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Volumn 22, Issue 2, 2010, Pages 392-402

The Arabidopsis rcn1-1 mutation impairs dephosphorylation of phot2, resulting in enhanced blue light responses

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Indexed keywords

ARABIDOPSIS;

EID: 77950361848     PISSN: 10404651     EISSN: 1532298X     Source Type: Journal    
DOI: 10.1105/tpc.109.066423     Document Type: Article
Times cited : (68)

References (51)
  • 1
    • 38949214828 scopus 로고    scopus 로고
    • Specificity of RCN1mediated protein phosphatase 2A regulation in meristem organization and stress responses in roots
    • Blakeslee, J.J., Zhou, H.-W., Heath, J.T., Skottke, K.R., Rodriguez Barrios, J.A., Liu, S.-Y., and DeLong, A. (2008). Specificity of RCN1mediated protein phosphatase 2A regulation in meristem organization and stress responses in roots. Plant Physiol. 146: 539-553.
    • (2008) Plant Physiol , vol.146 , pp. 539-553
    • Blakeslee, J.J.1    Zhou, H.-W.2    Heath, J.T.3    Skottke, K.R.4    Rodriguez Barrios, J.A.5    Liu, S.-Y.6    Delong, A.7
  • 2
    • 0035208894 scopus 로고    scopus 로고
    • Phototropins: A new family of flavins-binding blue light receptors in plants
    • Briggs, W.R., Christie, J.M., and Salomon, M. (2001). Phototropins: A new family of flavins-binding blue light receptors in plants. Antioxid. Redox Signal. 5: 775-788.
    • (2001) Antioxid. Redox Signal , vol.5 , pp. 775-788
    • Briggs, W.R.1    Christie, J.M.2    Salomon, M.3
  • 3
    • 33846377245 scopus 로고    scopus 로고
    • Physiological roles of the light, oxygen, or voltage domains of phototropin 1 and phototropin 2 in Arabidopsis
    • Cho, H.-Y., Tseng, T.-S., Kaiserli, E., Sullivan, S., Christie, J.M., and Briggs, W.R. (2007). Physiological roles of the light, oxygen, or voltage domains of phototropin 1 and phototropin 2 in Arabidopsis. Plant Physiol. 143: 517-529.
    • (2007) Plant Physiol , vol.143 , pp. 517-529
    • Cho, H.-Y.1    Tseng, T.-S.2    Kaiserli, E.3    Sullivan, S.4    Christie, J.M.5    Briggs, W.R.6
  • 4
    • 33846118688 scopus 로고    scopus 로고
    • Crystal structure of a protein phosphatase 2A heterotrimeric holoenzyme
    • Cho, U.S., and Xu, W. (2007). Crystal structure of a protein phosphatase 2A heterotrimeric holoenzyme. Nature 445: 53-57.
    • (2007) Nature , vol.445 , pp. 53-57
    • Cho, U.S.1    Xu, W.2
  • 5
    • 34250183058 scopus 로고    scopus 로고
    • Phototropin blue-light receptors
    • Christie, J.M. (2007). Phototropin blue-light receptors. Annu. Rev. Plant Biol. 58: 21-45.
    • (2007) Annu. Rev. Plant Biol , vol.58 , pp. 21-45
    • Christie, J.M.1
  • 7
    • 0033587744 scopus 로고    scopus 로고
    • LOV (light, oxygen, or voltage) domains of the blue-light photoreceptor phototropin (nph1): Binding sites for the chromophore flavins mononucleotide
    • Christie, J.M., Salomon, M., Nozue, K., Wada, M., and Briggs, W.R. (1999). LOV (light, oxygen, or voltage) domains of the blue-light photoreceptor phototropin (nph1): Binding sites for the chromophore flavins mononucleotide. Proc. Natl. Acad. Sci. USA 96: 8779-8783.
    • (1999) Proc. Natl. Acad. Sci. Usa , vol.96 , pp. 8779-8783
    • Christie, J.M.1    Salomon, M.2    Nozue, K.3    Wada, M.4    Briggs, W.R.5
  • 8
    • 0036776294 scopus 로고    scopus 로고
    • Phototropin LOV domains exhibit distinct roles in regulating photoreceptor function
    • Christie, J.M., Swartz, T.E., Bogomolni, R., and Briggs, W.R. (2002). Phototropin LOV domains exhibit distinct roles in regulating photoreceptor function. Plant J. 32: 205-219.
    • (2002) Plant J , vol.32 , pp. 205-219
    • Christie, J.M.1    Swartz, T.E.2    Bogomolni, R.3    Briggs, W.R.4
  • 9
    • 0035853139 scopus 로고    scopus 로고
    • Structure of a flavin-binding plant photoreceptor domain: Insights into light-mediated signal transduction
    • Crosson, S., and Moffat, K. (2001). Structure of a flavin-binding plant photoreceptor domain: insights into light-mediated signal transduction. Proc. Natl. Acad. Sci. USA 98: 2995-3000.
    • (2001) Proc. Natl. Acad. Sci. Usa , vol.98 , pp. 2995-3000
    • Crosson, S.1    Moffat, K.2
  • 10
    • 0036016438 scopus 로고    scopus 로고
    • Photoexcited structure of a plant photoreceptor domain reveals a light-driven molecular switch
    • Crosson, S., and Moffat, K. (2002). Photoexcited structure of a plant photoreceptor domain reveals a light-driven molecular switch. Plant Cell 14: 1067-1075.
    • (2002) Plant Cell , vol.14 , pp. 1067-1075
    • Crosson, S.1    Moffat, K.2
  • 11
    • 33747886506 scopus 로고    scopus 로고
    • Switching the flip: Protein phosphatase roles in signaling pathways
    • DeLong, A. (2006). Switching the flip: protein phosphatase roles in signaling pathways. Curr. Opin. Plant Biol. 9: 470-477.
    • (2006) Curr. Opin. Plant Biol , vol.9 , pp. 470-477
    • Delong, A.1
  • 12
    • 0039613876 scopus 로고    scopus 로고
    • The RCN-encoded A subunit of protein phosphatase 2A increases phosphatase activity in vivo
    • Deruère, J., Jackson, K., Garbers, C., Söll, D., and DeLong, A. (1999). The RCN-encoded A subunit of protein phosphatase 2A increases phosphatase activity in vivo. Plant J. 20: 389-399.
    • (1999) Plant J , vol.20 , pp. 389-399
    • Deruère, J.1    Jackson, K.2    Garbers, C.3    Söll, D.4    Delong, A.5
  • 13
    • 0029940505 scopus 로고    scopus 로고
    • A mutation in protein phosphatase 2A regulatory subunit A affects auxin transport in Arabidopsis
    • Garbers, C., DeLong, A., Deruère, J., Bernasconi, P., and Söll, D. (1996). A mutation in protein phosphatase 2A regulatory subunit A affects auxin transport in Arabidopsis. EMBO J. 15: 2115-2124.
    • (1996) Embo J , vol.15 , pp. 2115-2124
    • Garbers, C.1    Delong, A.2    Deruère, J.3    Bernasconi, P.4    Söll, D.5
  • 14
    • 0001629613 scopus 로고
    • Redox dependence of the blue-light-induced phosphorylation of a 100-kD protein on isolated plasma membranes from tips of coleoptiles
    • Hager, A., Brich, M., and Bazlen, I. (1993). Redox dependence of the blue-light-induced phosphorylation of a 100-kD protein on isolated plasma membranes from tips of coleoptiles. Planta 190: 120-126.
    • (1993) Planta , vol.190 , pp. 120-126
    • Hager, A.1    Brich, M.2    Bazlen, I.3
  • 15
    • 57749111980 scopus 로고    scopus 로고
    • Phytochrome A regulates the intracellular distribution of phototropin 1-green fluorescent protein in Arabidopsis thaliana
    • Han, I.-S., Tseng, T.-S., Eisinger, W., and Briggs, W.R. (2008).Phytochrome A regulates the intracellular distribution of phototropin 1-green fluorescent protein in Arabidopsis thaliana. Plant Cell 20: 2835-2847.
    • (2008) Plant Cell , vol.20 , pp. 2835-2847
    • Han, I.-S.1    Tseng, T.-S.2    Eisinger, W.3    Briggs, W.R.4
  • 16
    • 11144344967 scopus 로고    scopus 로고
    • Disruption of the LOV-Ja helix interaction activates phototropin kinase activity
    • Harper, S.M., Christie, J.M., and Gardner, K.H. (2004). Disruption of the LOV-Ja helix interaction activates phototropin kinase activity. Biochemistry 43: 16184-16192.
    • (2004) Biochemistry , vol.43 , pp. 16184-16192
    • Harper, S.M.1    Christie, J.M.2    Gardner, K.H.3
  • 17
    • 0141707094 scopus 로고    scopus 로고
    • Structural basis of a phototropin light switch
    • Harper, S.M., Neil, L.C., and Gardner, K.H. (2003). Structural basis of a phototropin light switch. Science 301: 1541-1544.
    • (2003) Science , vol.301 , pp. 1541-1544
    • Harper, S.M.1    Neil, L.C.2    Gardner, K.H.3
  • 18
    • 0031470701 scopus 로고    scopus 로고
    • Arabidopsis NPH1: A proteín kinase with a putative redox-sensing domain
    • Huala, E., Oeller, O.P.W., Liscum, E., Han, I.-S., Larsen, E., and Briggs, W.R. (1997). Arabidopsis NPH1: A proteín kinase with a putative redox-sensing domain. Science 278: 2120-2123.
    • (1997) Science , vol.278 , pp. 2120-2123
    • Huala, E.1    Oeller, O.P.W.2    Liscum, E.3    Han, I.-S.4    Larsen, E.5    Briggs, W.R.6
  • 19
    • 44449177765 scopus 로고    scopus 로고
    • Leaf positioning in Arabidopsis in response to blue light
    • Inoue, S., Kinoshita, T., Takemiya, A., Doi, M., and Shimazaki, K. (2008b). Leaf positioning in Arabidopsis in response to blue light. Mol. Plant 1: 15-26.
    • (2008) Mol. Plant , vol.1 , pp. 15-26
    • Inoue, S.1    Kinoshita, T.2    Takemiya, A.3    Doi, M.4    Shimazaki, K.5
  • 21
    • 0035252894 scopus 로고    scopus 로고
    • Protein phosphatase 2A: A highly regulated family of serine/threonine phosphatases implicated in cell growth and signaling
    • Janssens, V., and Goris, J. (2001). Protein phosphatase 2A: A highly regulated family of serine/threonine phosphatases implicated in cell growth and signaling. Biochem. J. 353: 417-439.
    • (2001) Biochem. J , vol.353 , pp. 417-439
    • Janssens, V.1    Goris, J.2
  • 22
    • 39949083195 scopus 로고    scopus 로고
    • PP2A holoenzyme assembly: In cauda venenum (the sting is in the tail)
    • Janssens, V., Longin, S., and Goris, J. (2008). PP2A holoenzyme assembly: in cauda venenum (the sting is in the tail). Trends Biochem. Sci. 33: 113-121.
    • (2008) Trends Biochem. Sci , vol.33 , pp. 113-121
    • Janssens, V.1    Longin, S.2    Goris, J.3
  • 23
    • 0035896393 scopus 로고    scopus 로고
    • Arabidopsis NPL1: A phototropin homolog controlling the chloroplast high-light avoidance response
    • Kagawa, T., Sakai, T., Suetsugu, N., Oikawa, K., Ishiguro, S., Kato, T., Tabata, S., Okada, K., and Wada, M. (2001). Arabidopsis NPL1: A phototropin homolog controlling the chloroplast high-light avoidance response. Science 291: 2138-2141.
    • (2001) Science , vol.291 , pp. 2138-2141
    • Kagawa, T.1    Sakai, T.2    Suetsugu, N.3    Oikawa, K.4    Ishiguro, S.5    Kato, T.6    Tabata, S.7    Okada, K.8    Wada, M.9
  • 24
    • 0035983657 scopus 로고    scopus 로고
    • Photochemical properties of the flavin mononucleotide-binding domains of the phototropins from Arabidopsis, rice, and Chlamydomonas reinhardtii
    • Kasahara, M., et al. (2002). Photochemical properties of the flavin mononucleotide-binding domains of the phototropins from Arabidopsis, rice, and Chlamydomonas reinhardtii. Plant Physiol. 129: 762-773.
    • (2002) Plant Physiol , vol.129 , pp. 762-773
    • Kasahara, M.1
  • 25
    • 77950343322 scopus 로고    scopus 로고
    • Mechanisms of light activation in flavins-binding photoreceptors
    • E. Silva and A.M. Edwards, eds (Cambridge, UK: RSC Publishing)
    • Kennis, J.T.M., and Alexandre, M.T.A. (2006). Mechanisms of light activation in flavins-binding photoreceptors. In Flavins, Photochemistry and Photbiology, E. Silva and A.M. Edwards, eds (Cambridge, UK: RSC Publishing), pp. 287-319.
    • (2006) Flavins, Photochemistry and Photbiology , pp. 287-319
    • Kennis, J.T.M.1    Alexandre, M.T.A.2
  • 26
    • 0030671551 scopus 로고    scopus 로고
    • Protein-protein interactions among Aux/IAA proteins
    • USA
    • Kim, J., Harter, K., and Theologis, A. (1997). Protein-protein interactions among Aux/IAA proteins. Proc. Natl. Acad. Sci. USA 94: 11786-11791.
    • (1997) Proc. Natl. Acad. Sci , vol.94 , pp. 11786-11791
    • Kim, J.1    Harter, K.2    Theologis, A.3
  • 27
    • 0035818967 scopus 로고    scopus 로고
    • Phot1 and phot2 mediate blue light regulation of stomatal opening
    • Kinoshita, T., Doi, M., Suetsugu, N., Kagawa, T., Wada, M., and Shimazaki, K.-I. (2001). Phot1 and phot2 mediate blue light regulation of stomatal opening. Nature 414: 656-660.
    • (2001) Nature , vol.414 , pp. 656-660
    • Kinoshita, T.1    Doi, M.2    Suetsugu, N.3    Kagawa, T.4    Wada, M.5    Shimazaki, K.-I.6
  • 28
    • 0345791404 scopus 로고    scopus 로고
    • Blue-lightand phosphorylation-dependent binding of a 14-3-3 protein to phototropins in stomatal guard cells of broad bean
    • Kinoshita, T., Emi, T., Tominaga, M., Sakamoto, K., Shigenaga, A., Doi, M., and Shimazaki, K.-I. (2003). Blue-lightand phosphorylation-dependent binding of a 14-3-3 protein to phototropins in stomatal guard cells of broad bean. Plant Physiol. 133: 1453-1463.
    • (2003) Plant Physiol , vol.133 , pp. 1453-1463
    • Kinoshita, T.1    Emi, T.2    Tominaga, M.3    Sakamoto, K.4    Shigenaga, A.5    Doi, M.6    Shimazaki, K.-I.7
  • 29
    • 34548118780 scopus 로고    scopus 로고
    • The C-terminal kinase fragment of Arabidopsis phototropin 2 triggers constitutive phototropin responses
    • Kong, S.-G., Kinoshita, T., Shimazaki, K.-I., Mochizuki, N., Suzuki, T., and Nagatani, A. (2007). The C-terminal kinase fragment of Arabidopsis phototropin 2 triggers constitutive phototropin responses. Plant J. 51: 862-873.
    • (2007) Plant J , vol.51 , pp. 862-873
    • Kong, S.-G.1    Kinoshita, T.2    Shimazaki, K.-I.3    Mochizuki, N.4    Suzuki, T.5    Nagatani, A.6
  • 30
    • 0036846816 scopus 로고    scopus 로고
    • Disruption of a guard cellexpressed protein phosphatase 2A regulatory subunit RCN1-1, confers abscisic acid insensitivity in Arabidopsis
    • Kwak, J.M., Moon, J.-H., Murata, Y., Kuchitsu, K., Leonhardt, N., DeLong, A., and Schroeder, J. (2002). Disruption of a guard cellexpressed protein phosphatase 2A regulatory subunit RCN1-1, confers abscisic acid insensitivity in Arabidopsis. Plant Cell 14: 2849-2861.
    • (2002) Plant Cell , vol.14 , pp. 2849-2861
    • Kwak, J.M.1    Moon, J.-H.2    Murata, Y.3    Kuchitsu, K.4    Leonhardt, N.5    Delong, A.6    Schroeder, J.7
  • 31
    • 0029278701 scopus 로고
    • Mutations in the NPH1 locus of Arabidopsis disrupt the perception of phototropic stimuli
    • Liscum, E., and Briggs, W.R. (1995). Mutations in the NPH1 locus of Arabidopsis disrupt the perception of phototropic stimuli. Plant Cell 7: 473-485.
    • (1995) Plant Cell , vol.7 , pp. 473-485
    • Liscum, E.1    Briggs, W.R.2
  • 32
    • 0003981471 scopus 로고
    • Carnegie Institution of Washington Publication 314. (Washington DC: A.B. Graham Co.)
    • Loftfield, J.V.G. (1921). The behavior of stomata. Carnegie Institution of Washington Publication 314. (Washington DC: A.B. Graham Co.), pp. 7-104.
    • (1921) The Behavior of Stomata , pp. 7-104
    • Loftfield, J.V.G.1
  • 33
    • 0001571652 scopus 로고
    • Blue light response of stomata with starch-containing (Vicia faba) and starch-deficient (Allium cepa) guard cells under background illumination with red light
    • Ogawa, T. (1978). Blue light response of stomata with starch-containing (Vicia faba) and starch-deficient (Allium cepa) guard cells under background illumination with red light. Plant Sci. Lett. 22: 103-108.
    • (1978) Plant Sci. Lett , vol.22 , pp. 103-108
    • Ogawa, T.1
  • 34
    • 0002689881 scopus 로고
    • Synergistic action of red and blue light and action spectra for malate formation in guard cells of Vicia faba L
    • Ogawa, T., Ishikawa, H., Shimada, K., and Shibata, K. (1981).Synergistic action of red and blue light and action spectra for malate formation in guard cells of Vicia faba L. Planta 142: 61-65.
    • (1981) Planta , vol.142 , pp. 61-65
    • Ogawa, T.1    Ishikawa, H.2    Shimada, K.3    Shibata, K.4
  • 35
    • 0000032477 scopus 로고
    • Blue light-induced phosphorylation of a plasma membrane-associated protein in Zea mays L
    • Palmer, J.M., Short, T.W., Gallagher, S., and Briggs, W.R. (1993). Blue light-induced phosphorylation of a plasma membrane-associated protein in Zea mays L. Plant Physiol. 102: 1211-1218.
    • (1993) Plant Physiol , vol.102 , pp. 1211-1218
    • Palmer, J.M.1    Short, T.W.2    Gallagher, S.3    Briggs, W.R.4
  • 36
    • 34547135478 scopus 로고    scopus 로고
    • Regulation of phototropic signaling in Arabidopsis via phosphorylation state changes in the phototropin 1-interacting protein NPH3
    • Pedmale, U.V., and Liscum, E. (2007). Regulation of phototropic signaling in Arabidopsis via phosphorylation state changes in the phototropin 1-interacting protein NPH3. J. Biol. Chem. 282: 19992-20001.
    • (2007) J. Biol. Chem , vol.282 , pp. 19992-20001
    • Pedmale, U.V.1    Liscum, E.2
  • 37
    • 0034928225 scopus 로고    scopus 로고
    • Genetic and chemical reductions in protein phosphatase activity alter auxin transport, gravity response, and lateral root growth
    • Rashotte, A.M., DeLong, A., and Muday, G.K. (2001). Genetic and chemical reductions in protein phosphatase activity alter auxin transport, gravity response, and lateral root growth. Plant Cell 13: 1683-1697.
    • (2001) Plant Cell , vol.13 , pp. 1683-1697
    • Rashotte, A.M.1    Delong, A.2    Muday, G.K.3
  • 38
    • 51749101973 scopus 로고    scopus 로고
    • Roles of RCN1, regulatory A subunit of protein phosphatase 2A, in methyl jasmonate signaling and signal crosstalk between methyl jasmonate and abscisic acid
    • Saito, N., Munemasa, S., Nakamura, Y., Shimoishi, Y., Mori, I.C., and Murata, Y. (2008). Roles of RCN1, regulatory A subunit of protein phosphatase 2A, in methyl jasmonate signaling and signal crosstalk between methyl jasmonate and abscisic acid. Plant Cell Physiol. 49: 1396-1401.
    • (2008) Plant Cell Physiol , vol.49 , pp. 1396-1401
    • Saito, N.1    Munemasa, S.2    Nakamura, Y.3    Shimoishi, Y.4    Mori, I.C.5    Murata, Y.6
  • 40
    • 0034622586 scopus 로고    scopus 로고
    • Photochemical and mutational analysis of the FMN-binding domains of the plant blue light receptor, phototropin
    • Salomon, M., Christie, J.M., Knieb, E., Lempert, U., and Briggs, W.R. (2000). Photochemical and mutational analysis of the FMN-binding domains of the plant blue light receptor, phototropin. Biochemistry 39: 9401-9410.
    • (2000) Biochemistry , vol.39 , pp. 9401-9410
    • Salomon, M.1    Christie, J.M.2    Knieb, E.3    Lempert, U.4    Briggs, W.R.5
  • 41
    • 0037446727 scopus 로고    scopus 로고
    • Mapping of lowand high-fluence autophosphorylation sites in phototropin 1
    • Salomon, M., Knieb, E., von Zeppelin, T., and Rüdiger, W. (2003). Mapping of lowand high-fluence autophosphorylation sites in phototropin 1. Biochemistry 42: 4217-4225.
    • (2003) Biochemistry , vol.42 , pp. 4217-4225
    • Salomon, M.1    Knieb, E.2    von Zeppelin, T.3
  • 42
    • 0003341864 scopus 로고
    • Characterization of a rapid, blue light-mediated change in detectable phosphorylation of a plasma membrane protein from etiolated pea (Pisum sativum L.) seedlings
    • Short, T.W., and Briggs, W.R. (1990). Characterization of a rapid, blue light-mediated change in detectable phosphorylation of a plasma membrane protein from etiolated pea (Pisum sativum L.) seedlings. Plant Physiol. 92: 179-185.
    • (1990) Plant Physiol , vol.92 , pp. 179-185
    • Short, T.W.1    Briggs, W.R.2
  • 43
    • 0028117990 scopus 로고
    • Blue light induces phosphorylation at seryl residues in a pea (Pisum sativum L.) plasma membrane protein
    • Short, T.W., Porst, M., Palmer, J., Fernbach, E., and Briggs, W.R.(1994). Blue light induces phosphorylation at seryl residues in a pea (Pisum sativum L.) plasma membrane protein. Plant Physiol. 104: 1317-1324.
    • (1994) Plant Physiol , vol.104 , pp. 1317-1324
    • Short, T.W.1    Porst, M.2    Palmer, J.3    Fernbach, E.4    Briggs, W.R.5
  • 44
    • 34547873925 scopus 로고    scopus 로고
    • Chloroplast photorelocation movement mediated by phototropin family proteins in green plants
    • Suetsugu, N., and Wada, M. (2007). Chloroplast photorelocation movement mediated by phototropin family proteins in green plants. Biol. Chem. 388: 927-935.
    • (2007) Biol. Chem , vol.388 , pp. 927-935
    • Suetsugu, N.1    Wada, M.2
  • 45
    • 47849128479 scopus 로고    scopus 로고
    • In vivo phosphorylation site mapping and functional characterization of Arabidopsis phototropin 1
    • Sullivan, S., Thomson, C.E., Lamont, D.J., Jones, M.A., and Christie, J.M. (2008). In vivo phosphorylation site mapping and functional characterization of Arabidopsis phototropin 1. Mol. Plant 1: 178-194.
    • (2008) Mol. Plant , vol.1 , pp. 178-194
    • Sullivan, S.1    Thomson, C.E.2    Lamont, D.J.3    Jones, M.A.4    Christie, J.M.5
  • 46
    • 0035979317 scopus 로고    scopus 로고
    • Multiple transcription-factor genes are early targets of phytochrome A signaling
    • Tepperman, J.M., Zhu, T., Chang, H.S., Wang, X., and Quail, P.H. (2001). Multiple transcription-factor genes are early targets of phytochrome A signaling. Proc. Natl. Acad. Sci. USA 98: 9437-9442.
    • (2001) Proc. Natl. Acad. Sci. Usa , vol.98 , pp. 9437-9442
    • Tepperman, J.M.1    Zhu, T.2    Chang, H.S.3    Wang, X.4    Quail, P.H.5
  • 47
    • 2942692256 scopus 로고    scopus 로고
    • SPINDLY and GIGANTEA interact and act in Arabidopsis pathways involved in light responses, flowering, and rhythms in cotyledon movements
    • Tseng, T.-S., Salome, P.A., McClung, C.R., and Olszewski, N.E. (2004). SPINDLY and GIGANTEA interact and act in Arabidopsis pathways involved in light responses, flowering, and rhythms in cotyledon movements. Plant Cell 16: 1550-1563.
    • (2004) Plant Cell , vol.16 , pp. 1550-1563
    • Tseng, T.-S.1    Salome, P.A.2    McClung, C.R.3    Olszewski, N.E.4
  • 48
    • 0034948273 scopus 로고    scopus 로고
    • Ectopic expression of the tetratricopeptide repeat domain of SPINDLY causes defects in gibberellin response
    • Tseng, T.-S., Swain, S.M., and Olszewski, N.E. (2001). Ectopic expression of the tetratricopeptide repeat domain of SPINDLY causes defects in gibberellin response. Plant Physiol. 126: 1250-1258.
    • (2001) Plant Physiol , vol.126 , pp. 1250-1258
    • Tseng, T.-S.1    Swain, S.M.2    Olszewski, N.E.3
  • 50
    • 0037887123 scopus 로고
    • Photocontrol of the functional coupling between photosynthesis and stomatal conductance in the intact leaf
    • Zeiger, E., and Field, C. (1982). Photocontrol of the functional coupling between photosynthesis and stomatal conductance in the intact leaf. Plant Physiol. 70: 370-375.
    • (1982) Plant Physiol , vol.70 , pp. 370-375
    • Zeiger, E.1    Field, C.2
  • 51
    • 1542752539 scopus 로고    scopus 로고
    • Disparate roles for the regulatory subunit isoforms in Arabidopsis protein phosphatase 2A
    • Zhou, H.-W., Nussbaumer, C., Chao, Y., and DeLong, A. (2004). Disparate roles for the regulatory subunit isoforms in Arabidopsis protein phosphatase 2A. Plant Cell 16: 709-722.
    • (2004) Plant Cell , vol.16 , pp. 709-722
    • Zhou, H.-W.1    Nussbaumer, C.2    Chao, Y.3    Delong, A.4


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