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Volumn 11, Issue 5, 1997, Pages 346-354

G-protein-coupled receptors: molecular mechanisms involved in receptor activation and selectivity of G-protein recognition

Author keywords

receptor structure; receptor G protein interactions; signal transduction

Indexed keywords

GUANINE NUCLEOTIDE BINDING PROTEIN;

EID: 0030938936     PISSN: 08926638     EISSN: None     Source Type: Journal    
DOI: 10.1096/fasebj.11.5.9141501     Document Type: Review
Times cited : (513)

References (87)
  • 2
    • 0027318238 scopus 로고
    • Structural elements of Ga subunits that interact with Gβg, receptors, and effectors
    • Conklin, B. R., and Bourne, H. R. (1993) Structural elements of Ga subunits that interact with Gβg, receptors, and effectors. Cell 73, 631-641
    • (1993) Cell , vol.73 , pp. 631-641
    • Conklin, B.R.1    Bourne, H.R.2
  • 3
    • 0028860268 scopus 로고
    • Heterotrimeric G proteins: Organizers of transmembrane signals
    • Neer, E. J. (1995) Heterotrimeric G proteins: organizers of transmembrane signals. Cell 80, 249-257
    • (1995) Cell , vol.80 , pp. 249-257
    • Neer, E.J.1
  • 4
    • 0025812324 scopus 로고
    • Model systems for the study of seven-transmembrane-segment receptors
    • Dohlman, H. G., Thorner, J., Caron, M. G., and Lefkowitz, R. J. (1991) Model systems for the study of seven-transmembrane-segment receptors. Annu. Rev. Biochem. 60, 653-688
    • (1991) Annu. Rev. Biochem. , vol.60 , pp. 653-688
    • Dohlman, H.G.1    Thorner, J.2    Caron, M.G.3    Lefkowitz, R.J.4
  • 5
    • 0026548156 scopus 로고
    • In vitro mutagenesis and the search for structure-function relationships among G protein-coupled receptors
    • Savarese, T. M., and Fraser, C. M. (1992) In vitro mutagenesis and the search for structure-function relationships among G protein-coupled receptors, Biochem. J. 283, 1-19
    • (1992) Biochem. J. , vol.283 , pp. 1-19
    • Savarese, T.M.1    Fraser, C.M.2
  • 7
    • 0028230817 scopus 로고
    • Expanding horizons for receptors coupled to G proteins: Diversity and disease
    • Coughlin, S. R. (1994) Expanding horizons for receptors coupled to G proteins: diversity and disease. Curr. Opin. Cell. Biol. 6, 191-197
    • (1994) Curr. Opin. Cell. Biol. , vol.6 , pp. 191-197
    • Coughlin, S.R.1
  • 8
    • 0027933763 scopus 로고
    • Locating ligand-binding sites in 7TM receptors by protein engineering
    • Schwartz, T. W. (1994) Locating ligand-binding sites in 7TM receptors by protein engineering. Curr. Opin. Biotechnol. 5, 434-444
    • (1994) Curr. Opin. Biotechnol. , vol.5 , pp. 434-444
    • Schwartz, T.W.1
  • 10
    • 0028962270 scopus 로고
    • Low resolution structure of bovine rhodopsin determined by electron cryo-microscopy
    • Linger, V. M., and Schertler, G. F. X. (1995) Low resolution structure of bovine rhodopsin determined by electron cryo-microscopy. Biophys. J. 68, 1776-1786
    • (1995) Biophys. J. , vol.68 , pp. 1776-1786
    • Linger, V.M.1    Schertler, G.F.X.2
  • 11
    • 0029556994 scopus 로고
    • Projection structure of frog rhodopsin in two crystal forms
    • Schertler, G. F. X., and Hargrave, P. A. (1995) Projection structure of frog rhodopsin in two crystal forms. Proc. Natl. Acad. Sci. USA 92, 11578-11582
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 11578-11582
    • Schertler, G.F.X.1    Hargrave, P.A.2
  • 12
    • 0025292355 scopus 로고
    • Model of the structure of bacteriorhodopsin based on high-resolution electron cryo-microseopy
    • Henderson, R., Baldwin, J. M., Ceska, T. A., Zemlin, F., Beckmann, E., and Downing, K. H. (1990) Model of the structure of bacteriorhodopsin based on high-resolution electron cryo-microseopy. J. Mol. Biol. 213, 899-929
    • (1990) J. Mol. Biol. , vol.213 , pp. 899-929
    • Henderson, R.1    Baldwin, J.M.2    Ceska, T.A.3    Zemlin, F.4    Beckmann, E.5    Downing, K.H.6
  • 13
    • 0027506471 scopus 로고
    • The probable arrangement of the helices in G protein-coupled receptors
    • Baldwin, J. M. (1993) The probable arrangement of the helices in G protein-coupled receptors. EMBO J. 12, 1693-1703
    • (1993) EMBO J. , vol.12 , pp. 1693-1703
    • Baldwin, J.M.1
  • 14
    • 0028227013 scopus 로고
    • Structure and function of receptors coupled to G proteins
    • Baldwin, J. M. (1994) Structure and function of receptors coupled to G proteins. Curr. Opin. Cell Biol. 6, 180-190
    • (1994) Curr. Opin. Cell Biol. , vol.6 , pp. 180-190
    • Baldwin, J.M.1
  • 15
    • 0026592867 scopus 로고
    • Identification of intramolecular interactions in adrenergic receptors
    • Suryanarayana, S., von Zastrow, M., and Kobilka, B. K. (1992) Identification of intramolecular interactions in adrenergic receptors. J. Biol. Chem. 267, 21991-21994
    • (1992) J. Biol. Chem. , vol.267 , pp. 21991-21994
    • Suryanarayana, S.1    Von Zastrow, M.2    Kobilka, B.K.3
  • 16
    • 0028012105 scopus 로고
    • Intramolecular interactions in muscarinic acetylcholine receptors studied with chimeric m2/m5 receptors
    • Pittel, Z., and Wess, J. (1994) Intramolecular interactions in muscarinic acetylcholine receptors studied with chimeric m2/m5 receptors. Mol. Pharmacol. 45, 61-64
    • (1994) Mol. Pharmacol. , vol.45 , pp. 61-64
    • Pittel, Z.1    Wess, J.2
  • 18
    • 0029096818 scopus 로고
    • Mutational analysis of the relative orientation of transmembrane helices I and VII in G protein-coupled receptors
    • Liu, J., Schöneberg, T., van Rhee, M., and Wess, J. (1995) Mutational analysis of the relative orientation of transmembrane helices I and VII in G protein-coupled receptors. J. Biol. Chem. 270, 19532-19539
    • (1995) J. Biol. Chem. , vol.270 , pp. 19532-19539
    • Liu, J.1    Schöneberg, T.2    Van Rhee, M.3    Wess, J.4
  • 19
    • 0030028517 scopus 로고    scopus 로고
    • Arrangement of transmembrane domains in adrenergic receptors: Similarity to bacteriorhodopsin
    • Mizobe, T., Maze, M., Suryanarayana, S., and Kobilka, B. K. (1996) Arrangement of transmembrane domains in adrenergic receptors: similarity to bacteriorhodopsin. J. Biol. Chem. 271, 2387-2389
    • (1996) J. Biol. Chem. , vol.271 , pp. 2387-2389
    • Mizobe, T.1    Maze, M.2    Suryanarayana, S.3    Kobilka, B.K.4
  • 20
    • 0028800729 scopus 로고
    • Conversion of antagonist-binding site to metal-ion site in the tachykinin NK-1 receptor
    • Elling, C. E., Nielsen, S. M., and Schwartz, T. W. (1995) Conversion of antagonist-binding site to metal-ion site in the tachykinin NK-1 receptor. Nature (London) 374, 74-77
    • (1995) Nature (London) , vol.374 , pp. 74-77
    • Elling, C.E.1    Nielsen, S.M.2    Schwartz, T.W.3
  • 21
    • 0029778268 scopus 로고    scopus 로고
    • Rhodopsin activation blocked by metal-ion-binding sites linking transmembrane helices C and F
    • Sheikh, S. P., Zvyaga, T. A., Lichtarge, O., Sakmar, T. P., and Bourne, H. R. (1996) Rhodopsin activation blocked by metal-ion-binding sites linking transmembrane helices C and F. Nature (London) 383, 347-350
    • (1996) Nature (London) , vol.383 , pp. 347-350
    • Sheikh, S.P.1    Zvyaga, T.A.2    Lichtarge, O.3    Sakmar, T.P.4    Bourne, H.R.5
  • 22
    • 0029907599 scopus 로고    scopus 로고
    • Requirement of rigid-body motion of transmembrane helices for light activation of rhodopsin
    • Farrens, D. L., Altenbach, C., Yang, K., Hubbell, W. L., and Khorana, H. G. (1996) Requirement of rigid-body motion of transmembrane helices for light activation of rhodopsin. Science 274, 768-770
    • (1996) Science , vol.274 , pp. 768-770
    • Farrens, D.L.1    Altenbach, C.2    Yang, K.3    Hubbell, W.L.4    Khorana, H.G.5
  • 23
    • 0029680797 scopus 로고    scopus 로고
    • Structure and function in rhodopsin. Cysteines 65 and 316 are in proximity in a rhodopsin mutant as indicated by disulfide formation and interactions between attached spin labels
    • In press
    • Yang, K., Farrens, D. L., Altenbach, C., Hubbell, W. L., and Khorana, H. G. (1996) Structure and function in rhodopsin. Cysteines 65 and 316 are in proximity in a rhodopsin mutant as indicated by disulfide formation and interactions between attached spin labels. Biochemistry In press
    • (1996) Biochemistry
    • Yang, K.1    Farrens, D.L.2    Altenbach, C.3    Hubbell, W.L.4    Khorana, H.G.5
  • 24
    • 0028890276 scopus 로고
    • NMR and circular dichroism studies of synthetic peptides derived from the third intracellular loop of the β-adrenoceptor
    • Jung, H., Windhaber, R., Palm, D., and Schnackerz, K. D. (1995) NMR and circular dichroism studies of synthetic peptides derived from the third intracellular loop of the β-adrenoceptor. FEBS Lett. 358, 133-136
    • (1995) FEBS Lett. , vol.358 , pp. 133-136
    • Jung, H.1    Windhaber, R.2    Palm, D.3    Schnackerz, K.D.4
  • 25
    • 0029882204 scopus 로고    scopus 로고
    • Conformation of a β-adrenoceptor-derived signal transducing peptide as inferred by circular dichroism and 1H NMR spectroscopy
    • Jung, H., Windhaber, R., Palm, D., and Schnackerz, K. D. (1996) Conformation of a β-adrenoceptor-derived signal transducing peptide as inferred by circular dichroism and 1H NMR spectroscopy. Biochemistry 35, 6399-6405
    • (1996) Biochemistry , vol.35 , pp. 6399-6405
    • Jung, H.1    Windhaber, R.2    Palm, D.3    Schnackerz, K.D.4
  • 26
    • 0030606345 scopus 로고    scopus 로고
    • Structure determination of the fourth cytoplasmic loop and carboxyl terminal domain of bovine rhodopsin
    • In press
    • Yeagle, P. L., Alderfer, J. L., and Albert, A. D. (1996) Structure determination of the fourth cytoplasmic loop and carboxyl terminal domain of bovine rhodopsin. Mol. Vision In press
    • (1996) Mol. Vision
    • Yeagle, P.L.1    Alderfer, J.L.2    Albert, A.D.3
  • 27
    • 0029818551 scopus 로고    scopus 로고
    • Structural features and light-dependent changes in the cytoplasmic interhelical E-F loop region of rhodopsin: A site-directed spin labeling study
    • Altenbach, C., Yang, K., Farrens, D. L. Farahbakhsh, Z. T., Khorana, H. G., and Hubbell, W. L. (1996) Structural features and light-dependent changes in the cytoplasmic interhelical E-F loop region of rhodopsin: a site-directed spin labeling study. Biochemistry 35, 12470-12478
    • (1996) Biochemistry , vol.35 , pp. 12470-12478
    • Altenbach, C.1    Yang, K.2    Farrens, D.L.3    Farahbakhsh, Z.T.4    Khorana, H.G.5    Hubbell, W.L.6
  • 28
    • 0029035661 scopus 로고
    • Mapping light-dependent structural changes in the cytoplasmic loop connecting helices C and D in rhodopsin: A site-directed spin labeling study
    • Farahbakhsh, Z. T., Ridge, K. D., Khorana, H. G., and Hubbell, W. L. (1995) Mapping light-dependent structural changes in the cytoplasmic loop connecting helices C and D in rhodopsin: a site-directed spin labeling study. Biochemistry 34, 8812-8819
    • (1995) Biochemistry , vol.34 , pp. 8812-8819
    • Farahbakhsh, Z.T.1    Ridge, K.D.2    Khorana, H.G.3    Hubbell, W.L.4
  • 29
    • 0026522293 scopus 로고
    • Rhodopsin and phototransduction: A model system for G protein-linked receptors
    • Hargrave, P. A., and McDowell, J. H. (1992) Rhodopsin and phototransduction: a model system for G protein-linked receptors. FASEB J. 6, 2323-2331
    • (1992) FASEB J. , vol.6 , pp. 2323-2331
    • Hargrave, P.A.1    McDowell, J.H.2
  • 30
    • 0029756165 scopus 로고    scopus 로고
    • Specific tryptophan UV-absorbance changes are probes of the transition of rhodopsin to its active state
    • Lin, S. W., and Sakmar, T. P. (1996) Specific tryptophan UV-absorbance changes are probes of the transition of rhodopsin to its active state. Biochemistry 35, 11149-11159
    • (1996) Biochemistry , vol.35 , pp. 11149-11159
    • Lin, S.W.1    Sakmar, T.P.2
  • 31
    • 0027716597 scopus 로고
    • Photoactivated conformational changes in rhodopsin: A time-resolved spin label study
    • Farahhakhsh, Z. T., Hideg, K., and Hubbell, W. L. (1993) Photoactivated conformational changes in rhodopsin: a time-resolved spin label study. Science 262, 1416-1419
    • (1993) Science , vol.262 , pp. 1416-1419
    • Farahhakhsh, Z.T.1    Hideg, K.2    Hubbell, W.L.3
  • 32
    • 0027439826 scopus 로고
    • Electron diffraction analysis of structural changes in the photocylce of bacteriorhodopsin
    • Subramaniam, S., Gerstein, M., Oesterhelt, D., and Henderson, R. (1993) Electron diffraction analysis of structural changes in the photocylce of bacteriorhodopsin. EMBO J. 12, 1-8
    • (1993) EMBO J. , vol.12 , pp. 1-8
    • Subramaniam, S.1    Gerstein, M.2    Oesterhelt, D.3    Henderson, R.4
  • 33
    • 0029759342 scopus 로고    scopus 로고
    • Agonist-specific conformational changes in the yeast α-factor pheromone receptor
    • Bukusoglu, G., and Jenness, D. D. (1996) Agonist-specific conformational changes in the yeast α-factor pheromone receptor. Mol. Cell. Biol. 16, 4818-4823
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 4818-4823
    • Bukusoglu, G.1    Jenness, D.D.2
  • 34
    • 0028856707 scopus 로고
    • Fluorescent labeling of purified β2 adrenergic receptor: Evidence for ligand-specific conformational changes
    • Gether, U., Lin, S., and Kobilka, B. K. (1995) Fluorescent labeling of purified β2 adrenergic receptor: evidence for ligand-specific conformational changes. J. Biol. Chem. 270, 28268-28275
    • (1995) J. Biol. Chem. , vol.270 , pp. 28268-28275
    • Gether, U.1    Lin, S.2    Kobilka, B.K.3
  • 35
    • 0027297275 scopus 로고
    • Constitutive activity of receptors coupled to guanine nucleotide regulatory proteins
    • Lefkowitz, R. J., Cotecchia, S., Samama, P., and Costa, T. (1993) Constitutive activity of receptors coupled to guanine nucleotide regulatory proteins. Trends Pharmacol. Sci. 14, 303-307
    • (1993) Trends Pharmacol. Sci. , vol.14 , pp. 303-307
    • Lefkowitz, R.J.1    Cotecchia, S.2    Samama, P.3    Costa, T.4
  • 36
    • 0029963793 scopus 로고    scopus 로고
    • Defects in G protein-coupled signal transduction in human disease
    • Spiegel, A. M. (1996) Defects in G protein-coupled signal transduction in human disease. Annu. Rev. Physiol. 58, 143-170
    • (1996) Annu. Rev. Physiol. , vol.58 , pp. 143-170
    • Spiegel, A.M.1
  • 37
    • 0029898348 scopus 로고    scopus 로고
    • Is there a "lock" for all agonist "keys" in 7TM receptors?
    • Schwartz, T. W., and Rosenkilde, M. M. (1996) Is there a "lock" for all agonist "keys" in 7TM receptors? Trends Pharmarol. Sci. 17, 213-216
    • (1996) Trends Pharmarol. Sci. , vol.17 , pp. 213-216
    • Schwartz, T.W.1    Rosenkilde, M.M.2
  • 39
    • 0028125886 scopus 로고
    • Rhodopsin mutation G90D and a molecular mechanism for congenital night blindness
    • Rao, V. R., Cohen, G. B., and Oprian, D. D. (1994) Rhodopsin mutation G90D and a molecular mechanism for congenital night blindness. Nature (London) 367, 639-642
    • (1994) Nature (London) , vol.367 , pp. 639-642
    • Rao, V.R.1    Cohen, G.B.2    Oprian, D.D.3
  • 40
    • 0029661256 scopus 로고    scopus 로고
    • 1b-adrenergic receptor is initiated by disruption of an interhelical salt bridge constraint
    • 1b-adrenergic receptor is initiated by disruption of an interhelical salt bridge constraint. J. Biol. Chem. 271, 28318-28323
    • (1996) J. Biol. Chem. , vol.271 , pp. 28318-28323
    • Porter, J.E.1    Hwa, J.2    Perez, D.M.3
  • 41
    • 0029832901 scopus 로고    scopus 로고
    • Transmembrane regions V and VI of the human luteinizing hormone receptor are required for constitutive activation by a mutation in the third intracellular loop
    • Kudo, M., Osuga, Y., Kobilka, B. K., and Hsueh, A. J. W. (1996) Transmembrane regions V and VI of the human luteinizing hormone receptor are required for constitutive activation by a mutation in the third intracellular loop. J. Biol. Chem. 271, 22470-22478
    • (1996) J. Biol. Chem. , vol.271 , pp. 22470-22478
    • Kudo, M.1    Osuga, Y.2    Kobilka, B.K.3    Hsueh, A.J.W.4
  • 42
    • 0029664397 scopus 로고    scopus 로고
    • 1-adrenergic receptor subtypes identify critical residues that modulate active state isomerization
    • 1-adrenergic receptor subtypes identify critical residues that modulate active state isomerization. J. Biol. Chem. 271, 7956-7964
    • (1996) J. Biol. Chem. , vol.271 , pp. 7956-7964
    • Hwa, J.1    Graham, R.M.2    Perez, D.M.3
  • 43
    • 0027422737 scopus 로고
    • Specificity of receptor-G protein interactions: Searching for the structure behind the signal
    • Hedin, K. E., Duerson, K., and Clapham, D. E. (1993) Specificity of receptor-G protein interactions: searching for the structure behind the signal. Cell. Signalling 5, 505-518
    • (1993) Cell. Signalling , vol.5 , pp. 505-518
    • Hedin, K.E.1    Duerson, K.2    Clapham, D.E.3
  • 44
    • 0028842093 scopus 로고
    • Multiple mechanisms of receptor-G protein signaling specificity
    • Raymond, J. R. (1995) Multiple mechanisms of receptor-G protein signaling specificity. Am. J. Physiol. 269, F141-F158
    • (1995) Am. J. Physiol. , vol.269
    • Raymond, J.R.1
  • 46
    • 0027936892 scopus 로고
    • Membrane organization in G-protein mechanisms
    • Neubig, R. R. (1994) Membrane organization in G-protein mechanisms. FASEB J. 8, 939-946
    • (1994) FASEB J. , vol.8 , pp. 939-946
    • Neubig, R.R.1
  • 49
    • 0025882303 scopus 로고
    • Multisite contacts involved in coupling of the β-adrenergic receptor with the stimulatory guanine-nucleotide-binding regulatory protein
    • Münch, G., Dees, C., Hekman, M., and Palm, D. (1991) Multisite contacts involved in coupling of the β-adrenergic receptor with the stimulatory guanine-nucleotide-binding regulatory protein. Eur. J. Biochem. 198, 357-364
    • (1991) Eur. J. Biochem. , vol.198 , pp. 357-364
    • Münch, G.1    Dees, C.2    Hekman, M.3    Palm, D.4
  • 50
    • 0026630552 scopus 로고
    • 2-adrenergic receptors based upon characteristics in primary structure
    • 2-adrenergic receptors based upon characteristics in primary structure. J. Biol. Chem. 267, 8342-8346
    • (1992) J. Biol. Chem. , vol.267 , pp. 8342-8346
    • Okamoto, T.1    Nishimoto, I.2
  • 52
    • 0028361809 scopus 로고
    • Chimeric muscarinic cholinergic: β-adrenergic receptors that are functionally promiscuous among G proteins
    • Wong, S. K.-F., and Ross, E. M. (1994) Chimeric muscarinic cholinergic: β-adrenergic receptors that are functionally promiscuous among G proteins. J. Biol. Chem. 269, 18968-18976
    • (1994) J. Biol. Chem. , vol.269 , pp. 18968-18976
    • Wong, S.K.-F.1    Ross, E.M.2
  • 53
    • 0029059732 scopus 로고
    • q/11 by the m3 muscarinic acetylcholine receptor
    • q/11 by the m3 muscarinic acetylcholine receptor. J. Biol. Chem. 270, 17741-17748
    • (1995) J. Biol. Chem. , vol.270 , pp. 17741-17748
    • Blin, N.1    Yun, J.2    Wess, J.3
  • 54
    • 0026780339 scopus 로고
    • Structure and function in rhodopsin: Studies of the interaction between the rhodopsin cytoplasmic domain and transducin
    • Franke, R. R., Sakmar, T. P., Graham, R. M., and Khorana, H. G. (1992) Structure and function in rhodopsin: studies of the interaction between the rhodopsin cytoplasmic domain and transducin. J. Biol. Chem. 267, 14767-14774
    • (1992) J. Biol. Chem. , vol.267 , pp. 14767-14774
    • Franke, R.R.1    Sakmar, T.P.2    Graham, R.M.3    Khorana, H.G.4
  • 55
    • 0027430336 scopus 로고
    • Nephrogenic diabetes insipidus: A V2 vasopressin receptor unable to stimulate adenylyl cyclase
    • Rosenthal, W., Antaramian, A., Gilbert, S., and Birnbaumer, M. (1993) Nephrogenic diabetes insipidus: a V2 vasopressin receptor unable to stimulate adenylyl cyclase. J. Biol. Chem. 268, 13030-13033
    • (1993) J. Biol. Chem. , vol.268 , pp. 13030-13033
    • Rosenthal, W.1    Antaramian, A.2    Gilbert, S.3    Birnbaumer, M.4
  • 56
    • 0009603660 scopus 로고
    • An arginine residue conserved in most G protein-coupled receptors is essential for the function of the m1 muscarinic receptor
    • Zhu, S. Z., Wang, S. Z., Hu, J., and El-Fakahany, E. E. (1994) An arginine residue conserved in most G protein-coupled receptors is essential for the function of the m1 muscarinic receptor. Mol. Pharmacol. 45, 517-523
    • (1994) Mol. Pharmacol. , vol.45 , pp. 517-523
    • Zhu, S.Z.1    Wang, S.Z.2    Hu, J.3    El-Fakahany, E.E.4
  • 59
    • 0028276459 scopus 로고
    • A common step for signal transduction in G protein-coupled receptors
    • Oliveira, L., Paiva, A. C. M., Sander, C., and Vriend, G. (1994) A common step for signal transduction in G protein-coupled receptors. Trends Pharmacol. Sci. 15, 170-172
    • (1994) Trends Pharmacol. Sci. , vol.15 , pp. 170-172
    • Oliveira, L.1    Paiva, A.C.M.2    Sander, C.3    Vriend, G.4
  • 61
    • 0028061193 scopus 로고
    • A conserved carboxylic acid group mediates light-dependent proton uptake and signaling by rhodopsin
    • Arnis, S., Fahmy, K., Hofmann, K. P., and Sakmar, T. P. (1994) A conserved carboxylic acid group mediates light-dependent proton uptake and signaling by rhodopsin. J. Biol. Chem. 269, 23879-23881
    • (1994) J. Biol. Chem. , vol.269 , pp. 23879-23881
    • Arnis, S.1    Fahmy, K.2    Hofmann, K.P.3    Sakmar, T.P.4
  • 62
    • 0027298812 scopus 로고
    • Constitutive activation of opsin: Influence of charge at position 134 and size at position 296
    • Cohen, G. B., Yang, T., Robinson, P. R., and Oprian, D. D. (1993) Constitutive activation of opsin: influence of charge at position 134 and size at position 296. Biochemistry 32, 6111-6115
    • (1993) Biochemistry , vol.32 , pp. 6111-6115
    • Cohen, G.B.1    Yang, T.2    Robinson, P.R.3    Oprian, D.D.4
  • 63
    • 0027328071 scopus 로고
    • Charged amino acids required for signal transduction by the m3 muscarinic acetylcholine receptor
    • Kunkel, M. T., and Peralta E. G. (1993) Charged amino acids required for signal transduction by the m3 muscarinic acetylcholine receptor. EMBO J. 12, 3809-3815
    • (1993) EMBO J. , vol.12 , pp. 3809-3815
    • Kunkel, M.T.1    Peralta, E.G.2
  • 64
    • 0028944574 scopus 로고
    • Activating and inactivating mutations in N- and C-terminal i3 loop junctions of muscarinic acetylcholine Hm1 receptors
    • Högger, P., Shockley, M. S., Lameh, J., and Sadee, W. (1995) Activating and inactivating mutations in N-and C-terminal i3 loop junctions of muscarinic acetylcholine Hm1 receptors. J. Biol. Chem. 270, 7405-7410
    • (1995) J. Biol. Chem. , vol.270 , pp. 7405-7410
    • Högger, P.1    Shockley, M.S.2    Lameh, J.3    Sadee, W.4
  • 65
    • 0029789994 scopus 로고    scopus 로고
    • Molecular biology of muscarinic acetylcholine receptors
    • Wess J. (1996) Molecular biology of muscarinic acetylcholine receptors. Crit. Rev. Neurobiol. 10, 69-99
    • (1996) Crit. Rev. Neurobiol. , vol.10 , pp. 69-99
    • Wess, J.1
  • 66
    • 0027964847 scopus 로고
    • Insertion mutagenesis as a tool to predict the secondary structure of a muscarinic receptor domain determining specificity of G-protein coupling
    • Blüml, K., Mutschler, E., and Wess, J. (1994) Insertion mutagenesis as a tool to predict the secondary structure of a muscarinic receptor domain determining specificity of G-protein coupling. Proc. Natl. Acad. Sci. USA 91, 7980-7984
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 7980-7984
    • Blüml, K.1    Mutschler, E.2    Wess, J.3
  • 67
    • 0030039837 scopus 로고    scopus 로고
    • Structure of a G protein-coupling domain of a muscarinic receptor predicted by random saturation mutagenesis
    • Hill-Eubanks, D., Burstein, E. S., Spalding, T. A., Bräuner-Osborne, H., and Brann, M. R. (1996) Structure of a G protein-coupling domain of a muscarinic receptor predicted by random saturation mutagenesis. J. Biol. Chem. 271, 3058-3065
    • (1996) J. Biol. Chem. , vol.271 , pp. 3058-3065
    • Hill-Eubanks, D.1    Burstein, E.S.2    Spalding, T.A.3    Bräuner-Osborne, H.4    Brann, M.R.5
  • 68
    • 0028158607 scopus 로고
    • Identification of an intracellular tyrosine residue critical for muscarinic receptor-mediated stimulation of phosphatidyl inositol hydrolysis
    • Blüml, K., Mutschler, E., and Wess, J. (1994) Identification of an intracellular tyrosine residue critical for muscarinic receptor-mediated stimulation of phosphatidyl inositol hydrolysis. J. Biol. Chem. 269, 402-405
    • (1994) J. Biol. Chem. , vol.269 , pp. 402-405
    • Blüml, K.1    Mutschler, E.2    Wess, J.3
  • 69
    • 0028244065 scopus 로고
    • Functional role of a cytoplasmic aromatic amino acid in muscarinic receptor-mediated activation of phospholipase C
    • Blüml, K., Mutschler, E., and Wess, J. (1994) Functional role of a cytoplasmic aromatic amino acid in muscarinic receptor-mediated activation of phospholipase C. J. Biol. Chem. 269, 11537-11541
    • (1994) J. Biol. Chem. , vol.269 , pp. 11537-11541
    • Blüml, K.1    Mutschler, E.2    Wess, J.3
  • 70
    • 0028814543 scopus 로고
    • Structure-function of muscarinic receptor coupling to G proteins: Random saturation mutagenesis identifies a critical determinant of receptor affinity for G proteins
    • Burstein, E. S., Spalding, T. A., Hill-Eubanks, D., and Brann, M. R. (1995) Structure-function of muscarinic receptor coupling to G proteins: random saturation mutagenesis identifies a critical determinant of receptor affinity for G proteins. J. Biol. Chem. 270, 3141-3146
    • (1995) J. Biol. Chem. , vol.270 , pp. 3141-3146
    • Burstein, E.S.1    Spalding, T.A.2    Hill-Eubanks, D.3    Brann, M.R.4
  • 71
    • 0029589916 scopus 로고
    • Identification of a receptor/G-protein contact site critical for signalling specificity and G-protein activation
    • Liu, J., Conklin, B. R., Blin, N., Yun, J., and Wess, J. (1995) Identification of a receptor/G-protein contact site critical for signalling specificity and G-protein activation. Proc. Natl. Acad. Sci. USA 92, 11642-11646
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 11642-11646
    • Liu, J.1    Conklin, B.R.2    Blin, N.3    Yun, J.4    Wess, J.5
  • 73
    • 0029784196 scopus 로고    scopus 로고
    • The luteinizing hormone/chorionic gonadotropin receptor has distinct transmembrane conductors for cAMP and inositol phosphate signals
    • Gilchrist, R. L., Ryu, K.-S., Ji, I., and Ji, T. H. (1996) The luteinizing hormone/chorionic gonadotropin receptor has distinct transmembrane conductors for cAMP and inositol phosphate signals. J. Biol. Chem. 271, 19283-19287
    • (1996) J. Biol. Chem. , vol.271 , pp. 19283-19287
    • Gilchrist, R.L.1    Ryu, K.-S.2    Ji, I.3    Ji, T.H.4
  • 74
    • 0030049488 scopus 로고    scopus 로고
    • Constitutive activation of a single effector pathway: Evidence for multiple activation states of a G protein-coupled receptor
    • Perez, D. M., Hwa, J., Gaivin, R., Mathur, M., Brown, F., and Graham, R. M. (1996) Constitutive activation of a single effector pathway: evidence for multiple activation states of a G protein-coupled receptor. Mol. Pharmacol. 49, 112-122
    • (1996) Mol. Pharmacol. , vol.49 , pp. 112-122
    • Perez, D.M.1    Hwa, J.2    Gaivin, R.3    Mathur, M.4    Brown, F.5    Graham, R.M.6
  • 78
    • 0029145416 scopus 로고
    • Structural and functional relationships of heterotrimeric G-proteins
    • Rens-Domiano, S., and Hamm, H. E. (1995) Structural and functional relationships of heterotrimeric G-proteins. FASEB J. 9, 1059-1066
    • (1995) FASEB J. , vol.9 , pp. 1059-1066
    • Rens-Domiano, S.1    Hamm, H.E.2
  • 79
    • 0030987069 scopus 로고    scopus 로고
    • How receptors talk to trimeric G proteins
    • In press
    • Bourne, H. R. (1997) How receptors talk to trimeric G proteins. Curr. Opin. Cell Biol. In press
    • (1997) Curr. Opin. Cell Biol.
    • Bourne, H.R.1
  • 82
    • 0030064529 scopus 로고    scopus 로고
    • Receptor and membrane interaction sites on Gβ: A receptor-derived peptide binds to the carboxyl terminus
    • Taylor, J. M., Jacob-Mosier, G. G., Lawton, R. G., VanDort, M., and Neubig, R. R. (1996) Receptor and membrane interaction sites on Gβ: a receptor-derived peptide binds to the carboxyl terminus. J. Biol. Chem. 271, 3336-3339
    • (1996) J. Biol. Chem. , vol.271 , pp. 3336-3339
    • Taylor, J.M.1    Jacob-Mosier, G.G.2    Lawton, R.G.3    VanDort, M.4    Neubig, R.R.5
  • 83
    • 0030614427 scopus 로고    scopus 로고
    • Receptor and βγ binding sites in the α subunit of the retinal G protein transducin
    • Onrust, R., Herzniark, P., Chi, P., Garcia, P. D., Lichtarge, O., Kingsley, C., and Bourne, H. R. (1996) Receptor and βγ binding sites in the α subunit of the retinal G protein transducin. Science 275, 381-384
    • (1996) Science , vol.275 , pp. 381-384
    • Onrust, R.1    Herzniark, P.2    Chi, P.3    Garcia, P.D.4    Lichtarge, O.5    Kingsley, C.6    Bourne, H.R.7
  • 84
    • 0029969175 scopus 로고    scopus 로고
    • Interaction of transducin with light-activated rhodopsin protects it from proteolytic digestion by trypsin
    • Mazzoni, M. R., and Hamm, H. E. (1996) Interaction of transducin with light-activated rhodopsin protects it from proteolytic digestion by trypsin. J. Biol. Chem. 271, 30034-30040
    • (1996) J. Biol. Chem. , vol.271 , pp. 30034-30040
    • Mazzoni, M.R.1    Hamm, H.E.2
  • 86
    • 0023191072 scopus 로고
    • Identification of a family of muscarinic acetylcholine receptor genes
    • Bonner, T. I., Buckley, N. J., Young, A. C., and Brann, M. R. (1987) Identification of a family of muscarinic acetylcholine receptor genes. Science 237, 527-532
    • (1987) Science , vol.237 , pp. 527-532
    • Bonner, T.I.1    Buckley, N.J.2    Young, A.C.3    Brann, M.R.4
  • 87
    • 0030935667 scopus 로고    scopus 로고
    • Structural basis of receptor/G protein coupling selectivity studied with muscarinic receptors as model systems
    • Wess, J., Liu, J., Blin, B., Yun, J., Lerche, C., and Kostenis, E. (1997) Structural basis of receptor/G protein coupling selectivity studied with muscarinic receptors as model systems. Life Sci. 60, 1007-1014
    • (1997) Life Sci. , vol.60 , pp. 1007-1014
    • Wess, J.1    Liu, J.2    Blin, B.3    Yun, J.4    Lerche, C.5    Kostenis, E.6


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