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Volumn 289, Issue 52, 2014, Pages 35918-35928

Differential light-induced responses in sectorial inherited retinal degeneration

Author keywords

[No Author keywords available]

Indexed keywords

CHEMICAL ACTIVATION; CHROMOPHORES; OPHTHALMOLOGY; PHOTOBLEACHING; PROTEINS;

EID: 84919797982     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.609958     Document Type: Article
Times cited : (32)

References (62)
  • 1
    • 84891376088 scopus 로고    scopus 로고
    • Advances in gene therapy technologies to treat retinitis pigmentosa
    • Petrs-Silva, H., and Linden, R. (2014) Advances in gene therapy technologies to treat retinitis pigmentosa. Clin. Ophthalmol. 8, 127-136
    • (2014) Clin. Ophthalmol. , vol.8 , pp. 127-136
    • Petrs-Silva, H.1    Linden, R.2
  • 2
    • 0027537949 scopus 로고
    • Retinitis pigmentosa. The friedenwald lecture
    • Berson, E. L. (1993) Retinitis pigmentosa. The Friedenwald Lecture. Invest. Ophthalmol. Vis. Sci. 34, 1659-1676
    • (1993) Invest. Ophthalmol. Vis. Sci. , vol.34 , pp. 1659-1676
    • Berson, E.L.1
  • 3
    • 33645535034 scopus 로고    scopus 로고
    • G protein-coupled receptor rhodopsin
    • Palczewski, K. (2006) G protein-coupled receptor rhodopsin. Annu. Rev. Biochem. 75, 743-767
    • (2006) Annu. Rev. Biochem. , vol.75 , pp. 743-767
    • Palczewski, K.1
  • 4
    • 84872221774 scopus 로고    scopus 로고
    • Structure-function of the G protein-coupled receptor superfamily
    • Katritch, V., Cherezov, V., and Stevens, R. C. (2013) Structure-function of the G protein-coupled receptor superfamily. Annu. Rev. Pharmacol. Toxicol. 53, 531-556
    • (2013) Annu. Rev. Pharmacol. Toxicol. , vol.53 , pp. 531-556
    • Katritch, V.1    Cherezov, V.2    Stevens, R.C.3
  • 5
    • 66249144426 scopus 로고    scopus 로고
    • The structure and function of G-protein-coupled receptors
    • Rosenbaum, D. M., Rasmussen, S. G., and Kobilka, B. K. (2009) The structure and function of G-protein-coupled receptors. Nature 459, 356-363
    • (2009) Nature , vol.459 , pp. 356-363
    • Rosenbaum, D.M.1    Rasmussen, S.G.2    Kobilka, B.K.3
  • 6
    • 47049130668 scopus 로고    scopus 로고
    • Crystal structure of the ligand-free G-protein-coupled receptor opsin
    • Park, J. H., Scheerer, P., Hofmann, K. P., Choe, H. W., and Ernst, O. P. (2008) Crystal structure of the ligand-free G-protein-coupled receptor opsin. Nature 454, 183-187
    • (2008) Nature , vol.454 , pp. 183-187
    • Park, J.H.1    Scheerer, P.2    Hofmann, K.P.3    Choe, H.W.4    Ernst, O.P.5
  • 9
    • 0035171024 scopus 로고    scopus 로고
    • Rhodopsin structure, function, and topography the friedenwald lecture
    • Hargrave, P. A. (2001) Rhodopsin structure, function, and topography the Friedenwald lecture. Invest. Ophthalmol. Vis. Sci. 42, 3-9
    • (2001) Invest. Ophthalmol. Vis. Sci. , vol.42 , pp. 3-9
    • Hargrave, P.A.1
  • 11
    • 77950896264 scopus 로고    scopus 로고
    • Covalent bond between ligand and receptor required for efficient activation in rhodopsin
    • Matsuyama, T., Yamashita, T., Imai, H., and Shichida, Y. (2010) Covalent bond between ligand and receptor required for efficient activation in rhodopsin. J. Biol. Chem. 285, 8114-8121
    • (2010) J. Biol. Chem. , vol.285 , pp. 8114-8121
    • Matsuyama, T.1    Yamashita, T.2    Imai, H.3    Shichida, Y.4
  • 12
    • 0014411230 scopus 로고
    • Molecular basis of visual excitation
    • Wald, G. (1968) Molecular basis of visual excitation. Science 162, 230-239
    • (1968) Science , vol.162 , pp. 230-239
    • Wald, G.1
  • 13
    • 77953384365 scopus 로고    scopus 로고
    • Complexes between photoactivated rhodopsin and transducin: Progress and questions
    • Jastrzebska, B., Tsybovsky, Y., and Palczewski, K. (2010) Complexes between photoactivated rhodopsin and transducin: progress and questions. Biochem. J. 428, 1-10
    • (2010) Biochem. J. , vol.428 , pp. 1-10
    • Jastrzebska, B.1    Tsybovsky, Y.2    Palczewski, K.3
  • 14
    • 69549108193 scopus 로고    scopus 로고
    • Multiple switches in G protein-coupled receptor activation
    • Ahuja, S., and Smith, S. O. (2009) Multiple switches in G protein-coupled receptor activation. Trends Pharmacol. Sci. 30, 494-502
    • (2009) Trends Pharmacol. Sci. , vol.30 , pp. 494-502
    • Ahuja, S.1    Smith, S.O.2
  • 15
    • 77953252509 scopus 로고    scopus 로고
    • The quest to understand heterotrimeric G protein signaling
    • Tesmer, J. J. (2010) The quest to understand heterotrimeric G protein signaling. Nat. Struct. Mol. Biol. 17, 650-652
    • (2010) Nat. Struct. Mol. Biol. , vol.17 , pp. 650-652
    • Tesmer, J.J.1
  • 16
    • 27744542188 scopus 로고    scopus 로고
    • Cell toxicity and conformational disease
    • Carrell, R. W. (2005) Cell toxicity and conformational disease. Trends Cell Biol. 15, 574-580
    • (2005) Trends Cell Biol. , vol.15 , pp. 574-580
    • Carrell, R.W.1
  • 17
    • 73649098238 scopus 로고    scopus 로고
    • Molecular mechanisms of rhodopsin retinitis pigmentosa and the efficacy of pharmacological rescue
    • Krebs, M. P., Holden, D. C., Joshi, P., Clark, C. L., 3rd, Lee, A. H., and Kaushal, S. (2010) Molecular mechanisms of rhodopsin retinitis pigmentosa and the efficacy of pharmacological rescue. J. Mol. Biol. 395, 1063-1078
    • (2010) J. Mol. Biol. , vol.395 , pp. 1063-1078
    • Krebs, M.P.1    Holden, D.C.2    Joshi, P.3    Clark, C.L.4    Lee, A.H.5    Kaushal, S.6
  • 18
    • 71349083669 scopus 로고    scopus 로고
    • Conformational diseases: Looking into the eyes
    • Surguchev, A., and Surguchov, A. (2010) Conformational diseases: looking into the eyes. Brain Res. Bull. 81, 12-24
    • (2010) Brain Res. Bull. , vol.81 , pp. 12-24
    • Surguchev, A.1    Surguchov, A.2
  • 20
    • 17044363529 scopus 로고    scopus 로고
    • Mechanisms of cell death in rhodopsin retinitis pigmentosa: Implications for therapy
    • Mendes, H. F., van der Spuy, J., Chapple, J. P., and Cheetham, M. E. (2005) Mechanisms of cell death in rhodopsin retinitis pigmentosa: implications for therapy. Trends Mol. Med. 11, 177-185
    • (2005) Trends Mol. Med. , vol.11 , pp. 177-185
    • Mendes, H.F.1    Van Der Spuy, J.2    Chapple, J.P.3    Cheetham, M.E.4
  • 21
    • 0034015064 scopus 로고    scopus 로고
    • Characterization of rhodopsin mis-sorting and constitutive activation in a transgenic rat model of retinitis pigmentosa
    • Green, E. S., Menz, M. D., LaVail, M. M., and Flannery, J. G. (2000) Characterization of rhodopsin mis-sorting and constitutive activation in a transgenic rat model of retinitis pigmentosa. Invest. Ophthalmol. Vis. Sci. 41, 1546-1553
    • (2000) Invest. Ophthalmol. Vis. Sci. , vol.41 , pp. 1546-1553
    • Green, E.S.1    Menz, M.D.2    LaVail, M.M.3    Flannery, J.G.4
  • 22
    • 0032590225 scopus 로고    scopus 로고
    • 2+, and photoreceptor death: New evidence for the equivalent-light hypothesis from arrestin knockout mice
    • 2+, and photoreceptor death: new evidence for the equivalent-light hypothesis from arrestin knockout mice. Invest. Ophthalmol. Vis. Sci. 40, 2770-2772
    • (1999) Invest. Ophthalmol. Vis. Sci. , vol.40 , pp. 2770-2772
    • Fain, G.L.1    Lisman, J.E.2
  • 23
    • 0028892944 scopus 로고
    • Support for the equivalent light hypothesis for RP
    • Lisman, J., and Fain, G. (1995) Support for the equivalent light hypothesis for RP. Nat. Med. 1, 1254-1255
    • (1995) Nat. Med. , vol.1 , pp. 1254-1255
    • Lisman, J.1    Fain, G.2
  • 24
    • 0030931599 scopus 로고    scopus 로고
    • Structure and function in rhodopsin: Packing of the helices in the transmembrane domain and folding to a tertiary structure in the intradiscal domain are coupled
    • Hwa, J., Garriga, P., Liu, X., and Khorana, H. G. (1997) Structure and function in rhodopsin: packing of the helices in the transmembrane domain and folding to a tertiary structure in the intradiscal domain are coupled. Proc. Natl. Acad. Sci. U.S.A. 94, 10571-10576
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 10571-10576
    • Hwa, J.1    Garriga, P.2    Liu, X.3    Khorana, H.G.4
  • 25
    • 0031966320 scopus 로고    scopus 로고
    • Mechanisms of cell death in the inherited retinal degenerations
    • Travis, G. H. (1998) Mechanisms of cell death in the inherited retinal degenerations. Am. J. Hum. Genet. 62, 503-508
    • (1998) Am. J. Hum. Genet. , vol.62 , pp. 503-508
    • Travis, G.H.1
  • 26
    • 0033603239 scopus 로고    scopus 로고
    • Rhodopsin's carboxy-terminal cytoplasmic tail acts as a membrane receptor for cytoplasmic dynein by binding to the dynein light chain Tctex-1
    • Tai, A. W., Chuang, J. Z., Bode, C., Wolfrum, U., and Sung, C. H. (1999) Rhodopsin's carboxy-terminal cytoplasmic tail acts as a membrane receptor for cytoplasmic dynein by binding to the dynein light chain Tctex-1. Cell 97, 877-887
    • (1999) Cell , vol.97 , pp. 877-887
    • Tai, A.W.1    Chuang, J.Z.2    Bode, C.3    Wolfrum, U.4    Sung, C.H.5
  • 27
    • 0032617816 scopus 로고    scopus 로고
    • Severe autosomal dominant retinitis pigmentosa caused by a novel rhodopsin mutation (Ter349Glu). Mutations in brief no. 208. Online
    • Bessant, D. A., Khaliq, S., Hameed, A., Anwar, K., Payne, A. M., Mehdi, S. Q., and Bhattacharya, S. S. (1999) Severe autosomal dominant retinitis pigmentosa caused by a novel rhodopsin mutation (Ter349Glu). Mutations in brief no. 208. Online. Hum. Mutat. 13, 83
    • (1999) Hum. Mutat. , vol.13 , pp. 83
    • Bessant, D.A.1    Khaliq, S.2    Hameed, A.3    Anwar, K.4    Payne, A.M.5    Mehdi, S.Q.6    Bhattacharya, S.S.7
  • 28
    • 0027452148 scopus 로고
    • Rhodopsin mutations responsible for autosomal dominant retinitis pigmentosa. Clustering of functional classes along the polypeptide chain
    • Sung, C. H., Davenport, C. M., and Nathans, J. (1993) Rhodopsin mutations responsible for autosomal dominant retinitis pigmentosa. Clustering of functional classes along the polypeptide chain. J. Biol. Chem. 268, 26645-26649
    • (1993) J. Biol. Chem. , vol.268 , pp. 26645-26649
    • Sung, C.H.1    Davenport, C.M.2    Nathans, J.3
  • 29
    • 19044370864 scopus 로고    scopus 로고
    • Sector retinitis pigmentosa
    • Van Woerkom, C., and Ferrucci, S. (2005) Sector retinitis pigmentosa. Optometry 76, 309-317
    • (2005) Optometry , vol.76 , pp. 309-317
    • Van Woerkom, C.1    Ferrucci, S.2
  • 31
    • 77957055780 scopus 로고
    • Integrated methods for the construction of three-dimensional models and computational probing of structure-function relations in G protein-coupled receptors
    • Ballesteros, J. A., and Weinstein, H. (1995) Integrated methods for the construction of three-dimensional models and computational probing of structure-function relations in G protein-coupled receptors. Methods Neurosci. 25, 366-428
    • (1995) Methods Neurosci. , vol.25 , pp. 366-428
    • Ballesteros, J.A.1    Weinstein, H.2
  • 33
    • 0035754285 scopus 로고    scopus 로고
    • Signal transmission via G protein-coupled receptors in the light of rhodopsin structure determination
    • Ciarkowski, J., Drabik, P., Gieldoń, A., Kaźmierkiewicz, R., and Slusarz, R. (2001) Signal transmission via G protein-coupled receptors in the light of rhodopsin structure determination. Acta Biochim. Pol. 48, 1203-1207
    • (2001) Acta Biochim. Pol. , vol.48 , pp. 1203-1207
    • Ciarkowski, J.1    Drabik, P.2    Gieldoń, A.3    Kaźmierkiewicz, R.4    Slusarz, R.5
  • 35
    • 52949134162 scopus 로고    scopus 로고
    • Pharmacological manipulation of gain-of-function and dominant-negative mechanisms in rhodopsin retinitis pigmentosa
    • Mendes, H. F., and Cheetham, M. E. (2008) Pharmacological manipulation of gain-of-function and dominant-negative mechanisms in rhodopsin retinitis pigmentosa. Hum. Mol. Genet. 17, 3043-3054
    • (2008) Hum. Mol. Genet. , vol.17 , pp. 3043-3054
    • Mendes, H.F.1    Cheetham, M.E.2
  • 38
    • 0028957661 scopus 로고
    • Structure and function in rhodopsin. Measurement of the rate of metarhodopsin II decay by fluorescence spectroscopy
    • Farrens, D. L., and Khorana, H. G. (1995) Structure and function in rhodopsin. Measurement of the rate of metarhodopsin II decay by fluorescence spectroscopy. J. Biol. Chem. 270, 5073-5076
    • (1995) J. Biol. Chem. , vol.270 , pp. 5073-5076
    • Farrens, D.L.1    Khorana, H.G.2
  • 39
    • 82955194481 scopus 로고    scopus 로고
    • Salt effects on the conformational stability of the visual G-proteincoupled receptor rhodopsin
    • Reyes-Alcaraz, A., Martínez-Archundia, M., Ramon, E., and Garriga, P. (2011) Salt effects on the conformational stability of the visual G-proteincoupled receptor rhodopsin. Biophys. J. 101, 2798-2806
    • (2011) Biophys. J. , vol.101 , pp. 2798-2806
    • Reyes-Alcaraz, A.1    Martínez-Archundia, M.2    Ramon, E.3    Garriga, P.4
  • 41
    • 4344581120 scopus 로고    scopus 로고
    • The retinal conformation and its environment in rhodopsin in light of a new 2.2 Å crystal structure
    • Okada, T., Sugihara, M., Bondar, A. N., Elstner, M., Entel, P., and Buss, V. (2004) The retinal conformation and its environment in rhodopsin in light of a new 2.2 Å crystal structure. J. Mol. Biol. 342, 571-583
    • (2004) J. Mol. Biol. , vol.342 , pp. 571-583
    • Okada, T.1    Sugihara, M.2    Bondar, A.N.3    Elstner, M.4    Entel, P.5    Buss, V.6
  • 43
  • 44
    • 33846302070 scopus 로고    scopus 로고
    • The role of internal water molecules in the structure and function of the rhodopsin family of G protein-coupled receptors
    • Pardo, L., Deupi, X., Dölker, N., López-Rodríguez, M. L., and Campillo, M. (2007) The role of internal water molecules in the structure and function of the rhodopsin family of G protein-coupled receptors. Chembiochem 8, 19-24
    • (2007) Chembiochem , vol.8 , pp. 19-24
    • Pardo, L.1    Deupi, X.2    Dölker, N.3    López-Rodríguez, M.L.4    Campillo, M.5
  • 45
    • 79955064613 scopus 로고    scopus 로고
    • Alterations in the photoactivation pathway of rhodopsin mutants associated with retinitis pigmentosa
    • Bosch-Presegué, L., Ramon, E., Toledo, D., Cordomí, A., and Garriga, P. (2011) Alterations in the photoactivation pathway of rhodopsin mutants associated with retinitis pigmentosa. FEBS J. 278, 1493-1505
    • (2011) FEBS J. , vol.278 , pp. 1493-1505
    • Bosch-Presegué, L.1    Ramon, E.2    Toledo, D.3    Cordomí, A.4    Garriga, P.5
  • 46
    • 84874994703 scopus 로고    scopus 로고
    • Improved conformational stability of the visual G protein-coupled receptor rhodopsin by specific interaction with docosahexaenoic acid phospholipid
    • Sánchez-Martín, M. J., Ramon, E., Torrent-Burgués, J., and Garriga, P. (2013) Improved conformational stability of the visual G protein-coupled receptor rhodopsin by specific interaction with docosahexaenoic acid phospholipid. Chembiochem 14, 639-644
    • (2013) Chembiochem , vol.14 , pp. 639-644
    • Sánchez-Martín, M.J.1    Ramon, E.2    Torrent-Burgués, J.3    Garriga, P.4
  • 50
    • 0026058548 scopus 로고
    • Functional heterogeneity of mutant rhodopsins responsible for autosomal dominant retinitis pigmentosa
    • Sung, C. H., Schneider, B. G., Agarwal, N., Papermaster, D. S., and Nathans, J. (1991) Functional heterogeneity of mutant rhodopsins responsible for autosomal dominant retinitis pigmentosa. Proc. Natl. Acad. Sci. U.S.A. 88, 8840-8844
    • (1991) Proc. Natl. Acad. Sci. U.S.A. , vol.88 , pp. 8840-8844
    • Sung, C.H.1    Schneider, B.G.2    Agarwal, N.3    Papermaster, D.S.4    Nathans, J.5
  • 51
    • 84893200167 scopus 로고    scopus 로고
    • Vitamin A derivatives as treatment options for retinal degenerative diseases
    • Perusek, L., and Maeda, T. (2013) Vitamin A derivatives as treatment options for retinal degenerative diseases. Nutrients 5, 2646-2666
    • (2013) Nutrients , vol.5 , pp. 2646-2666
    • Perusek, L.1    Maeda, T.2
  • 52
    • 0027374544 scopus 로고
    • Protonation states of membrane-embedded carboxylic acid groups in rhodopsin and metarhodopsin II: A Fourier-transform infrared spectroscopy study of site-directed mutants
    • Fahmy, K., Jäger, F., Beck, M., Zvyaga, T. A., Sakmar, T. P., and Siebert, F. (1993) Protonation states of membrane-embedded carboxylic acid groups in rhodopsin and metarhodopsin II: a Fourier-transform infrared spectroscopy study of site-directed mutants. Proc. Natl. Acad. Sci. U.S.A. 90, 10206-10210
    • (1993) Proc. Natl. Acad. Sci. U.S.A. , vol.90 , pp. 10206-10210
    • Fahmy, K.1    Jäger, F.2    Beck, M.3    Zvyaga, T.A.4    Sakmar, T.P.5    Siebert, F.6
  • 55
    • 0037309870 scopus 로고    scopus 로고
    • A morphometric study of light-induced damage in transgenic rat models of retinitis pigmentosa
    • Vaughan, D. K., Coulibaly, S. F., Darrow, R. M., and Organisciak, D. T. (2003) A morphometric study of light-induced damage in transgenic rat models of retinitis pigmentosa. Invest. Ophthalmol. Vis. Sci. 44, 848-855
    • (2003) Invest. Ophthalmol. Vis. Sci. , vol.44 , pp. 848-855
    • Vaughan, D.K.1    Coulibaly, S.F.2    Darrow, R.M.3    Organisciak, D.T.4
  • 58
    • 0037402504 scopus 로고    scopus 로고
    • Blue light dose distribution and retinitis pigmentosa visual field defects: An hypothesis
    • Schwartz, L., Boëlle, P. Y., D'hermies, F., Ledanois, G., and Virmont, J. (2003) Blue light dose distribution and retinitis pigmentosa visual field defects: an hypothesis. Med. Hypotheses 60, 644-649
    • (2003) Med. Hypotheses , vol.60 , pp. 644-649
    • Schwartz, L.1    Boëlle, P.Y.2    D'Hermies, F.3    Ledanois, G.4    Virmont, J.5
  • 60
    • 84907484404 scopus 로고    scopus 로고
    • Photoactivation-induced instability of rhodopsin mutants T4K and T17M in rod outer segments underlies retinal degeneration in X. Laevis transgenic models of retinitis pigmentosa
    • Tam, B. M., Noorwez, S. M., Kaushal, S., Kono, M., and Moritz, O. L. (2014) Photoactivation-induced instability of rhodopsin mutants T4K and T17M in rod outer segments underlies retinal degeneration in X. laevis transgenic models of retinitis pigmentosa. J. Neurosci. 34, 13336-13348
    • (2014) J. Neurosci. , vol.34 , pp. 13336-13348
    • Tam, B.M.1    Noorwez, S.M.2    Kaushal, S.3    Kono, M.4    Moritz, O.L.5
  • 61
    • 71349086327 scopus 로고    scopus 로고
    • Light-dependent translocation of arrestin in rod photoreceptors is signaled through a phospholipase C cascade and requires ATP
    • Orisme, W., Li, J., Goldmann, T., Bolch, S., Wolfrum, U., and Smith, W. C. (2010) Light-dependent translocation of arrestin in rod photoreceptors is signaled through a phospholipase C cascade and requires ATP. Cell. Signal. 22, 447-456
    • (2010) Cell. Signal. , vol.22 , pp. 447-456
    • Orisme, W.1    Li, J.2    Goldmann, T.3    Bolch, S.4    Wolfrum, U.5    Smith, W.C.6


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