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Volumn 26, Issue 5, 2001, Pages 318-324

Activation of rhodopsin: New insights from structural and biochemical studies

Author keywords

[No Author keywords available]

Indexed keywords

G PROTEIN COUPLED RECEPTOR; HORMONE; NEUROTRANSMITTER; RHODOPSIN;

EID: 0035336676     PISSN: 09680004     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0968-0004(01)01799-6     Document Type: Review
Times cited : (378)

References (54)
  • 1
    • 0027190359 scopus 로고
    • Projection structure of rhodopsin
    • Schertler G.F., et al. Projection structure of rhodopsin. Nature. 362:1993;770-772.
    • (1993) Nature , vol.362 , pp. 770-772
    • Schertler, G.F.1
  • 2
    • 0030775615 scopus 로고    scopus 로고
    • Arrangement of rhodopsin transmembrane α-helices
    • Unger V.M., et al. Arrangement of rhodopsin transmembrane α-helices. Nature. 389:1997;203-206.
    • (1997) Nature , vol.389 , pp. 203-206
    • Unger, V.M.1
  • 3
    • 0031565726 scopus 로고    scopus 로고
    • An α-carbon template for the transmembrane helices in the rhodopsin family of G-protein-coupled receptors
    • Baldwin J.M., et al. An α-carbon template for the transmembrane helices in the rhodopsin family of G-protein-coupled receptors. J. Mol. Biol. 272:1997;144-164.
    • (1997) J. Mol. Biol. , vol.272 , pp. 144-164
    • Baldwin, J.M.1
  • 4
    • 0034604451 scopus 로고    scopus 로고
    • Crystal structure of rhodopsin: A G protein-coupled receptor
    • Palczewski K., et al. Crystal structure of rhodopsin: a G protein-coupled receptor. Science. 289:2000;739-745.
    • (2000) Science , vol.289 , pp. 739-745
    • Palczewski, K.1
  • 5
    • 0344241924 scopus 로고    scopus 로고
    • Structural basis of G-protein-coupled receptor function
    • Schöneberg T., et al. Structural basis of G-protein-coupled receptor function. Mol. Cell. Endocrinol. 151:1999;181-193.
    • (1999) Mol. Cell. Endocrinol. , vol.151 , pp. 181-193
    • Schöneberg, T.1
  • 7
    • 0033597777 scopus 로고    scopus 로고
    • Folding and assembly in rhodopsin. Effect of mutations in the sixth transmembrane helix on the conformation of the third cytoplasmic loop
    • Ridge K.D., et al. Folding and assembly in rhodopsin. Effect of mutations in the sixth transmembrane helix on the conformation of the third cytoplasmic loop. J. Biol. Chem. 274:1999;21437-21442.
    • (1999) J. Biol. Chem. , vol.274 , pp. 21437-21442
    • Ridge, K.D.1
  • 8
    • 0034695482 scopus 로고    scopus 로고
    • Mutation of the fourth cytoplasmic loop of rhodopsin affects binding of transducin and peptides derived from the carboxyl-terminal sequences of transducin α and γ subunits
    • Ernst O.P., et al. Mutation of the fourth cytoplasmic loop of rhodopsin affects binding of transducin and peptides derived from the carboxyl-terminal sequences of transducin α and γ subunits. J. Biol. Chem. 275:2000;1937-1943.
    • (2000) J. Biol. Chem. , vol.275 , pp. 1937-1943
    • Ernst, O.P.1
  • 9
    • 0028156875 scopus 로고
    • Control of rhodopsin multiple phosphorylation
    • Ohguro H., et al. Control of rhodopsin multiple phosphorylation. Biochemistry. 33:1994;1023-1028.
    • (1994) Biochemistry , vol.33 , pp. 1023-1028
    • Ohguro, H.1
  • 10
    • 0032168064 scopus 로고    scopus 로고
    • Regulation of sorting and post-Golgi trafficking of rhodopsin by its C-terminal sequence QVS(A)PA
    • Deretic D., et al. Regulation of sorting and post-Golgi trafficking of rhodopsin by its C-terminal sequence QVS(A)PA. Proc. Natl. Acad. Sci. U. S. A. 95:1998;10620-10625.
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 10620-10625
    • Deretic, D.1
  • 11
    • 0034618268 scopus 로고    scopus 로고
    • AT1-receptor heterodimers show enhanced G-protein activation and altered receptor sequestration
    • AbdAlla S., et al. AT1-receptor heterodimers show enhanced G-protein activation and altered receptor sequestration. Nature. 407:2000;94-98.
    • (2000) Nature , vol.407 , pp. 94-98
    • AbdAlla, S.1
  • 12
    • 0021906833 scopus 로고
    • Transient dichroism in photoreceptor membranes indicates that stable oligomers of rhodopsin do not form during excitation
    • Downer N.W., Cone R.A. Transient dichroism in photoreceptor membranes indicates that stable oligomers of rhodopsin do not form during excitation. Biophys. J. 47:1985;277-284.
    • (1985) Biophys. J. , vol.47 , pp. 277-284
    • Downer, N.W.1    Cone, R.A.2
  • 13
    • 0033609101 scopus 로고    scopus 로고
    • Signal transfer from rhodopsin to the G-protein: Evidence for a two-site sequential fit mechanism
    • Kisselev O.G., et al. Signal transfer from rhodopsin to the G-protein: evidence for a two-site sequential fit mechanism. Proc. Natl. Acad. Sci. U. S. A. 96:1999;4898-4903.
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 4898-4903
    • Kisselev, O.G.1
  • 14
    • 0000259990 scopus 로고    scopus 로고
    • How color visual pigments are tuned
    • Kochendoerfer G.G., et al. How color visual pigments are tuned. Trends Biochem. Sci. 24:1999;300-305.
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 300-305
    • Kochendoerfer, G.G.1
  • 15
    • 0027410367 scopus 로고
    • Identification of the Cl(-)-binding site in the human red and green color vision pigments
    • Wang Z., et al. Identification of the Cl(-)-binding site in the human red and green color vision pigments. Biochemistry. 32:1993;2125-2130.
    • (1993) Biochemistry , vol.32 , pp. 2125-2130
    • Wang, Z.1
  • 16
    • 0033399668 scopus 로고    scopus 로고
    • Molecular genetics of human retinal disease
    • Rattner A., et al. Molecular genetics of human retinal disease. Annu. Rev. Genet. 33:1999;89-131.
    • (1999) Annu. Rev. Genet. , vol.33 , pp. 89-131
    • Rattner, A.1
  • 17
    • 0343580431 scopus 로고    scopus 로고
    • A comparison of the efficiency of G-protein activation by ligand-free and light-activated forms of rhodopsin
    • Melia T.J.J., et al. A comparison of the efficiency of G-protein activation by ligand-free and light-activated forms of rhodopsin. Biophys. J. 73:1997;3182-3191.
    • (1997) Biophys. J. , vol.73 , pp. 3182-3191
    • Melia, T.J.J.1
  • 18
    • 0017073070 scopus 로고
    • Energetics of primary processes in visula escitation: Photocalorimetry of rhodopsin in rod outer segment membranes
    • Cooper A., Converse C.A. Energetics of primary processes in visula escitation: photocalorimetry of rhodopsin in rod outer segment membranes. Biochemistry. 15:1976;2970-2978.
    • (1976) Biochemistry , vol.15 , pp. 2970-2978
    • Cooper, A.1    Converse, C.A.2
  • 19
    • 85025380736 scopus 로고
    • Energy, quanta, and vision
    • Hecht S., et al. Energy, quanta, and vision. J. Gen. Physiol. 25:1941;819-822.
    • (1941) J. Gen. Physiol. , vol.25 , pp. 819-822
    • Hecht, S.1
  • 20
    • 0026661978 scopus 로고
    • Constitutively active mutants of rhodopsin
    • Robinson P.R., et al. Constitutively active mutants of rhodopsin. Neuron. 9:1992;719-725.
    • (1992) Neuron , vol.9 , pp. 719-725
    • Robinson, P.R.1
  • 21
    • 0033607270 scopus 로고    scopus 로고
    • Conversion of agonistsite to metal-ion chelator site in the β(2)-adrenergic receptor
    • Elling C.E., et al. Conversion of agonistsite to metal-ion chelator site in the β(2)-adrenergic receptor. Proc. Natl. Acad. Sci. U.S.A. 96:1999;12322-12327.
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 12322-12327
    • Elling, C.E.1
  • 22
    • 0031446595 scopus 로고    scopus 로고
    • Structure and function in rhodopsin: Rhodopsin mutants with a neutral amino acid at E134 have a partially activated conformation in the dark state
    • Kim J.M., et al. Structure and function in rhodopsin: rhodopsin mutants with a neutral amino acid at E134 have a partially activated conformation in the dark state. Proc. Natl. Acad. Sci. U. S. A. 94:1997;14273-14278.
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 14273-14278
    • Kim, J.M.1
  • 23
    • 0032474444 scopus 로고    scopus 로고
    • Constitutive activation of opsin by mutation of methionine 257 on transmembrane helix 6
    • Han M., et al. Constitutive activation of opsin by mutation of methionine 257 on transmembrane helix 6. Biochemistry. 37:1998;8253-8261.
    • (1998) Biochemistry , vol.37 , pp. 8253-8261
    • Han, M.1
  • 24
    • 0034465336 scopus 로고    scopus 로고
    • Constitutive activation of G-protein-coupled receptors as a result of selective substitution of a conserved leucine residue in transmembrane helix III
    • Tao Y.X., et al. Constitutive activation of G-protein-coupled receptors as a result of selective substitution of a conserved leucine residue in transmembrane helix III. Mol. Endocrinol. 14:2000;1272-1282.
    • (2000) Mol. Endocrinol. , vol.14 , pp. 1272-1282
    • Tao, Y.X.1
  • 25
    • 0033548654 scopus 로고    scopus 로고
    • The functional topography of transmembrane domain 3 of the M1 muscarinic acetylcholine receptor, revealed by scanning mutagenesis
    • Lu Z.L., Hulme E.C. The functional topography of transmembrane domain 3 of the M1 muscarinic acetylcholine receptor, revealed by scanning mutagenesis. J. Biol. Chem. 274:1999;7309-7315.
    • (1999) J. Biol. Chem. , vol.274 , pp. 7309-7315
    • Lu, Z.L.1    Hulme, E.C.2
  • 26
    • 0018567294 scopus 로고
    • Energy uptake in the first step of visual excitation
    • Cooper A. Energy uptake in the first step of visual excitation. Nature. 282:1979;531-533.
    • (1979) Nature , vol.282 , pp. 531-533
    • Cooper, A.1
  • 27
    • 0024550169 scopus 로고
    • Complete assignment of the hydrogen out-of-plane wagging vibrations of bathorhodopsin: Chromophore structure and energy storage in the primary photoproduct of vision
    • Palings I., et al. Complete assignment of the hydrogen out-of-plane wagging vibrations of bathorhodopsin: chromophore structure and energy storage in the primary photoproduct of vision. Biochemistry. 28:1989;1498-1507.
    • (1989) Biochemistry , vol.28 , pp. 1498-1507
    • Palings, I.1
  • 28
    • 0034705612 scopus 로고    scopus 로고
    • Movement of retinal along the visual transduction path
    • Borhan B., et al. Movement of retinal along the visual transduction path. Science. 288:2000;2209-2212.
    • (2000) Science , vol.288 , pp. 2209-2212
    • Borhan, B.1
  • 29
    • 85005675452 scopus 로고
    • Spectral and kinetic characterization of visual pigment photointermediates
    • Kliger D.S., Lewis J.W. Spectral and kinetic characterization of visual pigment photointermediates. Isr. J. Chem. 35:1995;289-307.
    • (1995) Isr. J. Chem. , vol.35 , pp. 289-307
    • Kliger, D.S.1    Lewis, J.W.2
  • 30
    • 0028179864 scopus 로고
    • Interactions of the β-ionone ring with the protein in the visual pigment rhodopsin control the activation mechanism. An FTIR and fluorescence study on artificial vertebrate rhodopsins
    • Jäger F., et al. Interactions of the β-ionone ring with the protein in the visual pigment rhodopsin control the activation mechanism. An FTIR and fluorescence study on artificial vertebrate rhodopsins. Biochemistry. 33:1994;7389-7397.
    • (1994) Biochemistry , vol.33 , pp. 7389-7397
    • Jäger, F.1
  • 31
    • 0031600116 scopus 로고    scopus 로고
    • Rhodopsin: A prototypical G-protein-coupled receptor
    • Sakmar T.P. Rhodopsin: a prototypical G-protein-coupled receptor. Prog. Nucl. Acids Res. Mol. Biol. 59:1998;1-34.
    • (1998) Prog. Nucl. Acids Res. Mol. Biol. , vol.59 , pp. 1-34
    • Sakmar, T.P.1
  • 32
    • 0027298812 scopus 로고
    • Constitutive activation of opsin: Influence of charge at position 134 and size at position 296
    • Cohen G.B., et al. Constitutive activation of opsin: influence of charge at position 134 and size at position 296. Biochemistry. 32:1993;6111-6115.
    • (1993) Biochemistry , vol.32 , pp. 6111-6115
    • Cohen, G.B.1
  • 33
    • 0027716597 scopus 로고
    • Photoactivated conformational changes in rhodopsin: Atime-resolved spin label study
    • Farahbakhsh Z.T., et al. Photoactivated conformational changes in rhodopsin: atime-resolved spin label study. Science. 262:1993;1416-1419.
    • (1993) Science , vol.262 , pp. 1416-1419
    • Farahbakhsh, Z.T.1
  • 34
    • 0029907599 scopus 로고    scopus 로고
    • Requirement of rigid-body motion of transmembrane helices for light activation of rhodopsin
    • Farrens D.L., et al. Requirement of rigid-body motion of transmembrane helices for light activation of rhodopsin. Science. 274:1996;768-770.
    • (1996) Science , vol.274 , pp. 768-770
    • Farrens, D.L.1
  • 35
    • 0028017506 scopus 로고
    • Identification of glutamic acid 113 as the Schiff base proton acceptor in the metarhodopsin II photointermediate of rhodopsin
    • Jäger F., et al. Identification of glutamic acid 113 as the Schiff base proton acceptor in the metarhodopsin II photointermediate of rhodopsin. Biochemistry. 33:1994;10878-10882.
    • (1994) Biochemistry , vol.33 , pp. 10878-10882
    • Jäger, F.1
  • 36
    • 0025181491 scopus 로고
    • The dynamic aspects of proton transfer processes
    • Gutman M., Nachliel E. The dynamic aspects of proton transfer processes. Biochim. Biophys. Acta. 1015:1990;391-414.
    • (1990) Biochim. Biophys. Acta , vol.1015 , pp. 391-414
    • Gutman, M.1    Nachliel, E.2
  • 37
    • 0027317273 scopus 로고
    • Two different forms of metarhodopsin II: Schiff base deprotonation precedes proton uptake and signaling state
    • Arnis S., Hofmann K.P. Two different forms of metarhodopsin II: Schiff base deprotonation precedes proton uptake and signaling state. Proc. Natl. Acad. Sci. U. S. A. 90:1993;7849-7853.
    • (1993) Proc. Natl. Acad. Sci. U. S. A. , vol.90 , pp. 7849-7853
    • Arnis, S.1    Hofmann, K.P.2
  • 38
    • 0034730097 scopus 로고    scopus 로고
    • Transducin-dependent protonation of glutamic acid 134 in rhodopsin
    • Fahmy K., et al. Transducin-dependent protonation of glutamic acid 134 in rhodopsin. Biochemistry. 39:2000;10607-10612.
    • (2000) Biochemistry , vol.39 , pp. 10607-10612
    • Fahmy, K.1
  • 39
    • 0028061193 scopus 로고
    • A conserved carboxylic acid group mediates light-dependent proton uptake and signaling by rhodopsin
    • Arnis S., et al. A conserved carboxylic acid group mediates light-dependent proton uptake and signaling by rhodopsin. J. Biol. Chem. 269:1994;23879-23881.
    • (1994) J. Biol. Chem. , vol.269 , pp. 23879-23881
    • Arnis, S.1
  • 40
    • 0342646933 scopus 로고    scopus 로고
    • Structural alterations for proton translocation in the M state of wild-type bacteriorhodopsin
    • Sass H.J., et al. Structural alterations for proton translocation in the M state of wild-type bacteriorhodopsin. Nature. 406:2000;649-653.
    • (2000) Nature , vol.406 , pp. 649-653
    • Sass, H.J.1
  • 41
    • 0033536594 scopus 로고    scopus 로고
    • Structural changes inbacteriorhodopsin during ion transportat 2 angstrom resolution
    • Luecke H., et al. Structural changes inbacteriorhodopsin during ion transportat 2 angstrom resolution. Science. 286:1999;255-261.
    • (1999) Science , vol.286 , pp. 255-261
    • Luecke, H.1
  • 42
    • 0027967379 scopus 로고
    • Protein-protein interaction converts a proton pump into a sensory receptor
    • Spudich J.L. Protein-protein interaction converts a proton pump into a sensory receptor. Cell. 79:1994;747-750.
    • (1994) Cell , vol.79 , pp. 747-750
    • Spudich, J.L.1
  • 43
    • 0034714097 scopus 로고    scopus 로고
    • Time-resolved detection of transient movement of helix F in spin-labelled pharaonis sensory rhodopsin II
    • Wegener A.A., et al. Time-resolved detection of transient movement of helix F in spin-labelled pharaonis sensory rhodopsin II. J. Mol. Biol. 301:2000;881-891.
    • (2000) J. Mol. Biol. , vol.301 , pp. 881-891
    • Wegener, A.A.1
  • 45
    • 0034671530 scopus 로고    scopus 로고
    • Functionally discrete mimics of light-activated rhodopsin identified through expression of soluble cytoplasmic domains
    • Abdulaev N.G., et al. Functionally discrete mimics of light-activated rhodopsin identified through expression of soluble cytoplasmic domains. J. Biol. Chem. 275:2000;39354-39363.
    • (2000) J. Biol. Chem. , vol.275 , pp. 39354-39363
    • Abdulaev, N.G.1
  • 46
    • 0040141552 scopus 로고    scopus 로고
    • Signaling states of rhodopsin: Retinal provides a scaffold for activating proton transfer switches
    • Meyer C.K., et al. Signaling states of rhodopsin: retinal provides a scaffold for activating proton transfer switches. J. Biol. Chem. 275:2000;19713-19718.
    • (2000) J. Biol. Chem. , vol.275 , pp. 19713-19718
    • Meyer, C.K.1
  • 47
    • 0034254233 scopus 로고    scopus 로고
    • The molecular origin of the inhibition of transducin activation in rhodopsin lacking the 9-methyl group of the retinal chromophore: A UV-Vis and FTIR spectroscopic study
    • Vogel R., et al. The molecular origin of the inhibition of transducin activation in rhodopsin lacking the 9-methyl group of the retinal chromophore: a UV-Vis and FTIR spectroscopic study. Biochemistry. 39:2000;8895-8908.
    • (2000) Biochemistry , vol.39 , pp. 8895-8908
    • Vogel, R.1
  • 48
    • 0034640502 scopus 로고    scopus 로고
    • FTIR spectroscopy of complexes formed between metarhodopsin IIand C-terminal peptides from the G-protein α-and γ-subunits
    • Bartl F., et al. FTIR spectroscopy of complexes formed between metarhodopsin IIand C-terminal peptides from the G-protein α-and γ-subunits. FEBS Lett. 473:2000;259-264.
    • (2000) FEBS Lett. , vol.473 , pp. 259-264
    • Bartl, F.1
  • 49
    • 0026772266 scopus 로고
    • The ligand-binding domainof rhodopsin and other G protein-linked receptors
    • Oprian D.D. The ligand-binding domainof rhodopsin and other G protein-linked receptors. J. Bioenerg. Biomembr. 24:1992;211-217.
    • (1992) J. Bioenerg. Biomembr. , vol.24 , pp. 211-217
    • Oprian, D.D.1
  • 50
    • 0030614337 scopus 로고    scopus 로고
    • The activation process ofthe α1B-adrenergic receptor: Potential roleofprotonation and hydrophobicity of a highly conserved aspartate
    • Scheer A., et al. The activation process ofthe α1B-adrenergic receptor: potential roleofprotonation and hydrophobicity of a highly conserved aspartate. Proc. Natl. Acad. Sci. U.S.A. 94:1997;808-813.
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 808-813
    • Scheer, A.1
  • 51
    • 0033572969 scopus 로고    scopus 로고
    • Activation of the rod G-protein Gt by the thrombin receptor (PAR1) expressed in Sf9 cells
    • Seibert C., et al. Activation of the rod G-protein Gt by the thrombin receptor (PAR1) expressed in Sf9 cells. Eur. J. Biochem. 266:1999;911-916.
    • (1999) Eur. J. Biochem. , vol.266 , pp. 911-916
    • Seibert, C.1
  • 52
    • 0030815133 scopus 로고    scopus 로고
    • Raster3D: Photorealistic molecular graphics
    • Merritt E.A., Bacon D.J. Raster3D: photorealistic molecular graphics. Methods Enzymol. 277:1997;505-524.
    • (1997) Methods Enzymol. , vol.277 , pp. 505-524
    • Merritt, E.A.1    Bacon, D.J.2
  • 53
    • 0026522293 scopus 로고
    • Rhodopsin and phototransduction: A model system for G-protein-linked receptors
    • Hargrave P.A., McDowell J.H. Rhodopsin and phototransduction: a model system for G-protein-linked receptors. FASEBJ. 6:1992;2323-2331.
    • (1992) FASEBJ. , vol.6 , pp. 2323-2331
    • Hargrave, P.A.1    McDowell, J.H.2
  • 54
    • 0032412196 scopus 로고    scopus 로고
    • Visual pigment: G-protein-coupled receptor for light signals
    • Shichida Y., Imai H. Visual pigment: G-protein-coupled receptor for light signals. Cell. Mol. Life Sci. 54:1998;1299-1315.
    • (1998) Cell. Mol. Life Sci. , vol.54 , pp. 1299-1315
    • Shichida, Y.1    Imai, H.2


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