Diversity of visual pigments from the viewpoint of G protein activation - Comparison with other G protein-coupled receptors

Photochemical and Photobiological Sciences

Volumn 2, Issue 12, 2003, Pages 1237-1246

  Shichida, Yoshinori ^a   Yamashita, Takahiro ^a,b  

^a KYOTO UNIVERSITY   (Japan)

^b JAPAN SCIENCE AND TECHNOLOGY AGENCY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

G PROTEIN COUPLED RECEPTOR; VISUAL PIGMENT; GUANINE NUCLEOTIDE BINDING PROTEIN;

MOLECULAR MECHANICS; PHOTORECEPTOR; PRIORITY JOURNAL; REVIEW; ANIMAL; ARTICLE; COMPARATIVE STUDY; PHYSIOLOGY; RETINA; VERTEBRATE;

ANIMALS; GTP-BINDING PROTEINS; RECEPTORS, G-PROTEIN-COUPLED; RETINA; RETINAL PIGMENTS; VERTEBRATES;

EID: 3042836946     PISSN: 1474905X     EISSN: 14749092     Source Type: Journal    
DOI: 10.1039/b300434a     Document Type: Review

References (121)

1. A. Ovchinnikov Yu, Rhodopsin and bacteriorhodopsin: structure-function relationships, FEBS Lett., 1982, 148, 179-191.
2. P. A. Hargrave, J. H. McDowell, D. R. Curtis, J. K. Wang, E. Juszczak, S. L. Fong, J. K. Rao and P. Argos, The structure of bovine rhodopsin, Biophys. Struct. Mech., 1983, 9, 235-244.
3. J. Nathans and D. S. Hogness, Isolation, sequence analysis, and intron-exon arrangement of the gene encoding bovine rhodopsin, Cell, 1983, 34, 807-814.
4. T. Hara and R. Hara, New photosensitive pigment found in the retina of the squid Ommastrephes, Nature, 1965, 206, 1331-1334.
5. M. Koyanagi, A. Terakita, K. Kubokawa and Y. Shichida, Amphioxus homologs of Go-coupled rhodopsin and peropsin having 11-cis- and all-trans-retinals as their chromophore, FEBS Lett., 2002, 531, 525-528.
6. B. K. Fung, J. B. Hurley and L. Stryer, Flow of information in the light-triggered cyclic nucleotide cascade of vision, Proc. Natl. Acad. Sci. U.S.A., 1981, 78, 152-156.
7. T. Shinozawa, S. Uchida, E. Martin, D. Cafiso, W. Hubbell and M. Bitensky, Additional component required for activity and reconstitution of light-activated vertebrate photoreceptor GTPase, Proc. Natl. Acad. Sci. U.S.A., 1980, 77, 1408-1411.
8. E. E. Fesenko, S. S. Kolesnikov and A. L. Lyubarsky, Induction by cyclic GMP of cationic conductance in plasma membrane of retinal rod outer segment, Nature, 1985, 313, 310-313.
9. B. Rayer, M. Naynert and H. Stieve, Phototransduction: different mechanisms in vertebrates and invertebrates, J. Photochem. Photobiol. B, 1990, 7, 107-148.
10. S. Yarfitz and J. B. Hurley, Transduction mechanisms of vertebrate and invertebrate photoreceptors, J. Biol. Chem., 1994, 269, 14329-14332.
11. A. Terakita, T. Hariyama, Y. Tsukahara, Y. Katsukura and H. Tashiro, Interaction of GTP-binding protein Gq with photo-activated rhodopsin in the photoreceptor membranes of crayfish, FEBS Lett., 1993, 330, 197-200.
12. Y. J. Lee, S. Shah, E. Suzuki, T. Zars, P. M. O'Day and D. R. Hyde, The Drosophila dgq gene encodes a G alpha protein that mediates phototransduction, Neuron, 1994, 13, 1143-1157.
13. T. Suzuki, K. Narita, K. Yoshihara, K. Nagai and Y. Kito, Phosphatidyl inositol-phospholipase C in squid photoreceptor membrane is activated by stable metarhodopsin via GTP-binding protein, Gq, Vision Res., 1995, 35, 1011-1017.
14. S. Kikkawa, K. Tominaga, M. Nakagawa, T. Iwasa and M. Tsuda, Simple purification and functional reconstitution of octopus photoreceptor Gq, which couples rhodopsin to phospholipase C, Biochemistry, 1996, 35, 15857-15864.
15. H. Reuss, M. H. Mojet, S. Chyb and R. C. Hardie, In vivo analysis of the drosophila light-sensitive channels, TRP and TRPL, Neuron, 1997, 19, 1249-1259.
16. 2+ cascade, Neuron, 1995, 15, 607-618.
17. D. Kojima, A. Terakita, T. Ishikawa, Y. Tsukahara, A. Maeda and Y. Shichida, A novel Go-mediated phototransduction cascade in scallop visual cells, J. Biol. Chem., 1997, 272, 22979-22982.
18. G. Wald, Molecular basis of visual excitation, Science, 1968, 162, 230-239.
19. D. Bownds, Site of attachment of retinal in rhodopsin, Nature, 1967, 216, 1178-1181.
20. T. Okada, I. Le Trong, B. A. Fox, C. A. Behnke, R. E. Stenkamp and K. Palczewski, X-Ray diffraction analysis of three-dimensional crystals of bovine rhodopsin obtained from mixed micelles, J. Struct. Biol., 2000, 130, 73-80.
21. K. Palczewski, T. Kumasaka, T. Hori, C. A. Behnke, H. Motoshima, B. A. Fox, I. Le Trong, D. C. Teller, T. Okada, R. E. Stenkamp, M. Yamamoto and M. Miyano, Crystal structure of rhodopsin: A G protein-coupled receptor, Science, 2000, 289, 739-745.
22. E. A. Zhukovsky and D. D. Oprian, Effect of carboxylic acid side chains on the absorption maximum of visual pigments, Science, 1989, 246, 928-930.
23. T. P. Sakmar, R. R. Franke and H. G. Khorana, Glutamic acid-113 serves as the retinylidene Schiff base counterion in bovine rhodopsin, Proc. Natl. Acad. Sci. U.S.A., 1989, 86, 8309-8313.
24. J. Nathans, Determinants of visual pigment absorbance: identification of the retinylidene Schiffs base counterion in bovine rhodopsin, Biochemistry, 1990, 29, 9746-9752.
25. A. Terakita, T. Yamashita and Y. Shichida, Highly conserved glutamic acid in the extracellular IV-V loop in rhodopsins acts as the counterion in retinochrome, a member of the rhodopsin family, Proc. Natl. Acad. Sci. U.S.A., 2000, 97, 14263-14267.
26. Y. Gat and M. Sheves, A mechanism for controlling the pKa of the retinal protonated Schiff base in retinal proteins. A study with model compounds, J. Am. Chem. Soc., 1993, 115, 3772-3773.
27. M. Han, B. S. DeDecker and S. O. Smith, Localization of the retinal protonated Schiff base counterion in rhodopsin, Biophys. J., 1993, 65, 899-906.
28. T. Okada, Y. Fujiyoshi, M. Silow, J. Navarro, E. M. Landau and Y. Shichida, Functional role of internal water molecules in rhodopsin revealed by X-ray crystallography, Proc. Natl. Acad. Sci. U.S.A., 2002, 99, 5982-5987.
29. T. Nagata, A. Terakita, H. Kandori, D. Kojima, Y. Shichida and A. Maeda, Water and peptide backbone structure in the active center of bovine rhodopsin, Biochemistry, 1997, 36, 6164-6170.
30. E. C. Yan, M. A. Kazmi, S. De, B. S. Chang, C. Seibert, E. P. Marin, R. A. Mathies and T. P. Sakmar, Function of extracellular loop 2 in rhodopsin: glutamic acid 181 modulates stability and absorption wavelength of metarhodopsin II, Biochemistry, 2002, 41, 3620-3627.
31. Y. Shichida, S. Matuoka and T. Yoshizawa, Formation of photorhodopsin, a precursor of bathorhodopsin, detected by a pico-second laser photolysis at room temperature, Photobiochem. Photobiophys., 1984, 7, 221-228.
32. T. Yoshizawa and Y. Shichida, Low-temperature spectrophotometry of intermediates of rhodopsin, Methods Enzymol., 1982, 81, 333-354.
33. S. J. Hug, J. W. Lewis, C. M. Einterz, T. E. Thorgeirsson and D. S. Kliger, Nanosecond photolysis of rhodopsin: evidence for a new, blue-shifted intermediate, Biochemistry, 1990, 29, 1475-1485.
34. Y. Shichida and H. Imai, Visual pigment: G-protein-coupled receptor for light signals, Cell. Mol. Life Sci., 1998, 54, 1299-1315.
35. Y. Fukada and T. Yoshizawa, Activation of phosphodiesterase in frog rod outer segment by an intermediate of rhodopsin photolysis. II, Biochim. Biophys. Acta, 1981, 675, 195-200.
36. D. Emeis, H. Kuhn, J. Reichert and K. P. Hofmann, Complex formation between metarhodopsin II and GTP-binding protein in bovine photoreceptor membranes leads to a shift of the photoproduct equilibrium, FEBS Lett., 1982, 143, 29-34.
37. S. Tachibanaki, H. Imai, T. Mizukami, T. Okada, Y. Imamoto, T. Matsuda, Y. Fukada, A. Terakita and Y. Shichida, Presence of two rhodopsin intermediates responsible for transducin activation, Biochemistry, 1997, 36, 14173-14180.
38. S. Tachibanaki, H. Imai, A. Terakita and Y. Shichida, Identification of a new intermediate state that binds but not activates transducin in the bleaching process of bovine rhodopsin, FEBS Lett., 1998, 425, 126-130.
39. Y. Shichida, T. Okada, H. Kandori, Y. Fukada and T. Yoshizawa, Nanosecond laser photolysis of iodopsin, a chicken red-sensitive cone visual pigment, Biochemistry, 1993, 32, 10832-10838.
40. H. Imai, Y. Imamoto, T. Yoshizawa and Y. Shichida, Difference in molecular properties between chicken green and rhodopsin as related to the functional difference between cone and rod photoreceptor cells, Biochemistry, 1995, 34, 10525-10531.
41. H. Imai, A. Terakita, S. Tachibanaki, Y. Imamoto, T. Yoshizawa and Y. Shichida, Photochemical and biochemical properties of chicken blue-sensitive cone visual pigment, Biochemistry, 1997, 36, 12773-12779.
42. E. N. Pugh, Jr. and T. D. Lamb, Amplification and kinetics of the activation steps in phototransduction, Biochim. Biophys. Acta, 1993, 1141, 111-149.
43. K. W. Yau, Phototransduction mechanism in retinal rods and cones. The Friedenwald Lecture, Invest. Ophthalmol. Vis. Sci., 1994, 35, 9-32.
44. D. Baylor, How photons start vision, Proc. Natl. Acad. Sci. U.S.A., 1996, 93, 560-565.
45. S. Tachibanaki, S. Tsushima and S. Kawamura, Low amplification and fast visual pigment phosphorylation as mechanisms characterizing cone photoresponses, Proc. Natl. Acad. Sci. U.S.A., 2001, 98, 14044-14049.
46. H. Imai, D. Kojima, T. Oura, S. Tachibanaki, A. Terakita and Y. Shichida, Single amino acid residue as a functional determinant of rod and cone visual pigments, Proc. Natl. Acad. Sci. U.S.A., 1997, 94, 2322-2326.
47. S. Kuwayama, H. Imai, T. Hirano, A. Terakita and Y. Shichida, Conserved proline residue at position 189 in cone visual pigments as a determinant of molecular properties different from rhodopsins, Biochemistry, 2002, 41, 15245-15252.
48. B. Borhan, M. L. Souto, H. Imai, Y. Shichida and K. Nakanishi, Movement of retinal along the visual transduction path, Science, 2000, 288, 2209-2212.
49. T. Okano, D. Kojima, Y. Fukada, Y. Shichida and T. Yoshizawa, Primary structures of chicken cone visual pigments: vertebrate rhodopsins have evolved out of cone visual pigments, Proc. Natl. Acad. Sci. U.S.A., 1992, 89, 5932-5936.
50. T. Okano, T. Yoshizawa and Y. Fukada, Pinopsin is a chicken pineal photoreceptive molecule, Nature, 1994, 372, 94-97.
51. S. Blackshaw and S. H. Snyder, Parapinopsin, a novel catfish opsin localized to the parapineal organ, defines a new gene family, J. Neurosci., 1997, 17, 8083-8092.
52. H. Mano, D. Kojima and Y. Fukada, Exo-rhodopsin: a novel rhodopsin expressed in the zebrafish pineal gland, Brain Res. Mol. Brain Res., 1999, 73, 110-118.
53. I. Provencio, G. Jiang, W. J. De Grip, W. P. Hayes and M. D. Rollag, Melanopsin: An opsin in melanophores, brain, and eye, Proc. Natl. Acad. Sci. U.S.A., 1998, 95, 340-345.
54. I. Provencio, I. R. Rodriguez, G. Jiang, W. P. Hayes, E. F. Moreira and M. D. Rollag, A novel human opsin in the inner retina, J. Neurosci., 2000, 20, 600-605.
55. H. Sun, D. J. Gilbert, N. G. Copeland, N. A. Jenkins and J. Nathans, Peropsin, a novel visual pigment-like protein located in the apical microvilli of the retinal pigment epithelium, Proc. Natl. Acad. Sci. U.S.A., 1997, 94, 9893-9898.
56. B. G. Soni, A. R. Philp, R. G. Foster and B. E. Knox, Novel retinal photoreceptors, Nature, 1998, 394, 27-28.
57. M. Jiang, S. Pandey and H. K. Fong, An opsin homologue in the retina and pigment epithelium, Invest. Ophthalmol. Vis. Sci., 1993, 34, 3669-3678.
58. R. A. Dixon, B. K. Kobilka, D. J. Strader, J. L. Benovic, H. G. Dohlman, T. Frielle, M. A. Bolanowski, C. D. Bennett, E. Rands, R. E. Diehl, R. A. Mumford, E. E. Slater, I. S. Sigal, M. G. Caron, R. J. Lefkowitz and C. D. Strader, Cloning of the gene and cDNA for mammalian beta-adrenergic receptor and homology with rhodopsin, Nature, 1986, 321, 75-79.
59. D. L. Farrens, C. Altenbach, K. Yang, W. L. Hubbell and H. G. Khorana, Requirement of rigid-body motion of transmembrane helices for light activation of rhodopsin, Science, 1996, 274, 768-770.
60. S. P. Sheikh, T. A. Zvyaga, O. Lichtarge, T. P. Sakmar and H. R. Bourne, Rhodopsin activation blocked by metal-ion-binding sites linking transmembrane helices C and F, Nature, 1996, 383, 347-350.
61. T. D. Dunham and D. L. Farrens, Conformational changes in rhodopsin. Movement of helix f detected by site-specific chemical labeling and fluorescence spectroscopy, J. Biol. Chem., 1999, 274, 1683-1690.
62. R. R. Franke, B. Konig, T. P. Sakmar, H. G. Khorana and K. P. Hofmann, Rhodopsin mutants that bind but fail to activate transducin, Science, 1990, 250, 123-125.
63. R. R. Franke, T. P. Sakmar, R. M. Graham and H. G. Khorana, Structure and function in rhodopsin. Studies of the interaction between the rhodopsin cytoplasmic domain and transducin, J. Biol. Chem., 1992, 267, 14767-14774.
64. W. Shi, S. Osawa, C. D. Dickerson and E. R. Weiss, Rhodopsin mutants discriminate sites important for the activation of rhodopsin kinase and Gt, J. Biol. Chem., 1995, 270, 2112-2119.
65. K. D. Ridge, C. Zhang and H. G. Khorana, Mapping of the amino acids in the cytoplasmic loop connecting helices C and D in rhodopsin. Chemical reactivity in the dark state following single cysteine replacements, Biochemistry, 1995, 34, 8804-8811.
66. K. Yang, D. L. Farrens, W. L. Hubbell and H. G. Khorana, Structure and function in rhodopsin. Single cysteine substitution mutants in the cytoplasmic interhelical E-F loop region show position-specific effects in transducin activation, Biochemistry, 1996, 35, 12464-12469.
67. S. Acharya, Y. Saad and S. S. Karnik, Transducin-alpha C-terminal peptide binding site consists of C-D and E-F loops of rhodopsin, J. Biol. Chem., 1997, 272, 6519-6524.
68. E. P. Marin, A. G. Krishna, T. A. Zvyaga, J. Isele, F. Siebert and T. P. Sakmar, The amino terminus of the fourth cytoplasmic loop of rhodopsin modulates rhodopsin-transducin interaction, J. Biol. Chem., 2000, 275, 1930-1936.
69. O. P. Ernst, C. K. Meyer, E. P. Marin, P. Henklein, W. Y. Fu, T. P. Sakmar and K. P. Hofmann, Mutation of the fourth cytoplasmic loop of rhodopsin affects binding of transducin and peptides derived from the carboxyl-terminal sequences of transducin alpha and gamma subunits, J. Biol. Chem., 2000, 275, 1937-1943.
70. B. Konig, A. Arendt, J. H. McDowell, M. Kahlert, P. A. Hargrave and K. P. Hofmann, Three cytoplasmic loops of rhodopsin interact with transducin, Proc. Natl. Acad. Sci. U.S.A., 1989, 86, 6878-6882.
71. E. R. Weiss, D. J. Kelleher and G. L. Johnson, Mapping sites of interaction between rhodopsin and transducin using rhodopsin antipeptide antibodies, J. Biol. Chem., 1988, 263, 6150-6154.
72. N. G. Abdulaev, T. Ngo, R. Chen, Z. Lu and K. D. Ridge, Functionally discrete mimics of light-activated rhodopsin identified through expression of soluble cytoplasmic domains, J. Biol. Chem., 2000, 275, 39354-39363.
73. J. F. Resek, Z. T. Farahbakhsh, W. L. Hubbell and H. G. Khorana, Formation of the meta II photointermediate is accompanied by conformational changes in the cytoplasmic surface of rhodopsin, Biochemistry, 1993, 32, 12025-12032.
74. Y. Imamoto, M. Kataoka, F. Tokunaga and K. Palczewski, Light-induced conformational changes of rhodopsin probed by fluorescent alexa594 immobilized on the cytoplasmic surface, Biochemistry, 2000, 39, 15225-15233.
75. D. G. Lambright, J. P. Noel, H. E. Hamm and P. B. Sigler, Structural determinants for activation of the alpha-subunit of a heterotrimeric G protein, Nature, 1994, 369, 621-628.
76. D. G. Lambright, J. Sondek, A. Bohm, N. P. Skiba, H. E. Hamm and P. B. Sieler, The 2.0 A crystal structure of a heterotrimeric G protein, Nature, 1996, 379, 311-319.
77. B. R. Conklin, Z. Farfel, K. D. Lustig, D. Julius and H. R. Bourne, Substitution of three amino acids switches receptor specificity of Gq alpha to that of Gi alpha, Nature, 1993, 363, 274-276.
78. H. E. Hamm, D. Deretic, A. Arendt, P. A. Hargrave, B. Koenig and K. P. Hofmann, Site of G protein binding to rhodopsin mapped with synthetic peptides from the alpha subunit, Science, 1988, 241, 832-835.
79. O. G. Kisselev, J. Kao, J. W. Ponder, Y. C. Fann, N. Gautam and G. R. Marshall, Light-activated rhodopsin induces structural binding motif in G protein alpha subunit, Proc. Natl. Acad. Sci. U.S.A., 1998, 95, 4270-4275.
80. S. Nishimura, H. Kandori and A. Maeda, Interaction between photoactivated rhodopsin and the C-terminal peptide of transducin alpha-subunit studied by FTIR spectroscopy, Biochemistry, 1998, 37, 15816-15824.
81. T. Morizumi, H. Imai and Y. Shichida to be submitted.
82. A. Terakita, T. Yamashita, N. Nimbari, D. Kojima and Y. Shichida, Functional interaction between bovine rhodopsin and G protein transducin, J. Biol. Chem., 2002, 277, 40-46.
83. K. Cai, Y. Itoh and H. G. Khorana, Mapping of contact sites in complex formation between transducin and light-activated rhodopsin by covalent crosslinking: use of a photoactivatable reagent, Proc. Natl. Acad. Sci. U.S.A., 2001, 98, 4877-4882.
84. Y. Itoh, K. Cai and H. G. Khorana, Mapping of contact sites in complex formation between light-activated rhodopsin and transducin by covalent crosslinking: use of a chemically preactivated reagent, Proc. Natl. Acad. Sci. U.S.A., 2001, 98, 4883-4887.
85. J. Liu, B. R. Conklin, N. Blin, J. Yun and J. Wess, Identification of a receptor/G-protein contact site critical for signaling specificity and G-protein activation, Proc. Natl. Acad. Sci. U.S.A., 1995, 92, 11642-11646.
86. Y. Takagi, H. Ninomiya, A. Sakamoto, S. Miwa and T. Masaki, Structural basis of G protein specificity of human endothelin receptors. A study with endothelinA/B chimeras, J. Biol. Chem., 1995, 270, 10072-10078.
87. J. Liu and J. Wess, Different single receptor domains determine the distinct G protein coupling profiles of members of the vasopressin receptor family, J. Biol. Chem., 1996, 271, 8772-8778.
88. M. G. Eason and S. B. Liggett, Chimeric mutagenesis of putative G-protein coupling domains of the alpha2A-adrenergic receptor. Localization of two redundant and fully competent gi coupling domains, J. Biol. Chem., 1996, 271, 12826-12832.
89. J. Wess, G-protein-coupled receptors: molecular mechanisms involved in receptor activation and selectivity of G-protein recognition, FASEB J., 1997, 11, 346-354.
90. S. K. Wong and E. M. Ross, Chimeric muscarinic cholinergic:beta- adrenergic receptors that are functionally promiscuous among G proteins, J. Biol. Chem., 1994, 269, 18968-18976.
91. F. Y. Zeng, A. Hopp, A. Soldner and J. Wess, Use of a disulfide cross-linking strategy to study muscarinic receptor structure and mechanisms of activation, J. Biol. Chem., 1999, 274, 16629-16640.
92. S. P. Sheikh, J. P. Vilardarga, T. J. Baranski, O. Lichtarge, T. Iiri, E. C. Meng, R. A. Nissenson and H. R. Bourne, Similar structures and shared switch mechanisms of the beta2-adrenoceptor and the parathyroid hormone receptor. Zn(II) bridces between helices III and VI block activation, J. Biol. Chem., 1999, 274, 17033-17041.
93. U. Gether, S. Lin, P. Ghanouni, J. A. Ballesteros, H. Weinstein and B. K. Kobilka, Agonists induce conformational changes in transmembrane domains III and VI of the beta2 adrenoceptor, EMBO J., 1997, 16, 6737-6747.
94. A. D. Jensen, F. Guarnieri, S. G. Rasmussen, F. Asmar, J. A. Ballesteros and U. Gether, Agonist-induced conformational changes at the cytoplasmic side of transmembrane segment 6 in the beta 2 adrenergic receptor mapped by site-selective fluorescent labeling, J. Biol. Chem., 2001, 276, 9279-9290.
95. P. Ghanouni, J. J. Steenhuis, D. L. Farrens and B. K. Kobilka, Agonist-induced conformational changes in the G-protein-coupling domain of the beta 2 adrenergic receptor, Proc. Natl. Acad. Sci. U.S.A., 2001, 98, 5997-6002.
96. S. D. Ward, F. F. Hamdan, L. M. Bloodworth and J. Wess, Conformational changes that occur during M3 muscarinic acetylcholine receptor activation probed by the use of an in situ disulfide cross-linking strategy, J. Biol. Chem., 2002, 277, 2247-2257.
97. J. P. Noel, H. E. Hamm and P. B. Sigler, The 2.2 A crystal structure of transducin-alpha complexed with GTP gamma S, Nature, 1993, 366, 654-663.
98. J. Sondek, D. G. Lambright, J. P. Noel, H. E. Hamm and P. B. Sigler, GTPase mechanism of Gproteins from the 1.7-A crystal structure of transducin alpha-GDP-AIF-4, Nature, 1994, 372, 276-279.
99. R. K. Sunahara, J. J. Tesmer, A. G. Gilman and S. R. Sprang, Crystal structure of the adenylyl cyclase activator Gsalpha, Science, 1997, 278, 1943-1947.
100. T. Yamashita and A. Terakita and Y. Shichida, Distinct roles of the second and third cytoplasmic loops of bovine rhodopsin in G protein activation, J. Biol. Chem., 2000, 275, 34272-34279.
101. K. J. Fryxell and E. M. Meyerowitz, The evolution of rhodopsins and neurotransmitter receptors, J. Mol. Evol., 1991, 33, 367-378.
102. N. Iwabe Diversification and Evolution of the Signal Transduction System: Rapid Divergence of Tissue Specific Genes in Early Evolution of Chordates, PhD thesis, 1993, Kyushu University, Japan.
103. K. J. Fryxell, The evolutionary divergence of neurotransmitter receptors and second-messenger pathways, J. Mol. Evol., 1995, 41, 85-97.
104. J. Bockaert and J. P. Pin, Molecular tinkering of G protein-coupled receptors: an evolutionary success, EMBO J., 1999, 18, 1723-1729.
105. U. Gether, Uncovering molecular mechanisms involved in activation of G protein-coupled receptors, Endocr. Rev., 2000, 21, 90-113.
106. T. Ishihara, S. Nakamura, Y. Kaziro, T. Takahashi, K. Takahashi and S. Nagata, Molecular cloning and expression of a cDNA encoding the secretin receptor, EMBO J., 1991, 10, 1635-1641.
107. M. Laburthe, A. Couvineau, P. Gaudin, J. J. Maoret, Rouyer-C. Fessard and P. Nicole, Receptors for VIP, PACAP, secretin, GRF, glucagon, GLP-1 and other members of their new family of G protein-linked receptors: structure-function relationship with special reference to the human VIP-1 receptor, Ann. New York Acad. Sci., 1996, 805, 94-111.
108. M. Masu, Y. Tanabe, K. Tsuchida, R. Shigemoto and S. Nakanishi, Sequence and expression of a metabotropic glutamate receptor, Nature, 1991, 349, 760-765.
109. K. M. Houamed, J. L. Kuijper, T. L. Gilbert, B. A. Haldeman, P. J. O'Hara, E. R. Mulvihill, W. Almers and F. S. Hagen, Cloning, expression and gene structure of a G protein-coupled glutamate receptor from rat brain, Science, 1991, 252, 1318-1321.
110. A. P. West, Jr., L. L. Llamas, P. M. Snow, S. Benzer and P. J. Bjorkman, Crystal structure of the ectodomain of Methuselah, a Drosophila G protein-coupled receptor associated with extended lifespan, Proc. Natl. Acad. Sci. U.S.A., 2001, 98, 3744-3749.
111. A. M. Cypess, C. G. Unson, C. R. Wu and T. P. Sakmar, Two cytoplasmic loops of the glucagon receptor are required to elevate cAMP or intracellular calcium, J. Biol. Chem., 1999, 274, 19455-19464.
112. M. Hallbrink, T. Holmqvist, M. Olsson, C. G. Ostenson, S. Efendic and U. Langel, Different domains in the third intracellular loop of the GLP-1 receptor are responsible for Galpha(s) and Galpha(i)/Galpha(o) activation, Biochim. Biophys. Acta, 2001, 1546, 79-86.
113. N. Kunishima, Y. Shimada, Y. Tsuji, T. Sato, M. Yamamoto, T. Kumasaka, S. Nakanishi, H. Jingami and K. Morikawa, Structural basis of glutamate recognition by a dimeric metabotropic glutamate receptor, Nature, 2000, 407, 971-977.
114. 3+, Proc. Natl. Acad. Sci. U.S.A., 2002, 99, 2660-2665.
115. J. P. Pin, C. Joly, S. F. Heinemann and J. Bockaert, Domains involved in the specificity of G protein activation in phospholipase C-coupled metabotropic glutamate receptors, EMBO J., 1994, 13, 342-348.
116. J. Gomeza, C. Joly, R. Kuhn, T. Knopfel, J. Bockaert and J. P. Pin, The second intracellular loop of metabotropic glutamate receptor 1 cooperates with the other intracellular domains to control coupling to G-proteins, J. Biol. Chem., 1996, 271, 2199-2205.
117. A. Francesconi and R. M. Duvoisin, Role of the second and third intracellular loops of metabotropic glutamate receptors in mediating dual signal transduction activation, J. Biol. Chem., 1998, 273, 5615-5624.
118. T. Yamashita, A. Terakita and Y. Shichida, The second cytoplasmic loop of metabotropic glutamate receptor functions at the third loop position of rhodopsin, J. Biochem. (Tokyo), 2001, 130, 149-155.
119. J. Blahos, 2nd, S. Mary, J. Perroy, C. de Colle, I. Brabet, J. Bockaert and J. P. Pin, Extreme C terminus of G protein alpha-subunits contains a site that discriminates between Gi-coupled metabotropic glutamate receptors, J. Biol. Chem., 1998, 273, 25765-25769.
120. M. Franek, A. Pagano, K. Kaupmann, B. Bettler, J. P. Pin and J. Blahos, The heteromeric GABA-B receptor recognizes G-protein alpha subunit C-termini, Neuropharmacology, 1999, 38, 1657-1666.
121. S. Blackshaw and S. H. Snyder, Encephalopsin: a novel mammalian extraretinal opsin discretely localized in the brain, J. Neurosci., 1999, 19, 3681-3690.