메뉴 건너뛰기




Volumn 105, Issue 14, 2008, Pages 5626-5631

Blue light-induced autophosphorylation of phototropin is a primary step for signaling

Author keywords

Light signaling; Photoreceptor; Protein kinase; Stomata

Indexed keywords

ALANINE; PHOSPHOPROTEIN; PHOTOTROPIN; PROTEIN KINASE; SERINE; THREONINE;

EID: 44449166482     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0709189105     Document Type: Article
Times cited : (217)

References (37)
  • 1
    • 0036583102 scopus 로고    scopus 로고
    • Phototropins 1 and 2: Versatile plant blue-light receptors
    • Briggs WR, Christie JM (2002) Phototropins 1 and 2: versatile plant blue-light receptors. Trends Plant Sci 7:204-210.
    • (2002) Trends Plant Sci , vol.7 , pp. 204-210
    • Briggs, W.R.1    Christie, J.M.2
  • 2
    • 0035810965 scopus 로고    scopus 로고
    • Arabidopsis nph1 and npl1: Blue light receptors that mediate both phototropism and chloroplast relocation
    • Sakai T, et al. (2001) Arabidopsis nph1 and npl1: Blue light receptors that mediate both phototropism and chloroplast relocation. Proc Natl Acad Sci USA 98:6969-6974.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 6969-6974
    • Sakai, T.1
  • 3
    • 0036671887 scopus 로고    scopus 로고
    • Cellular and subcellular localization of phototropin 1
    • Sakamoto K, Briggs WR (2002) Cellular and subcellular localization of phototropin 1. Plant Cell 14:1723-1735.
    • (2002) Plant Cell , vol.14 , pp. 1723-1735
    • Sakamoto, K.1    Briggs, W.R.2
  • 4
    • 34250183058 scopus 로고    scopus 로고
    • Phototropin blue-light receptors
    • Christie zJM (2007) Phototropin blue-light receptors. Annu Rev Plant Biol 58:21-45.
    • (2007) Annu Rev Plant Biol , vol.58 , pp. 21-45
    • Christie zJM1
  • 6
    • 23944471774 scopus 로고    scopus 로고
    • Phototropins promote plant growth in response to blue light in low light environments
    • Takemiya A, Inoue S, Doi M, Kinoshita T, Shimazaki K (2005) Phototropins promote plant growth in response to blue light in low light environments. Plant Cell 17:1120-1127.
    • (2005) Plant Cell , vol.17 , pp. 1120-1127
    • Takemiya, A.1    Inoue, S.2    Doi, M.3    Kinoshita, T.4    Shimazaki, K.5
  • 7
    • 0037180725 scopus 로고    scopus 로고
    • Chloroplast avoidance movement reduces photodamage in plants
    • Kasahara M, et al. (2002) Chloroplast avoidance movement reduces photodamage in plants. Nature 420:829-832.
    • (2002) Nature , vol.420 , pp. 829-832
    • Kasahara, M.1
  • 8
    • 0031470701 scopus 로고    scopus 로고
    • Arabidopsis NPH1: A protein kinase with a putative redox-sensing domain
    • Huala E, et al. (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
  • 9
    • 0032573502 scopus 로고    scopus 로고
    • Arabidopsis NPH1: A flavoprotein with the properties of a photoreceptor for phototropism
    • Christie JM, et al. (1998) Arabidopsis NPH1: A flavoprotein with the properties of a photoreceptor for phototropism. Science 282:1698-1701.
    • (1998) Science , vol.282 , pp. 1698-1701
    • Christie, J.M.1
  • 10
    • 0033587744 scopus 로고    scopus 로고
    • LOV (light, oxygen, voltage) domains of the blue-light photoreceptor phototropin (nph1): Binding sites for the chromophore flavin mononucleotide
    • Christie JM, Salomon M, Nozue K, Wada M, Briggs WR (1999) LOV (light, oxygen, voltage) domains of the blue-light photoreceptor phototropin (nph1): Binding sites for the chromophore flavin 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
  • 11
    • 0034622586 scopus 로고    scopus 로고
    • Photochemical and mutational analysis of the FMN binding domains of the plant blue light receptor, phototropin
    • Salomon M, Christie JM, Knieb E, Lempert U, Briggs WR (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
  • 12
    • 0035940398 scopus 로고    scopus 로고
    • An optomechanical transducer in the blue light receptor phototropin from Avena sativa
    • Salomon M, et al. (2001) An optomechanical transducer in the blue light receptor phototropin from Avena sativa. Proc Natl Acad Sci USA 98:12357-12361.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 12357-12361
    • Salomon, M.1
  • 13
    • 0035965307 scopus 로고    scopus 로고
    • The photocycle of a flavin-binding domain of the blue light photoreceptor phototropin
    • Swartz TE, et al. (2001) The photocycle of a flavin-binding domain of the blue light photoreceptor phototropin. J Biol Chem 276:36493-36500.
    • (2001) J Biol Chem , vol.276 , pp. 36493-36500
    • Swartz, T.E.1
  • 14
    • 0037062577 scopus 로고    scopus 로고
    • Vibration spectroscopy reveals light-induced chromophore and protein structural changes in the LOV2 domain of the plant blue-light receptor phototropin 1
    • Swartz TE, Wenzel PJ, Corchnoy SB, Briggs WR, Bogomolni RA (2002) Vibration spectroscopy reveals light-induced chromophore and protein structural changes in the LOV2 domain of the plant blue-light receptor phototropin 1. Biochemistry 41:7183-7189.
    • (2002) Biochemistry , vol.41 , pp. 7183-7189
    • Swartz, T.E.1    Wenzel, P.J.2    Corchnoy, S.B.3    Briggs, W.R.4    Bogomolni, R.A.5
  • 15
    • 3142617400 scopus 로고    scopus 로고
    • Role of Gln1029 in the photoactivation processes of the LOV2 domain in Adiantum phytochrome3
    • Nozaki D, et al. (2004) Role of Gln1029 in the photoactivation processes of the LOV2 domain in Adiantum phytochrome3. Biochemistry 43:8373-8379.
    • (2004) Biochemistry , vol.43 , pp. 8373-8379
    • Nozaki, D.1
  • 16
    • 11144344967 scopus 로고    scopus 로고
    • Disruption of the LOV-Jα helix interaction activates phototropin kinase activity
    • Harper SM, Christie JM, Gardner KH (2004) Disruption of the LOV-Jα 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
    • 0036776294 scopus 로고    scopus 로고
    • Phototropin LOV domains exhibit distinct roles in regulating photoreceptor function
    • Christie JM, Swartz TE, Bogomolni RA, Briggs WR (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.A.3    Briggs, W.R.4
  • 18
    • 24944553332 scopus 로고    scopus 로고
    • Blue light-regulated molecular switch of Ser/Thr kinase in phototropin
    • Matsuoka D, Tokutomi S (2005) Blue light-regulated molecular switch of Ser/Thr kinase in phototropin. Proc Natl Acad Sci USA 102:13337-13342.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 13337-13342
    • Matsuoka, D.1    Tokutomi, S.2
  • 19
    • 0000258296 scopus 로고
    • Light-mediated changes in two proteins found associated with the plasma membrane fractions from pea stem sections
    • Gallagher S, Short TW, Ray PM, Pratt LH, Briggs WR (1988) Light-mediated changes in two proteins found associated with the plasma membrane fractions from pea stem sections. Proc Natl Acad Sci USA 85:8003-8007.
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 8003-8007
    • Gallagher, S.1    Short, T.W.2    Ray, P.M.3    Pratt, L.H.4    Briggs, W.R.5
  • 20
    • 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 TW, Briggs WR (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
  • 21
    • 0026522616 scopus 로고
    • Light-induced phosphorylation of a membrane protein plays an early role in signal transduction for phototropism in Arabidopsis thaliana
    • Reymond P, Short TW, Briggs WR, Poff KL (1992) Light-induced phosphorylation of a membrane protein plays an early role in signal transduction for phototropism in Arabidopsis thaliana. Proc Natl Acad Sci USA 89:4718-4721.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 4718-4721
    • Reymond, P.1    Short, T.W.2    Briggs, W.R.3    Poff, K.L.4
  • 22
    • 0000032478 scopus 로고
    • Correlation of blue light-induced phosphorylation to phototropism in Zea mays L
    • Palmer JM, Short TW, Briggs WR (1993) Correlation of blue light-induced phosphorylation to phototropism in Zea mays L. Plant Physiol 102:1219-1225.
    • (1993) Plant Physiol , vol.102 , pp. 1219-1225
    • Palmer, J.M.1    Short, T.W.2    Briggs, W.R.3
  • 23
    • 0031401162 scopus 로고    scopus 로고
    • Asymmetric, blue light-dependent phosphorylation of a 116-kilodalton plasma membrane protein can be correlated with the first- and second-positive phototropic curvature of oat coleoptiles
    • Salomon M, Zacherl M, Rüdiger W (1997) Asymmetric, blue light-dependent phosphorylation of a 116-kilodalton plasma membrane protein can be correlated with the first- and second-positive phototropic curvature of oat coleoptiles. Plant Physiol 115:485-491
    • (1997) Plant Physiol , vol.115 , pp. 485-491
    • Salomon, M.1    Zacherl, M.2    Rüdiger, W.3
  • 24
    • 0037446727 scopus 로고    scopus 로고
    • Mapping of low- and high-fluence autophosphorylation sites in phototropin 1
    • Salomon M, Knieb E, von Zeppelin T, Rüdiger W (2003) Mapping of low- and 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    Rüdiger, W.4
  • 25
    • 0345791404 scopus 로고    scopus 로고
    • Blue-light- and phosphorylation- dependent binding of a 14-3-3 protein to phototropins in stomatal guard cell of broad bean
    • Kinoshita T, et al. (2003) Blue-light- and phosphorylation- dependent binding of a 14-3-3 protein to phototropins in stomatal guard cell of broad bean. Plant Physiol 133:1453-1463.
    • (2003) Plant Physiol , vol.133 , pp. 1453-1463
    • Kinoshita, T.1
  • 26
    • 0034949516 scopus 로고    scopus 로고
    • Molecular characterization of functional domains in the protein kinase SOS2 that Is required for plant salt tolerance
    • Guo Y, Halfter U, Ishitani M, Zhu J-K (2001) Molecular characterization of functional domains in the protein kinase SOS2 that Is required for plant salt tolerance. Plant Cell 13:1383-1399.
    • (2001) Plant Cell , vol.13 , pp. 1383-1399
    • Guo, Y.1    Halfter, U.2    Ishitani, M.3    Zhu, J.-K.4
  • 27
    • 0000232677 scopus 로고
    • Blue light activates electrogenic ion pumping in guard cell protoplasts of Vicia faba L
    • Assmann SM, Simoncini L, Schroeder JI (1985) Blue light activates electrogenic ion pumping in guard cell protoplasts of Vicia faba L. Nature 318:285-287.
    • (1985) Nature , vol.318 , pp. 285-287
    • Assmann, S.M.1    Simoncini, L.2    Schroeder, J.I.3
  • 28
    • 33947283972 scopus 로고
    • Blue light-dependent proton extrusion by guard cell protoplasts of Vicia faba
    • Shimazaki K, Iino M, Zeiger E (1986) Blue light-dependent proton extrusion by guard cell protoplasts of Vicia faba. Nature 319:324-326.
    • (1986) Nature , vol.319 , pp. 324-326
    • Shimazaki, K.1    Iino, M.2    Zeiger, E.3
  • 29
    • 0033570171 scopus 로고    scopus 로고
    • +-ATPase by phosphorylation of the C-terminus in stomatal guard cells
    • +-ATPase by phosphorylation of the C-terminus in stomatal guard cells. EMBO J 18:5548-5558.
    • (1999) EMBO J , vol.18 , pp. 5548-5558
    • Kinoshita, T.1    Shimazaki, K.2
  • 30
    • 0035818967 scopus 로고    scopus 로고
    • phot1 and phot2 mediate blue light regulation of stomatal opening
    • Kinoshita T, et al. (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
  • 31
    • 33947655903 scopus 로고    scopus 로고
    • Blue light inhibits guard cell plasma membrane anion channels in a phototropin-dependent manner
    • Marten H, Hedrich R, Roelfsema MRG (2007) Blue light inhibits guard cell plasma membrane anion channels in a phototropin-dependent manner. Plant J 50:29-39.
    • (2007) Plant J , vol.50 , pp. 29-39
    • Marten, H.1    Hedrich, R.2    Roelfsema, M.R.G.3
  • 34
    • 0029020282 scopus 로고
    • Protein kinases 6. The eukaryotic protein kinase superfamily: Kinase (catalytic) domain structure and classification
    • Hanks SK, Hunter T (1995) Protein kinases 6. The eukaryotic protein kinase superfamily: kinase (catalytic) domain structure and classification. FASEB J 9:576-596.
    • (1995) FASEB J , vol.9 , pp. 576-596
    • Hanks, S.K.1    Hunter, T.2
  • 35
    • 0037013143 scopus 로고    scopus 로고
    • The conformational plasticity of protein kinases
    • Huse M, Kuriyan J (2002) The conformational plasticity of protein kinases. Cell 109:275-282.
    • (2002) Cell , vol.109 , pp. 275-282
    • Huse, M.1    Kuriyan, J.2
  • 36
    • 0037469146 scopus 로고    scopus 로고
    • Activation loop phosphorylation and catalysis in protein kinases: Is there functional evidence for the autoinhibitor model?
    • Adams JA (2003) Activation loop phosphorylation and catalysis in protein kinases: Is there functional evidence for the autoinhibitor model? Biochemistry 38:601-607.
    • (2003) Biochemistry , vol.38 , pp. 601-607
    • Adams, J.A.1
  • 37
    • 34548118780 scopus 로고    scopus 로고
    • The C-terminal kinase fragment of Arabidopsis phototropin 2 triggers constitutive phototropin responses
    • Kong S-G, et al. (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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.