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Volumn 83, Issue 1, 2007, Pages 122-130

Primary processes during the light-signal transduction of phototropin

Author keywords

[No Author keywords available]

Indexed keywords

CYSTEINE; FLAVINE MONONUCLEOTIDE; OXYGEN; PHYTOCHROME; PROTEIN SERINE THREONINE KINASE; RIBOFLAVIN DERIVATIVE;

EID: 34247899116     PISSN: 00318655     EISSN: None     Source Type: Journal    
DOI: 10.1562/2006-03-29-RA-861     Document Type: Conference Paper
Times cited : (27)

References (70)
  • 1
    • 0036531885 scopus 로고    scopus 로고
    • Photosensory perception and signaling in plants: New paradigms?
    • Quail, P. H. (2002) Photosensory perception and signaling in plants: New paradigms? Curr. Opin. Cell Biol. 14, 180 188.
    • (2002) Curr. Opin. Cell Biol. , vol.14 , pp. 180-188
    • Quail, P.H.1
  • 2
    • 0141480569 scopus 로고    scopus 로고
    • Cryptochrome structure and signal transduction
    • Lin, C. D. Shalitin (2003) Cryptochrome structure and signal transduction. Annu. Rev. Plant Biol. 54, 469 496.
    • (2003) Annu. Rev. Plant Biol. , vol.54 , pp. 469-496
    • Lin, C.1    Shalitin, D.2
  • 3
    • 0036583102 scopus 로고    scopus 로고
    • Phototropins 1 and 2: Versatile plant blue-light receptors
    • Briggs, W. R. J. M. Christie (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
  • 4
    • 0037435618 scopus 로고    scopus 로고
    • The LOV domain family: Photoresponsive signaling modules coupled to diverse output domains
    • Crosson, S., S. Rajagopal K. Moffat (2003) The LOV domain family: Photoresponsive signaling modules coupled to diverse output domains. Biochemistry 42, 2 10.
    • (2003) Biochemistry , vol.42 , pp. 2-10
    • Crosson, S.1    Rajagopal, S.2    Moffat, K.3
  • 5
    • 14744276473 scopus 로고    scopus 로고
    • Phototropins and associated signaling: Providing the power of movement in higher plants
    • Celaya, R. B. E. Liscum (2005) Phototropins and associated signaling: Providing the power of movement in higher plants. Photochem. Photobiol. 81, 73 80.
    • (2005) Photochem. Photobiol. , vol.81 , pp. 73-80
    • Celaya, R.B.1    Liscum, E.2
  • 6
    • 0344443180 scopus 로고    scopus 로고
    • FKF1 is essential for photoperiodic-specific light signalling in Arabidopsis
    • Imaizumi, T., H. G. Tran, T. E. Swartz, W. R. Briggs S. A. Kay (2003) FKF1 is essential for photoperiodic-specific light signalling in Arabidopsis. Nature 426, 302 306.
    • (2003) Nature , vol.426 , pp. 302-306
    • Imaizumi, T.1    Tran, H.G.2    Swartz, T.E.3    Briggs, W.R.4    Kay, S.A.5
  • 7
    • 0348134861 scopus 로고    scopus 로고
    • Targeted degradation of TOC1 by ZTL modulates circadian function in Arabidopsis thaliana
    • Mas, P., W. Y. Kim, D. E. Somers S. A. Kay (2003) Targeted degradation of TOC1 by ZTL modulates circadian function in Arabidopsis thaliana. Nature 426, 567 570.
    • (2003) Nature , vol.426 , pp. 567-570
    • Mas, P.1    Kim, W.Y.2    Somers, D.E.3    Kay, S.A.4
  • 8
    • 24044478137 scopus 로고    scopus 로고
    • Identification of LOV KELCH PROTEIN2 (LKP2)-interacting factors that can recruit LKP2 to nuclear bodies
    • Fukamatsu, Y., S. Mitsui, M. Yasuhara, Y. Tokioka, N. Ihara, S. Fujita T. Kiyosue (2005) Identification of LOV KELCH PROTEIN2 (LKP2)-interacting factors that can recruit LKP2 to nuclear bodies. Plant Cell Physiol. 46, 1340 1349.
    • (2005) Plant Cell Physiol. , vol.46 , pp. 1340-1349
    • Fukamatsu, Y.1    Mitsui, S.2    Yasuhara, M.3    Tokioka, Y.4    Ihara, N.5    Fujita, S.6    Kiyosue, T.7
  • 9
    • 0029278701 scopus 로고
    • Mutations in the NPH1 locus of Arabidopsis disrupt the perception of phototropic stimuli
    • Liscum, E. W. R. Briggs (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
  • 13
  • 14
    • 0035912211 scopus 로고    scopus 로고
    • Phototropin-related NPL1 controls chloroplast relocalization induced by blue light
    • Jarillo, J. A., H. Gabrys, J. Capel, J. M. Alonso, J. R. Ecker A. R. Cashmore (2001) Phototropin-related NPL1 controls chloroplast relocalization induced by blue light. Nature 410, 952 954.
    • (2001) Nature , vol.410 , pp. 952-954
    • Jarillo, J.A.1    Gabrys, H.2    Capel, J.3    Alonso, J.M.4    Ecker, J.R.5    Cashmore, A.R.6
  • 15
    • 0035818967 scopus 로고    scopus 로고
    • Phot1 and phot2 mediate blue light regulation of stomatal opening
    • Kinoshita, T., M. Doi, N. Suetsugu, T. Kagawa, M. Wada K. Shimazaki (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.6
  • 16
    • 0036671887 scopus 로고    scopus 로고
    • Cellular and subcellular localization of phototropin1
    • Sakamoto, K. W. R. Briggs (2002) Cellular and subcellular localization of phototropin1. Plant Cell 14, 1723 1735.
    • (2002) Plant Cell , vol.14 , pp. 1723-1735
    • Sakamoto, K.1    Briggs, W.R.2
  • 17
    • 0345802384 scopus 로고    scopus 로고
    • Light signaling
    • Spalding, P. E. (2003) Light signaling. Plant Physiol. 133, 1417 1419.
    • (2003) Plant Physiol. , vol.133 , pp. 1417-1419
    • Spalding, P.E.1
  • 18
    • 0033587744 scopus 로고    scopus 로고
    • LOV (light, oxygen, or voltage) domains of the blue-light photoreceptor phototropin (nph1): Binding sites for the chromophore flavin mononucleotide
    • Christie, J. M., M. Salomon, K. Nozue, M. Wada W. R. Briggs (1999) LOV (light, oxygen, or 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
  • 19
    • 0038623933 scopus 로고    scopus 로고
    • Functional conservation of light, oxygen, or voltage domains in light sensing
    • Cheng, P., Q. He, Y. Yang, L. Wang Y. Liu (2003) Functional conservation of light, oxygen, or voltage domains in light sensing. Proc. Natl Acad. Sci. USA 100, 5938 5943.
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 5938-5943
    • Cheng, P.1    He, Q.2    Yang, Y.3    Wang, L.4    Liu, Y.5
  • 20
    • 0032990441 scopus 로고    scopus 로고
    • PAS domains: Internal sensors of oxygen, redox potential and light
    • Taylor, B. L. I. B. Zhilin (1999) PAS domains: Internal sensors of oxygen, redox potential and light. Microbiol. Mol. Biol. Rev. 63, 479 506.
    • (1999) Microbiol. Mol. Biol. Rev. , vol.63 , pp. 479-506
    • Taylor, B.L.1    Zhilin, I.B.2
  • 22
    • 26444576503 scopus 로고    scopus 로고
    • A chimeric photoreceptor gene, NEOCHROME, has arisen twice during plant evolution
    • Suetsugu, N., F. Mittmann, G. Wagner, J. Hughes M. Wada (2005) A chimeric photoreceptor gene, NEOCHROME, has arisen twice during plant evolution. Proc. Natl Acad. Sci. USA 102, 13705 13709.
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 13705-13709
    • Suetsugu, N.1    Mittmann, F.2    Wagner, G.3    Hughes, J.4    Wada, M.5
  • 24
    • 23944471774 scopus 로고    scopus 로고
    • Phototropins promote plant growth in response to blue light in low light environments
    • Takemiya, A., S. Inoue, M. Doi, T. Kinoshita K. Shimazakia (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    Shimazakia, K.5
  • 26
    • 0037428497 scopus 로고    scopus 로고
    • Intramolecular proton transfers and structural changes during the photocycle of the LOV2 domain of phototropin 1
    • Corchnoy, S. B., T. E. Swartz, J. W. Lewis, I. Szundi, W. Briggs R. A. Bogomolni (2003) Intramolecular proton transfers and structural changes during the photocycle of the LOV2 domain of phototropin 1. J. Biol. Chem. 278, 724 731.
    • (2003) J. Biol. Chem. , vol.278 , pp. 724-731
    • Corchnoy, S.B.1    Swartz, T.E.2    Lewis, J.W.3    Szundi, I.4    Briggs, W.5    Bogomolni, R.A.6
  • 30
    • 0037048688 scopus 로고    scopus 로고
    • Photoreaction of the cysteine S-H group in the LOV2 domain of Adiantum phytochrome3
    • Iwata, T., S. Tokutomi H. Kandori (2002) Photoreaction of the cysteine S-H group in the LOV2 domain of Adiantum phytochrome3. J. Am. Chem. Soc. 124, 11840 11841.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 11840-11841
    • Iwata, T.1    Tokutomi, S.2    Kandori, H.3
  • 31
    • 0037489440 scopus 로고    scopus 로고
    • Light-induced structural changes in the LOV2 domain of Adiantum phytochrome3 studied by low-temperature FTIR and UV-visible spectroscopy
    • Iwata, T., D. Nozaki, S. Tokutomi, T. Kagawa, M. Wada H. Kandori (2003) Light-induced structural changes in the LOV2 domain of Adiantum phytochrome3 studied by low-temperature FTIR and UV-visible spectroscopy. Biochemistry 42, 8183 8191.
    • (2003) Biochemistry , vol.42 , pp. 8183-8191
    • Iwata, T.1    Nozaki, D.2    Tokutomi, S.3    Kagawa, T.4    Wada, M.5    Kandori, H.6
  • 32
    • 13644257678 scopus 로고    scopus 로고
    • Reactive cysteine is protonated in the triplet excited state of the LOV2 domain in Adiantum phytochrome3
    • Sato, Y., T. Iwata, S. Tokutomi H. Kandori (2005) Reactive cysteine is protonated in the triplet excited state of the LOV2 domain in Adiantum phytochrome3. J. Am. Chem. Soc. 127, 1088 1089.
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 1088-1089
    • Sato, Y.1    Iwata, T.2    Tokutomi, S.3    Kandori, H.4
  • 34
    • 0034622586 scopus 로고    scopus 로고
    • Photochemical and mutational analysis of the FMN-binding domains of the plant blue light receptor, phototropin
    • Salomon, M., J. M. Christie, E. Knieb, U. Lempert W. R. Briggs (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
  • 36
    • 0034646178 scopus 로고    scopus 로고
    • Probing the photoreaction mechanism of phytochrome through analysis of resonance Raman vibrational spectra of recombinant analogues
    • Andel Jr., F., J. T. Murphy, J. A. Haas, M. T. McDowell, I. Van Der Hoef, J. Lugtenburg, J. C. Lagarias R. A. Mathies (2000) Probing the photoreaction mechanism of phytochrome through analysis of resonance Raman vibrational spectra of recombinant analogues. Biochemistry 39, 2667 2676.
    • (2000) Biochemistry , vol.39 , pp. 2667-2676
    • Andeljr, F.1    Murphy, J.T.2    Haas, J.A.3    McDowell, M.T.4    Van Der Hoef, I.5    Lugtenburg, J.6    Lagarias, J.C.7    Mathies, R.A.8
  • 37
    • 0029743968 scopus 로고    scopus 로고
    • Photobiology of microorganisms: How photosensors catch a photon to initialize signaling
    • Hellingwerf, K. J., W. D. Hoff W. Crielaard (1996) Photobiology of microorganisms: How photosensors catch a photon to initialize signaling. Mol. Microbiol. 21, 683 693.
    • (1996) Mol. Microbiol. , vol.21 , pp. 683-693
    • Hellingwerf, K.J.1    Hoff, W.D.2    Crielaard, W.3
  • 38
    • 0035853139 scopus 로고    scopus 로고
    • Structure of a flavin-binding plant photoreceptor domain: Insights into light-mediated signal transduction
    • Crosson, S. K. Moffat (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
  • 39
    • 0036016438 scopus 로고    scopus 로고
    • Photoexcited structure of a plant photoreceptor domain reveals a light-driven molecular switch
    • Crosson, S. K. Moffat (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
  • 40
    • 0037380836 scopus 로고    scopus 로고
    • Crystal structures and molecular mechanism of a light-induced signaling switch: The Phot-LOV1 domain from Chlamydomonas reinhardtii
    • Fedorov, R., I. Schlichting, E. Hartmann, T. Domratcheva, M. Fuhrmann P. Hegemann (2003) Crystal structures and molecular mechanism of a light-induced signaling switch: The Phot-LOV1 domain from Chlamydomonas reinhardtii. Biophys. J. 84, 2474 2482.
    • (2003) Biophys. J. , vol.84 , pp. 2474-2482
    • Fedorov, R.1    Schlichting, I.2    Hartmann, E.3    Domratcheva, T.4    Fuhrmann, M.5    Hegemann, P.6
  • 41
    • 0016147048 scopus 로고
    • Sulphydryl groups as a new molecular probe at the a1b1 interface in haemoglobin using Fourier transform infrared spectroscopy
    • Alben, J. O., G. H. Bare P. A. Bromberg (1974) Sulphydryl groups as a new molecular probe at the a1b1 interface in haemoglobin using Fourier transform infrared spectroscopy. Nature 252, 736 737.
    • (1974) Nature , vol.252 , pp. 736-737
    • Alben, J.O.1    Bare, G.H.2    Bromberg, P.A.3
  • 42
    • 0025970163 scopus 로고
    • Cysteine conformation and sulfhydryl interactions in proteins and viruses. 1. Correlation of the Raman S-H band with hydrogen bonding and intramolecular geometry in model compounds
    • Li, H. G. J. Thomas Jr. (1991) Cysteine conformation and sulfhydryl interactions in proteins and viruses. 1. Correlation of the Raman S-H band with hydrogen bonding and intramolecular geometry in model compounds. J. Am. Chem. Soc. 113, 456 462.
    • (1991) J. Am. Chem. Soc. , vol.113 , pp. 456-462
    • Li, H.1    Thomas Jr., G.J.2
  • 43
    • 18844391283 scopus 로고    scopus 로고
    • Comparative investigation of the LOV1 and LOV2 domains in Adiantum phytochrome3
    • Iwata, T., D. Nozaki, S. Tokutomi H. Kandori (2005) Comparative investigation of the LOV1 and LOV2 domains in Adiantum phytochrome3. Biochemistry 44, 7427 7434.
    • (2005) Biochemistry , vol.44 , pp. 7427-7434
    • Iwata, T.1    Nozaki, D.2    Tokutomi, S.3    Kandori, H.4
  • 44
    • 12244256754 scopus 로고    scopus 로고
    • Vibrational spectroscopy of an algal phot-LOV1 domain probes the molecular changes associated with blue-light reception
    • Ataka, K., P. Hegemann J. Heberle (2003) Vibrational spectroscopy of an algal phot-LOV1 domain probes the molecular changes associated with blue-light reception. Biophys. J. 84, 466 474.
    • (2003) Biophys. J. , vol.84 , pp. 466-474
    • Ataka, K.1    Hegemann, P.2    Heberle, J.3
  • 45
    • 3242759944 scopus 로고    scopus 로고
    • Functional variations among LOV domains as revealed by FT-IR difference spectroscopy
    • Bednarz, T., A. Losi, W. Gartner, P. Hegemann J. Heberle (2004) Functional variations among LOV domains as revealed by FT-IR difference spectroscopy. Photochem. Photobiol. Sci. 3, 575 579.
    • (2004) Photochem. Photobiol. Sci. , vol.3 , pp. 575-579
    • Bednarz, T.1    Losi, A.2    Gartner, W.3    Hegemann, P.4    Heberle, J.5
  • 46
    • 9744263917 scopus 로고    scopus 로고
    • Light-induced structural changes of LOV domain-containing polypeptides from Arabidopsis phototropin 1 and 2 studied by small-angle X-ray scattering
    • Nakasako, M., T. Iwata, D. Matsuoka S. Tokutomi (2004) Light-induced structural changes of LOV domain-containing polypeptides from Arabidopsis phototropin 1 and 2 studied by small-angle X-ray scattering. Biochemistry 43, 14881 14890.
    • (2004) Biochemistry , vol.43 , pp. 14881-14890
    • Nakasako, M.1    Iwata, T.2    Matsuoka, D.3    Tokutomi, S.4
  • 47
    • 4143081643 scopus 로고    scopus 로고
    • Dimerization of the plant photoreceptor phototropin is probably mediated by the LOV1 domain
    • Salomon, M., U. Lempert W. Rüdiger (2004) Dimerization of the plant photoreceptor phototropin is probably mediated by the LOV1 domain. FEBS Lett. 572, 8 10.
    • (2004) FEBS Lett. , vol.572 , pp. 8-10
    • Salomon, M.1    Lempert, U.2    Rüdiger, W.3
  • 49
    • 5444222175 scopus 로고    scopus 로고
    • Molecular dynamics simulation of the LOV2 domain from Adiantum capillus-veneris
    • Neiß, C. P. Saalfrank (2004) Molecular dynamics simulation of the LOV2 domain from Adiantum capillus-veneris. J. Chem. Inf. Comput. Sci. 44, 1788 1799.
    • (2004) J. Chem. Inf. Comput. Sci. , vol.44 , pp. 1788-1799
    • Neiß, C.1    Saalfrank, P.2
  • 50
    • 3142617400 scopus 로고    scopus 로고
    • Role of Gln1029 in the photoactivation processes of the LOV2 domain in Adiantum phytochrome3
    • Nozaki, D., T. Iwata, T. Ishikawa, T. Todo, S. Tokutomi H. Kandori (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    Iwata, T.2    Ishikawa, T.3    Todo, T.4    Tokutomi, S.5    Kandori, H.6
  • 51
    • 0141707094 scopus 로고    scopus 로고
    • Structural basis of a phototropin light switch
    • Harper, S. M., L. C. Neil K. H. Gardner (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
  • 52
    • 11144344967 scopus 로고    scopus 로고
    • Disruption of the LOV-Jα helix interaction activates phototropin kinase activity
    • Harper, S. M., J. M. Christie K. H. Gardner (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
  • 53
    • 25444492902 scopus 로고    scopus 로고
    • Conformational dynamics of phototropin 2 LOV2 domain with the linker upon photoexcitation
    • Eitoku, T., Y. Nakasone, D. Matsuoka, S. Tokutomi M. Terazima (2005) Conformational dynamics of phototropin 2 LOV2 domain with the linker upon photoexcitation. J. Am. Chem. Soc., 127, 13238 13244.
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 13238-13244
    • Eitoku, T.1    Nakasone, Y.2    Matsuoka, D.3    Tokutomi, S.4    Terazima, M.5
  • 55
    • 1142274297 scopus 로고    scopus 로고
    • Recording of blue light-induced energy and volume changes within the wild-type and mutated phot-LOV1 domain from Chlamydomonas reinhardtii
    • Losi, A., T. Kottke P. Hegemann (2004) Recording of blue light-induced energy and volume changes within the wild-type and mutated phot-LOV1 domain from Chlamydomonas reinhardtii. Biophys. J. 86, 1051 1060.
    • (2004) Biophys. J. , vol.86 , pp. 1051-1060
    • Losi, A.1    Kottke, T.2    Hegemann, P.3
  • 56
    • 84889274274 scopus 로고    scopus 로고
    • LOV-domain photochemistry
    • In. Edited by. W. R. Briggs. J. L. Spudich. pp. C.H.I.P.S., Texas.
    • Swartz, T. E. R. Bogomolni (2005) LOV-domain photochemistry. In Handbook of Photosensory Receptors (Edited by W. R. Briggs J. L. Spudich pp. 305 321. C.H.I.P.S., Texas.
    • (2005) Handbook of Photosensory Receptors , pp. 305-321
    • Swartz, T.E.1    Bogomolni, R.2
  • 57
    • 0001473930 scopus 로고
    • A pea plasma membrane protein exhibiting blue light-induced phosphorylation retains photosensitivity following Triton solubilization
    • Short, T. W., P. Reymond W. D. Briggs (1993) A pea plasma membrane protein exhibiting blue light-induced phosphorylation retains photosensitivity following Triton solubilization. Plant Physiol. 101, 647 655.
    • (1993) Plant Physiol. , vol.101 , pp. 647-655
    • Short, T.W.1    Reymond, P.2    Briggs, W.D.3
  • 58
    • 0000032477 scopus 로고
    • Blue light-induced phosphorylation of a plasma membrane-associated protein in Zea mays L
    • Palmer, J. M., T. M. Short, S. Gallagher W. R. Briggs (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.M.2    Gallagher, S.3    Briggs, W.R.4
  • 59
    • 0037446727 scopus 로고    scopus 로고
    • Mapping of low- and high-fluence autophosphorylation sites in phototropin 1
    • Salomon, M., E. Kneib, T. von Zeppelin W. Rüdiger (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    Kneib, E.2    Von Zeppelin, T.3    Rüdiger, W.4
  • 60
    • 0345791404 scopus 로고    scopus 로고
    • Blue-light- and phosphorylation-dependent binding of a 14-3-3 protein to phototropins in stomatal guard cells of broad bean
    • Kinoshita, T., T. Emi, M. Tominaga, K. Sakamoto, A. Shigenaga, M. Doi K. Shimazaki (2003) Blue-light- and 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.7
  • 61
    • 0036776294 scopus 로고    scopus 로고
    • Phototropin LOV domains exhibit distinct roles in regulating photoreceptor function
    • Christie, J. M., T. E. Swartz, R. A. Bogomolni W. R. Briggs (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
  • 62
    • 24944553332 scopus 로고    scopus 로고
    • Blue light-regulated molecular switch of Ser/Thr kinase in phototropin
    • Matsuoka, D. S. Tokutomi (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
  • 64
    • 0036774056 scopus 로고    scopus 로고
    • Structure and interactions of PAS kinase N-terminal PAS domain: Model for intramolecular kinase regulation
    • Amezcua, C. A., S. M. Harper, J. Rutter K. H. Gardner (2002) Structure and interactions of PAS kinase N-terminal PAS domain: Model for intramolecular kinase regulation. Structure 10, 1349 1361.
    • (2002) Structure , vol.10 , pp. 1349-1361
    • Amezcua, C.A.1    Harper, S.M.2    Rutter, J.3    Gardner, K.H.4
  • 65
    • 0029020282 scopus 로고
    • The eukaryotic protein kinase superfamily: Kinase (catalytic) domain structure and classification
    • Hanks, S. K. T. Hunter (1995) 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
  • 66
    • 0141503468 scopus 로고    scopus 로고
    • Growth signalling pathways in Arabidopsis and AGC protein kinases
    • Bögre, L., L. Ökrész, R. Henriques R. G. Anthony (2003) Growth signalling pathways in Arabidopsis and AGC protein kinases. Trends Plant Sci. 8, 424 431.
    • (2003) Trends Plant Sci. , vol.8 , pp. 424-431
    • Bögre, L.1    Ökrész, L.2    Henriques, R.3    Anthony, R.G.4
  • 67
    • 0024375582 scopus 로고
    • CAMP-dependent protein kinase. Model for an enzyme family
    • Taylor, S. S. (1989) cAMP-dependent protein kinase. Model for an enzyme family. J. Biol. Chem. 264, 8443 8445.
    • (1989) J. Biol. Chem. , vol.264 , pp. 8443-8445
    • Taylor, S.S.1
  • 68
    • 0027408171 scopus 로고
    • Crystal structure of the catalytic subunit of cAMP-dependent protein kinase complexed with MgATP and peptide inhibitor
    • Zheng, J., D. R. Kington, L. F. Ten Eyck, R. Karlsson, N.-H. Xuong, S. S. Taylor J. M. Sowadski (1993) Crystal structure of the catalytic subunit of cAMP-dependent protein kinase complexed with MgATP and peptide inhibitor. Biochemistry 32, 2154 2161.
    • (1993) Biochemistry , vol.32 , pp. 2154-2161
    • Zheng, J.1    Kington, D.R.2    Ten Eyck, L.F.3    Karlsson, R.4    Xuong, N.-H.5    Taylor, S.S.6    Sowadski, J.M.7
  • 69
    • 0029962871 scopus 로고    scopus 로고
    • Biochemical evidence for the interaction of regulatory subunit of cAMP-dependent protein kinase with IDA (Inter-DFG-APE) region of catalytic subunit
    • Sahara, S., K.-I. Sato, H. Kaise, K. Mori, A. Sato, M. Aoto, A. A. Tokmakov Y. Fukami (1996) Biochemical evidence for the interaction of regulatory subunit of cAMP-dependent protein kinase with IDA (Inter-DFG-APE) region of catalytic subunit. FEBS Lett. 384, 138 142.
    • (1996) FEBS Lett. , vol.384 , pp. 138-142
    • Sahara, S.1    Sato, K.-I.2    Kaise, H.3    Mori, K.4    Sato, A.5    Aoto, M.6    Tokmakov, A.A.7    Fukami, Y.8
  • 70
    • 0027407640 scopus 로고
    • Autoactivation of catalytic (Ca) subunit of cyclic AMP-dependent protein kinase by phosphorylation at threonine 197
    • Steinberg, R. A., R. D. Cauthron, M. M. Symcox H. Shuntoh (1993) Autoactivation of catalytic (Ca) subunit of cyclic AMP-dependent protein kinase by phosphorylation at threonine 197. Mol. Cell. Biol. 13, 2332 2341.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 2332-2341
    • Steinberg, R.A.1    Cauthron, R.D.2    Symcox, M.M.3    Shuntoh, H.4


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