem. , vol.58 , pp. 951-958
    • Natalie, C.1    Strynadka, J.2    James, M.N.G.3
  • 6
    • 0028921581 scopus 로고
    • Calmodulin-binding domains: Just two-faced or multifaceted?
    • James P., Vorherr T., Carafoli E. Calmodulin-binding domains: just two-faced or multifaceted? Trends Biochem. Sci. 20:1995;38-42.
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 38-42
    • James, P.1    Vorherr, T.2    Carafoli, E.3
  • 7
    • 0029149085 scopus 로고
    • Molecular and structural basis of target recognition by calmodulin
    • Crivici A., Ikura M. Molecular and structural basis of target recognition by calmodulin. Annu. Rev. Biomol. Struct. 24:1995;85-116.
    • (1995) Annu. Rev. Biomol. Struct. , vol.24 , pp. 85-116
    • Crivici, A.1    Ikura, M.2
  • 8
    • 0027420553 scopus 로고
    • The essential mitotic target of calmodulin is the 110-kilodalton component of the spindle pole body in Saccharomyces cerevisiae
    • Geiser J.R.et al. The essential mitotic target of calmodulin is the 110-kilodalton component of the spindle pole body in Saccharomyces cerevisiae. Mol. Cell. Biol. 13:1993;7913-7924.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 7913-7924
    • Geiser, J.R.1
  • 9
    • 0032510478 scopus 로고    scopus 로고
    • Translocation of calmodulin to the nucleus supports CREB phosphorylation in hypocampal neurons
    • Deisseroth K., Heist E.K., Tsien R.W. Translocation of calmodulin to the nucleus supports CREB phosphorylation in hypocampal neurons. Nature. 392:1998;198-202.
    • (1998) Nature , vol.392 , pp. 198-202
    • Deisseroth, K.1    Heist, E.K.2    Tsien, R.W.3
  • 10
    • 0001281471 scopus 로고    scopus 로고
    • Differential activation of NAD kinase by plant calmodulin isoforms. The critical role of domain I
    • Lee S.H.et al. Differential activation of NAD kinase by plant calmodulin isoforms. The critical role of domain I. J. Biol. Chem. 272:1997;9252-9259.
    • (1997) J. Biol. Chem. , vol.272 , pp. 9252-9259
    • Lee, S.H.1
  • 11
    • 0030063768 scopus 로고    scopus 로고
    • Differential stimulation of NAD kinase and binding of peptide substrates by wild-type and mutant plant calmodulin isoforms
    • Liao B., Gawienowski M.C., Zielinski R.E. Differential stimulation of NAD kinase and binding of peptide substrates by wild-type and mutant plant calmodulin isoforms. Arch. Biochem. Biophys. 327:1996;53-60.
    • (1996) Arch. Biochem. Biophys. , vol.327 , pp. 53-60
    • Liao, B.1    Gawienowski, M.C.2    Zielinski, R.E.3
  • 12
    • 0027085882 scopus 로고
    • Characterization of the human calmodulin-like protein expressed in Escherichia coli
    • Rhyner J.A.et al. Characterization of the human calmodulin-like protein expressed in Escherichia coli. Biochemistry. 31:1992;12826-12832.
    • (1992) Biochemistry , vol.31 , pp. 12826-12832
    • Rhyner, J.A.1
  • 13
    • 0029999946 scopus 로고    scopus 로고
    • Characterization of the calmodulin gene family in wheat: Structure, chromosomal location, and evolutionary aspects
    • Yang T.et al. Characterization of the calmodulin gene family in wheat: structure, chromosomal location, and evolutionary aspects. Mol. Gen. Genet. 252:1996;684-694.
    • (1996) Mol. Gen. Genet. , vol.252 , pp. 684-694
    • Yang, T.1
  • 14
    • 0030846077 scopus 로고    scopus 로고
    • Plant responses to environmental stress: Regulation and function of the Arabidopsis TCH genes
    • Braam J.et al. Plant responses to environmental stress: regulation and function of the Arabidopsis TCH genes. Planta. 203:1997;35-41.
    • (1997) Planta , vol.203 , pp. 35-41
    • Braam, J.1
  • 15
    • 0027597441 scopus 로고
    • Isolation of an Arabidopsis cDNA sequence encoding a 22 kDa calcium-binding protein (CaBP-22) related to calmodulin
    • Ling V., Zielinski R.E. Isolation of an Arabidopsis cDNA sequence encoding a 22 kDa calcium-binding protein (CaBP-22) related to calmodulin. Plant Mol. Biol. 22:1993;207-214.
    • (1993) Plant Mol. Biol. , vol.22 , pp. 207-214
    • Ling, V.1    Zielinski, R.E.2
  • 16
    • 0028387457 scopus 로고
    • Differential expression of two calmodulin genes in response to physical and chemical stimuli
    • Botella J.R., Arteca R.N. Differential expression of two calmodulin genes in response to physical and chemical stimuli. Plant Mol. Biol. 24:1994;757-766.
    • (1994) Plant Mol. Biol. , vol.24 , pp. 757-766
    • Botella, J.R.1    Arteca, R.N.2
  • 17
    • 0030220423 scopus 로고    scopus 로고
    • Cold-shock regulation of the Arabidopsis TCH genes and the effects of modulating intracellular calcium levels
    • Polisensky D.H., Braam J. Cold-shock regulation of the Arabidopsis TCH genes and the effects of modulating intracellular calcium levels. Plant Physiol. 111:1996;1271-1279.
    • (1996) Plant Physiol. , vol.111 , pp. 1271-1279
    • Polisensky, D.H.1    Braam, J.2
  • 19
    • 0032061003 scopus 로고    scopus 로고
    • Developmentally regulated organ-, tissue-, and cell-specific expression of calmodulin genes in common wheat
    • Yang T.et al. Developmentally regulated organ-, tissue-, and cell-specific expression of calmodulin genes in common wheat. Plant Mol. Biol. 37:1998;109-120.
    • (1998) Plant Mol. Biol. , vol.37 , pp. 109-120
    • Yang, T.1
  • 20
    • 0031432051 scopus 로고    scopus 로고
    • Signal perception and transduction: The origin of the phenotype
    • Trewavas A.J., Malho R. Signal perception and transduction: the origin of the phenotype. Plant Cell. 9:1997;1181-1195.
    • (1997) Plant Cell , vol.9 , pp. 1181-1195
    • Trewavas, A.J.1    Malho, R.2
  • 21
    • 0030945196 scopus 로고    scopus 로고
    • Sequence motifs for calmodulin recognition
    • Rhoads A.R., Friedberg F. Sequence motifs for calmodulin recognition. FASEB J. 11:1997;331-340.
    • (1997) FASEB J. , vol.11 , pp. 331-340
    • Rhoads, A.R.1    Friedberg, F.2
  • 22
    • 0031080102 scopus 로고    scopus 로고
    • Race-specific elicitors of Cladosporium fulvum promote translocation of cytosolic components of NADPH oxidase to the plasma membrane of tomato cells
    • Xing T., Higgins V.J., Blumwald E. Race-specific elicitors of Cladosporium fulvum promote translocation of cytosolic components of NADPH oxidase to the plasma membrane of tomato cells. Plant Cell. 9:1997;249-259.
    • (1997) Plant Cell , vol.9 , pp. 249-259
    • Xing, T.1    Higgins, V.J.2    Blumwald, E.3
  • 23
    • 0029814424 scopus 로고    scopus 로고
    • The role of calmodulin in the gravitropic response of the Arabidopsis thaliana agr-3 mutant
    • Sinclair W.et al. The role of calmodulin in the gravitropic response of the Arabidopsis thaliana agr-3 mutant. Planta. 199:1996;343-351.
    • (1996) Planta , vol.199 , pp. 343-351
    • Sinclair, W.1
  • 24
    • 0029690122 scopus 로고    scopus 로고
    • Characterization of a calcium/calmodulin-dependent kinase homolog from maize roots showing light-regulated gravitropism
    • Lu Y-T., Hidaka H., Feldman L.J. Characterization of a calcium/calmodulin-dependent kinase homolog from maize roots showing light-regulated gravitropism. Planta. 199:1996;18-24.
    • (1996) Planta , vol.199 , pp. 18-24
    • Lu, Y-T.1    Hidaka, H.2    Feldman, L.J.3
  • 25
    • 0030249805 scopus 로고    scopus 로고
    • Distinct UV-B and UV-A/blue light signal transduction pathways induce chalcone synthase gene expression in Arabidopsis cells
    • Christie J.M., Jenkins G.I. Distinct UV-B and UV-A/blue light signal transduction pathways induce chalcone synthase gene expression in Arabidopsis cells. Plant Cell. 8:1996;1555-1567.
    • (1996) Plant Cell , vol.8 , pp. 1555-1567
    • Christie, J.M.1    Jenkins, G.I.2
  • 26
    • 0031397032 scopus 로고    scopus 로고
    • 2+ and calmodulin dynamics during photopolarization in Fucus serratus zygotes
    • 2+ and calmodulin dynamics during photopolarization in Fucus serratus zygotes. Plant Physiol. 115:1996;249-261.
    • (1996) Plant Physiol. , vol.115 , pp. 249-261
    • Love, J.1    Brownlee, C.2    Trewavas, A.J.3
  • 27
    • 0029801217 scopus 로고    scopus 로고
    • Regulated expression of a calmodulin isoform alters growth and development in potato
    • Poovaiah B.W.et al. Regulated expression of a calmodulin isoform alters growth and development in potato. J. Plant Physiol. 149:1996;553-558.
    • (1996) J. Plant Physiol. , vol.149 , pp. 553-558
    • Poovaiah, B.W.1
  • 28
    • 0030907241 scopus 로고    scopus 로고
    • Transgenic tobacco expressing a foreign calmodulin gene shows an enhanced production of active oxygen species
    • Harding S.A., Oh S.H., Roberts D.M. Transgenic tobacco expressing a foreign calmodulin gene shows an enhanced production of active oxygen species. EMBO J. 16:1997;1137-1144.
    • (1997) EMBO J. , vol.16 , pp. 1137-1144
    • Harding, S.A.1    Oh, S.H.2    Roberts, D.M.3
  • 29
    • 0030014203 scopus 로고    scopus 로고
    • Calmodulin binding to glutamate decarboxylase is required for regulation of glutamate and GABA metabolism and normal development in plants
    • Baum G.et al. Calmodulin binding to glutamate decarboxylase is required for regulation of glutamate and GABA metabolism and normal development in plants. EMBO J. 15:1996;2988-2996.
    • (1996) EMBO J. , vol.15 , pp. 2988-2996
    • Baum, G.1
  • 30
    • 0030979742 scopus 로고    scopus 로고
    • Essential role of a kinesin-like protein in Arabidopsis trichome morphogenesis
    • Oppenheimer D.G.et al. Essential role of a kinesin-like protein in Arabidopsis trichome morphogenesis. Proc. Natl. Acad. Sci. U. S. A. 94:1997;6261-6266.
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 6261-6266
    • Oppenheimer, D.G.1
  • 31
    • 0030060208 scopus 로고    scopus 로고
    • Activation of a recombinant petunia glutamate decarboxylase by calcium/calmodulin or by a monoclonal antibody which recognizes the calmodulin binding domain
    • Snedden W.A.et al. Activation of a recombinant petunia glutamate decarboxylase by calcium/calmodulin or by a monoclonal antibody which recognizes the calmodulin binding domain. J. Biol. Chem. 271:1996;4148-4153.
    • (1996) J. Biol. Chem. , vol.271 , pp. 4148-4153
    • Snedden, W.A.1
  • 32
    • 0031403384 scopus 로고    scopus 로고
    • The metabolism and function of γ-aminobutyric acid
    • Bown A.W., Shelp B.J. The metabolism and function of γ-aminobutyric acid. Plant Physiol. 115:1997;1-5.
    • (1997) Plant Physiol. , vol.115 , pp. 1-5
    • Bown, A.W.1    Shelp, B.J.2
  • 33
    • 0030019538 scopus 로고    scopus 로고
    • Light-modulated abundance of an mRNA encoding a calmodulin-regulated, chromatin-associated NTPase in pea
    • Hsieh H-L.et al. Light-modulated abundance of an mRNA encoding a calmodulin-regulated, chromatin-associated NTPase in pea. Plant Mol. Biol. 30:1996;135-147.
    • (1996) Plant Mol. Biol. , vol.30 , pp. 135-147
    • Hsieh, H-L.1
  • 34
    • 0030981112 scopus 로고    scopus 로고
    • Functional domains of plant chimeric calcium/calmodulin-dependent protein kinase: Regulation by autoinhibitory and visinin-like domains
    • Ramachandiran S.et al. Functional domains of plant chimeric calcium/calmodulin-dependent protein kinase: regulation by autoinhibitory and visinin-like domains. J. Biochem. 121:1997;984-990.
    • (1997) J. Biochem. , vol.121 , pp. 984-990
    • Ramachandiran, S.1
  • 35
    • 0031963642 scopus 로고    scopus 로고
    • 2+-ATPase (ACA2) from Arabidopsis with an N-terminal autoinhibitory domain
    • 2+-ATPase (ACA2) from Arabidopsis with an N-terminal autoinhibitory domain. J. Biol. Chem. 273:1998;1099-1106.
    • (1998) J. Biol. Chem. , vol.273 , pp. 1099-1106
    • Harper, J.F.1
  • 36
    • 0030614802 scopus 로고    scopus 로고
    • 2+-ATPase from plant vacuolar membranes with a putative regulatory domain at its N-terminus
    • 2+-ATPase from plant vacuolar membranes with a putative regulatory domain at its N-terminus. FEBS Lett. 400:1997;324-328.
    • (1997) FEBS Lett. , vol.400 , pp. 324-328
    • Malmstrom, S.1    Askerlund, P.2    Palmgren, M.G.3
  • 37
    • 0032539554 scopus 로고    scopus 로고
    • Characterization of a calmodulin-binding transporter from the plasma membrane of barley aleurone
    • Schuurink R.C.et al. Characterization of a calmodulin-binding transporter from the plasma membrane of barley aleurone. Proc. Natl. Acad. Sci. U. S. A. 95:1998;1944-1949.
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 1944-1949
    • Schuurink, R.C.1
  • 39
    • 0028445306 scopus 로고
    • A calmodulin-sensitive interaction between microtubules and a higher plant homolog of elongation factor-1 alpha
    • Durso N.A., Cyr R.J. A calmodulin-sensitive interaction between microtubules and a higher plant homolog of elongation factor-1 alpha. Plant Cell. 6:1994;893-905.
    • (1994) Plant Cell , vol.6 , pp. 893-905
    • Durso, N.A.1    Cyr, R.J.2
  • 40
    • 0028343414 scopus 로고
    • A myosin from a higher plant has structural similarities to class V myosins
    • Kinkema M., Schiefelbein J. A myosin from a higher plant has structural similarities to class V myosins. J. Mol. Biol. 239:1994;591-597.
    • (1994) J. Mol. Biol. , vol.239 , pp. 591-597
    • Kinkema, M.1    Schiefelbein, J.2
  • 41
    • 0030174916 scopus 로고    scopus 로고
    • Calmodulin isoforms differentially enhance the binding of cauliflower nuclear proteins and recombinant TGA3 to a region derived from the Arabidopsis CaM-3 promoter
    • Gawienowski M.C.et al. Calmodulin isoforms differentially enhance the binding of cauliflower nuclear proteins and recombinant TGA3 to a region derived from the Arabidopsis CaM-3 promoter. Plant Cell. 8:1996;1069-1077.
    • (1996) Plant Cell , vol.8 , pp. 1069-1077
    • Gawienowski, M.C.1


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