메뉴 건너뛰기




Volumn 10, Issue 1, 1996, Pages 69-99

Molecular biology of muscarinic acetylcholine receptors

Author keywords

Ligand binding site; Mutagenesis; Receptor assembly; Receptor desensitization; Receptor phosphorylation; Receptor G protein coupling

Indexed keywords

CYCLIC AMP DEPENDENT PROTEIN KINASE; GUANINE NUCLEOTIDE BINDING PROTEIN; MUSCARINIC RECEPTOR; PROTEIN KINASE C; RECEPTOR SUBTYPE;

EID: 0029789994     PISSN: 08920915     EISSN: None     Source Type: Journal    
DOI: 10.1615/CritRevNeurobiol.v10.i1.40     Document Type: Review
Times cited : (439)

References (197)
  • 2
    • 0027208248 scopus 로고
    • Muscarinic receptors - Characterization, coupling and function
    • Caulfield, M. P., Muscarinic receptors - characterization, coupling and function, Pharmacol. Ther., 58, 319, 1993.
    • (1993) Pharmacol. Ther. , vol.58 , pp. 319
    • Caulfield, M.P.1
  • 6
    • 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., Identification of a family of muscarinic acetylcholine receptor genes, Science, 237, 527, 1987.
    • (1987) Science , vol.237 , pp. 527
    • Bonner, T.I.1    Buckley, N.J.2    Young, A.C.3    Brann, M.R.4
  • 8
    • 0023661365 scopus 로고
    • Distinct primary structures, ligand-binding properties and tissue-specific expression of four human muscarinic acetylcholine receptors
    • Peralta, E. G., Ashkenazi, A., Winslow, J. W., Smith, D. H., Ramachandran, J., and Capon, D. J., Distinct primary structures, ligand-binding properties and tissue-specific expression of four human muscarinic acetylcholine receptors, EMBO J., 6, 3923, 1987.
    • (1987) EMBO J. , vol.6 , pp. 3923
    • Peralta, E.G.1    Ashkenazi, A.2    Winslow, J.W.3    Smith, D.H.4    Ramachandran, J.5    Capon, D.J.6
  • 9
    • 0024039146 scopus 로고
    • Cloning and expression of the human and rat m5 muscarinic acetylcholine receptor genes
    • Bonner, T. I., Young, A. C., Brann, M. R., and Buckley, N. J., Cloning and expression of the human and rat m5 muscarinic acetylcholine receptor genes, Neuron, 1, 403, 1988.
    • (1988) Neuron , vol.1 , pp. 403
    • Bonner, T.I.1    Young, A.C.2    Brann, M.R.3    Buckley, N.J.4
  • 10
    • 0025359654 scopus 로고
    • Cloning and functional analysis of a gene encoding a novel muscarinic acetylcholine receptor expressed in chick heart and brain
    • Tietje, K. M., Goldman, P. S., and Nathanson, N. M., Cloning and functional analysis of a gene encoding a novel muscarinic acetylcholine receptor expressed in chick heart and brain, J. Biol. Chem., 265, 2828, 1990.
    • (1990) J. Biol. Chem. , vol.265 , pp. 2828
    • Tietje, K.M.1    Goldman, P.S.2    Nathanson, N.M.3
  • 11
    • 0026014153 scopus 로고
    • Embryonic chick heart expresses multiple muscarinic acetylcholine receptor subtypes
    • Tietje, K. M. and Nathanson, N. M., Embryonic chick heart expresses multiple muscarinic acetylcholine receptor subtypes, J. Biol. Chem., 266, 17382, 1991.
    • (1991) J. Biol. Chem. , vol.266 , pp. 17382
    • Tietje, K.M.1    Nathanson, N.M.2
  • 12
    • 0028172117 scopus 로고
    • 3 muscarinic acetylcholine receptor is expressed in chick atrium and ventricle
    • 3 muscarinic acetylcholine receptor is expressed in chick atrium and ventricle, J. Biol. Chem., 269, 25823, 1994.
    • (1994) J. Biol. Chem. , vol.269 , pp. 25823
    • Gadbut, A.P.1    Galper, J.B.2
  • 13
    • 0024391090 scopus 로고
    • Characterization and functional expression in mammalian cells of genomic and cDNA clones encoding a Drosophila muscarinic acetylcholine receptor
    • Shapiro, R. A., Wakimoto, B. T., Subers, E. M., and Nathanson, N. M., Characterization and functional expression in mammalian cells of genomic and cDNA clones encoding a Drosophila muscarinic acetylcholine receptor, Proc. Natl. Acad. Sci. U.S.A., 86, 9039, 1989.
    • (1989) Proc. Natl. Acad. Sci. U.S.A. , vol.86 , pp. 9039
    • Shapiro, R.A.1    Wakimoto, B.T.2    Subers, E.M.3    Nathanson, N.M.4
  • 14
    • 0028124243 scopus 로고
    • Cloning of a Xenopus laevis muscarinic receptor encoded by an intronless gene
    • Herrera, L., Carvallo, P., Antonelli, M., and Olate, J., Cloning of a Xenopus laevis muscarinic receptor encoded by an intronless gene, FEBS Lett., 352, 175, 1994.
    • (1994) FEBS Lett. , vol.352 , pp. 175
    • Herrera, L.1    Carvallo, P.2    Antonelli, M.3    Olate, J.4
  • 15
    • 0027465882 scopus 로고
    • Immunological localization of muscarinic acetylcholine receptors in peripheral tissues and brain
    • Levey, A. I., Immunological localization of muscarinic acetylcholine receptors in peripheral tissues and brain, Life Sci., 52, 441, 1993.
    • (1993) Life Sci. , vol.52 , pp. 441
    • Levey, A.I.1
  • 16
    • 0029042321 scopus 로고
    • Expression of m1-m4 muscarinic acetylcholine receptor proteins in rat hippocampus and regulation by cholinergic innervation
    • Levey, A. I., Edmunds, S. M., Koliatsos, V., Wiley, R. G., and Heilman, C. J., Expression of m1-m4 muscarinic acetylcholine receptor proteins in rat hippocampus and regulation by cholinergic innervation, J. Neurosci., 15, 4077, 1995.
    • (1995) J. Neurosci. , vol.15 , pp. 4077
    • Levey, A.I.1    Edmunds, S.M.2    Koliatsos, V.3    Wiley, R.G.4    Heilman, C.J.5
  • 17
    • 0028222025 scopus 로고
    • Distribution of m1-m4 muscarinic receptor proteins in the rat striatum: Light and electron microscopic immunocytochemistry using subtype-specific antibodies
    • Hersch, S. M., Gutekunst, C.-A., Rees, H. D., Heilman, C. J., and Levey, A. I., Distribution of m1-m4 muscarinic receptor proteins in the rat striatum: light and electron microscopic immunocytochemistry using subtype-specific antibodies, J. Neurosci., 14, 3351, 1994.
    • (1994) J. Neurosci. , vol.14 , pp. 3351
    • Hersch, S.M.1    Gutekunst, C.-A.2    Rees, H.D.3    Heilman, C.J.4    Levey, A.I.5
  • 18
    • 0025943814 scopus 로고
    • Identification and localization of muscarinic acetylcholine receptor proteins in brain with subtype-specific antibodies
    • Levey, A. I., Kitt, C. A., Simonds, W. F., Price, D. L., and Brann, M. R., Identification and localization of muscarinic acetylcholine receptor proteins in brain with subtype-specific antibodies, J. Neurosci., 11, 3218, 1991.
    • (1991) J. Neurosci. , vol.11 , pp. 3218
    • Levey, A.I.1    Kitt, C.A.2    Simonds, W.F.3    Price, D.L.4    Brann, M.R.5
  • 19
    • 0027328091 scopus 로고
    • Molecular basis of muscarinic acetylcholine receptor function
    • Wess, J., Molecular basis of muscarinic acetylcholine receptor function, Trends Pharmacol. Sci., 14, 308, 1993.
    • (1993) Trends Pharmacol. Sci. , vol.14 , pp. 308
    • Wess, J.1
  • 20
    • 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., Model systems for the study of seven-transmembrane-segment receptors, Annu. Rev. Biochem., 60, 653, 1991.
    • (1991) Annu. Rev. Biochem. , vol.60 , pp. 653
    • Dohlman, H.G.1    Thorner, J.2    Caron, M.G.3    Lefkowitz, R.J.4
  • 21
    • 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., In vitro mutagenesis and the search for structure-function relationships among G protein-coupled receptors, Biochem. J., 283, 1, 1992.
    • (1992) Biochem. J. , vol.283 , pp. 1
    • Savarese, T.M.1    Fraser, C.M.2
  • 23
    • 0027495684 scopus 로고
    • New roles for G-protein βγ-dimers in transmembrane signalling
    • Clapham, D. E. and Neer, E. J., New roles for G-protein βγ-dimers in transmembrane signalling, Nature, 365, 403, 1993.
    • (1993) Nature , vol.365 , pp. 403
    • Clapham, D.E.1    Neer, E.J.2
  • 24
    • 0025642826 scopus 로고
    • Site-directed mutagenesis of the m2 muscarinic acetylcholine receptor: Analysis of the role of N-glycosylation in receptor expression and function
    • Van Koppen, C. J. and Nathanson, N. M., Site-directed mutagenesis of the m2 muscarinic acetylcholine receptor: analysis of the role of N-glycosylation in receptor expression and function, J. Biol. Chem., 265, 20887, 1990.
    • (1990) J. Biol. Chem. , vol.265 , pp. 20887
    • Van Koppen, C.J.1    Nathanson, N.M.2
  • 26
    • 0025121206 scopus 로고
    • Muscarinic acetylcholine receptors: Peptide sequencing identifies residues involved in antagonist binding and disulfide bond formation
    • Kurtenbach, E., Curtis, C. A. M., Pedder, E. K., Aitken, A., Harris, A. C. M., and Hulme, E. C., Muscarinic acetylcholine receptors: peptide sequencing identifies residues involved in antagonist binding and disulfide bond formation, J. Biol. Chem., 265, 13702, 1990.
    • (1990) J. Biol. Chem. , vol.265 , pp. 13702
    • Kurtenbach, E.1    Curtis, C.A.M.2    Pedder, E.K.3    Aitken, A.4    Harris, A.C.M.5    Hulme, E.C.6
  • 27
    • 0026639831 scopus 로고
    • Site-directed mutagenesis of the rat m1 muscarinic acetylcholine receptor: Role of conserved cysteines in receptor function
    • Savarese, T. M., Wang, C.-D., and Fraser, C. M., Site-directed mutagenesis of the rat m1 muscarinic acetylcholine receptor: role of conserved cysteines in receptor function, J. Biol. Chem., 267, 11439, 1992.
    • (1992) J. Biol. Chem. , vol.267 , pp. 11439
    • Savarese, T.M.1    Wang, C.-D.2    Fraser, C.M.3
  • 28
    • 0023859049 scopus 로고
    • Two adjacent cysteine residues in the C-terminal cytoplasmic fragment of bovine rhodopsin are palmitoylated
    • Ovchinnikov, Y. A., Abdulaev, N. G., and Bogachuk, A. S., Two adjacent cysteine residues in the C-terminal cytoplasmic fragment of bovine rhodopsin are palmitoylated, FEBS Lett., 230, 1, 1988.
    • (1988) FEBS Lett. , vol.230 , pp. 1
    • Ovchinnikov, Y.A.1    Abdulaev, N.G.2    Bogachuk, A.S.3
  • 29
    • 0024544232 scopus 로고
    • Palmitoylation of the human β2-adrenergic receptor: Mutation of Cys341 in the carboxyl tail leads to an uncoupled nonpalmitoylated form of the receptor
    • O'Dowd, B. F., Hnatowich, M., Caron, M. G., Lefkowitz, R. J., and Bouvier, M., Palmitoylation of the human β2-adrenergic receptor: mutation of Cys341 in the carboxyl tail leads to an uncoupled nonpalmitoylated form of the receptor, J. Biol. Chem., 264, 7564, 1989.
    • (1989) J. Biol. Chem. , vol.264 , pp. 7564
    • O'Dowd, B.F.1    Hnatowich, M.2    Caron, M.G.3    Lefkowitz, R.J.4    Bouvier, M.5
  • 30
    • 0025790292 scopus 로고
    • The cysteine residue in the carboxyl-terminal domain of the m2 muscarinic acetylcholine receptor is not required for receptor-mediated inhibition of adenylate cyclase
    • Van Koppen, C. J. and Nathanson, N. M., The cysteine residue in the carboxyl-terminal domain of the m2 muscarinic acetylcholine receptor is not required for receptor-mediated inhibition of adenylate cyclase, J. Neurochem., 57, 1873, 1991.
    • (1991) J. Neurochem. , vol.57 , pp. 1873
    • Van Koppen, C.J.1    Nathanson, N.M.2
  • 31
    • 0027388977 scopus 로고
    • Muscarinic receptor subtypes: Modulation of ion channels
    • Jones, S. V. P., Muscarinic receptor subtypes: modulation of ion channels, Life Sci., 52, 457, 1993.
    • (1993) Life Sci. , vol.52 , pp. 457
    • Jones, S.V.P.1
  • 32
    • 0029013930 scopus 로고
    • Muscarinic acetylcholine receptors: signal transduction through multiple effectors
    • Felder, C. C., Muscarinic acetylcholine receptors: signal transduction through multiple effectors, FASEB J., 9, 619, 1995.
    • (1995) FASEB J. , vol.9 , pp. 619
    • Felder, C.C.1
  • 33
    • 0027506471 scopus 로고
    • The probable arrangement of the helices in G protein-coupled receptors
    • Baldwin, J. M., The probable arrangement of the helices in G protein-coupled receptors, EMBO J., 12, 1693, 1993.
    • (1993) EMBO J. , vol.12 , pp. 1693
    • Baldwin, J.M.1
  • 34
    • 0028227013 scopus 로고
    • Structure and function of receptors coupled to G proteins
    • Baldwin, J. M., Structure and function of receptors coupled to G proteins, Curr. Opin. Cell Biol., 6, 180, 1994.
    • (1994) Curr. Opin. Cell Biol. , vol.6 , pp. 180
    • Baldwin, J.M.1
  • 35
    • 0027933763 scopus 로고
    • Locating ligand-binding sites in 7TM receptors by protein engineering
    • Schwartz, T. W., Locating ligand-binding sites in 7TM receptors by protein engineering, Curr. Opin. Biotechnol., 5, 434, 1994.
    • (1994) Curr. Opin. Biotechnol. , vol.5 , pp. 434
    • Schwartz, T.W.1
  • 36
  • 37
    • 0027496941 scopus 로고
    • Mutational analysis of muscarinic acetylcholine receptors: Structural basis of ligand/receptor/ G protein interactions
    • Wess, J., Mutational analysis of muscarinic acetylcholine receptors: Structural basis of ligand/receptor/ G protein interactions, Life Sci., 53, 1447, 1993.
    • (1993) Life Sci. , vol.53 , pp. 1447
    • Wess, J.1
  • 38
    • 0026592867 scopus 로고
    • Identification of intramolecular interactions in adrenergic receptors
    • Suryanarayana, S., von Zastrow, M., and Kobilka, B. K., Identification of intramolecular interactions in adrenergic receptors, J. Biol. Chem., 267, 21991, 1992.
    • (1992) J. Biol. Chem. , vol.267 , pp. 21991
    • Suryanarayana, S.1    Von Zastrow, M.2    Kobilka, B.K.3
  • 39
    • 0028012105 scopus 로고
    • Intramolecular interactions in muscarinic acetylcholine receptors studied with chimeric m2/m5 receptors
    • Pittel, Z. and Wess, J., Intramolecular interactions in muscarinic acetylcholine receptors studied with chimeric m2/m5 receptors, Mol. Pharmacol., 45, 61, 1994.
    • (1994) Mol. Pharmacol. , vol.45 , pp. 61
    • Pittel, Z.1    Wess, J.2
  • 41
    • 0028125886 scopus 로고
    • Rhodopsin mutation G90D and a molecular mechanism for congenital night blindness
    • Rao, V. R., Cohen, G. B., and Oprian, D. D., Rhodopsin mutation G90D and a molecular mechanism for congenital night blindness, Nature, 367, 639, 1994.
    • (1994) Nature , vol.367 , pp. 639
    • Rao, V.R.1    Cohen, G.B.2    Oprian, D.D.3
  • 42
    • 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., Conversion of antagonist-binding site to metal-ion site in the tachykinin NK-1 receptor, Nature, 374, 74, 1995.
    • (1995) Nature , vol.374 , pp. 74
    • Elling, C.E.1    Nielsen, S.M.2    Schwartz, T.W.3
  • 43
    • 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., Mutational analysis of the relative orientation of transmembrane helices I and VII in G protein-coupled receptors, J. Biol. Chem., 270, 19532, 1995.
    • (1995) J. Biol. Chem. , vol.270 , pp. 19532
    • Liu, J.1    Schöneberg, T.2    Van Rhee, M.3    Wess, J.4
  • 45
    • 0027533276 scopus 로고
    • Reconstitution of functional muscarinic receptors by coexpression of amino and carboxyl terminal receptor fragments
    • Maggio, R., Vogel, Z., and Wess, J., Reconstitution of functional muscarinic receptors by coexpression of amino and carboxyl terminal receptor fragments, FEBS Lett., 319, 195, 1993.
    • (1993) FEBS Lett. , vol.319 , pp. 195
    • Maggio, R.1    Vogel, Z.2    Wess, J.3
  • 46
    • 0027467848 scopus 로고
    • Coexpression studies with mutant muscarinic/adrenergic receptors provide evidence for intermolecular crosstalk between G protein-linked receptors
    • Maggio, R., Vogel, Z., and Wess, J., Coexpression studies with mutant muscarinic/adrenergic receptors provide evidence for intermolecular crosstalk between G protein-linked receptors, Proc. Natl. Acad. Sci. U.S.A., 90, 3103, 1993.
    • (1993) Proc. Natl. Acad. Sci. U.S.A. , vol.90 , pp. 3103
    • Maggio, R.1    Vogel, Z.2    Wess, J.3
  • 47
    • 0028931922 scopus 로고
    • In vivo assembly of rhodopsin from expressed polypeptide fragments
    • Ridge, K. D., Lee, S. S. J., and Yao, L. L., In vivo assembly of rhodopsin from expressed polypeptide fragments, Proc. Natl. Acad. Sci. U.S.A., 92, 3204, 1995.
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 3204
    • Ridge, K.D.1    Lee, S.S.J.2    Yao, L.L.3
  • 48
    • 0029077235 scopus 로고
    • Plasma membrane localization and functional rescue of truncated forms of a G protein-coupled receptor
    • Schöneberg, T., Liu, J., and Wess, J., Plasma membrane localization and functional rescue of truncated forms of a G protein-coupled receptor, J. Biol. Chem., 270, 18000, 1995.
    • (1995) J. Biol. Chem. , vol.270 , pp. 18000
    • Schöneberg, T.1    Liu, J.2    Wess, J.3
  • 49
    • 0025249842 scopus 로고
    • Membrane protein folding and oligomerization: The two-stage model
    • Popot, J.-L. and Engelman, D. M., Membrane protein folding and oligomerization: the two-stage model, Biochemistry, 29, 4031, 1990.
    • (1990) Biochemistry , vol.29 , pp. 4031
    • Popot, J.-L.1    Engelman, D.M.2
  • 50
    • 0024847889 scopus 로고
    • Site-directed mutagenesis of m1 muscarinic acetylcholine receptors: Conserved aspartic acids play important roles in receptor function
    • Fraser, C. M., Wang, C.-D., Robinson, D. A., Gocayne, J. D., and Venter, J. C., Site-directed mutagenesis of m1 muscarinic acetylcholine receptors: conserved aspartic acids play important roles in receptor function, Mol. Pharmacol., 36, 840, 1989.
    • (1989) Mol. Pharmacol. , vol.36 , pp. 840
    • Fraser, C.M.1    Wang, C.-D.2    Robinson, D.A.3    Gocayne, J.D.4    Venter, J.C.5
  • 52
    • 0028087860 scopus 로고
    • Acetylcholine mustard labels the binding site aspartate in muscarinic acetylcholine receptors
    • Spalding, T. A., Birdsall, N. J. M., Curtis, C. A. M., and Hulme, E. C., Acetylcholine mustard labels the binding site aspartate in muscarinic acetylcholine receptors, J. Biol. Chem., 269, 4092, 1994.
    • (1994) J. Biol. Chem. , vol.269 , pp. 4092
    • Spalding, T.A.1    Birdsall, N.J.M.2    Curtis, C.A.M.3    Hulme, E.C.4
  • 53
    • 0028927705 scopus 로고
    • The role of charge interactions in muscarinic agonist binding, and receptor-response coupling
    • Huhne, E. C., Curtis, C. A. M., Page, K. M., and Jones, P. G., The role of charge interactions in muscarinic agonist binding, and receptor-response coupling, Life Sci., 56, 891, 1995.
    • (1995) Life Sci. , vol.56 , pp. 891
    • Huhne, E.C.1    Curtis, C.A.M.2    Page, K.M.3    Jones, P.G.4
  • 54
    • 0028907039 scopus 로고
    • Mutations of aspartate 103 in the Hm2 receptor and alterations in receptor binding properties of muscarinic agonists
    • Schwarz, R. D., Spencer, J. C., Jaen, C. J., Mirzadegan, T., Moreland, D., Tecle, H., and Thomas, A. J., Mutations of aspartate 103 in the Hm2 receptor and alterations in receptor binding properties of muscarinic agonists, Life. Sci., 56, 923, 1995.
    • (1995) Life. Sci. , vol.56 , pp. 923
    • Schwarz, R.D.1    Spencer, J.C.2    Jaen, C.J.3    Mirzadegan, T.4    Moreland, D.5    Tecle, H.6    Thomas, A.J.7
  • 55
    • 0026040728 scopus 로고
    • Site-directed mutagenesis of the m3 muscarinic receptor: Identification of a series of threonine and tyrosine residues involved in agonist but not antagonist binding
    • Wess, J., Gdula, D., and Brann, M. R., Site-directed mutagenesis of the m3 muscarinic receptor: identification of a series of threonine and tyrosine residues involved in agonist but not antagonist binding, EMBO J., 10, 3729, 1991.
    • (1991) EMBO J. , vol.10 , pp. 3729
    • Wess, J.1    Gdula, D.2    Brann, M.R.3
  • 56
    • 0026701973 scopus 로고
    • Role of conserved threonine and tyrosine residues in acetylcholine binding and muscarinic receptor activation: A study with m3 muscarinic receptor point mutants
    • Wess, J., Maggio, R., Palmer, J. R., and Vogel, Z., Role of conserved threonine and tyrosine residues in acetylcholine binding and muscarinic receptor activation: a study with m3 muscarinic receptor point mutants, J. Biol. Chem., 267, 19313, 1992.
    • (1992) J. Biol. Chem. , vol.267 , pp. 19313
    • Wess, J.1    Maggio, R.2    Palmer, J.R.3    Vogel, Z.4
  • 57
    • 0028815463 scopus 로고
    • Probing of the location of the allosteric site on m1 muscarinic receptors by site-directed mutagenesis
    • Matsui, H., Lazareno, S., and Birdsall, N. J. M., Probing of the location of the allosteric site on m1 muscarinic receptors by site-directed mutagenesis, Mol. Pharmacol., 47, 88, 1995.
    • (1995) Mol. Pharmacol. , vol.47 , pp. 88
    • Matsui, H.1    Lazareno, S.2    Birdsall, N.J.M.3
  • 58
    • 0027533339 scopus 로고
    • Functional role of proline and tryptophan residues highly conserved among G protein-coupled receptors studied by mutational analysis of the m3 muscarinic receptor
    • Wess, J., Nanavati, S., Vogel, Z., and Maggio, R., Functional role of proline and tryptophan residues highly conserved among G protein-coupled receptors studied by mutational analysis of the m3 muscarinic receptor, EMBO J., 12, 331, 1993.
    • (1993) EMBO J. , vol.12 , pp. 331
    • Wess, J.1    Nanavati, S.2    Vogel, Z.3    Maggio, R.4
  • 59
    • 0025881062 scopus 로고
    • Three-dimensional models of neurotransmitter G-binding protein-coupled receptors
    • Hibert, M. F., Trumpp-Kallmeyer, S., Bruinvels, A., and Hoflack, J., Three-dimensional models of neurotransmitter G-binding protein-coupled receptors, Mol. Pharmacol., 40, 8, 1991.
    • (1991) Mol. Pharmacol. , vol.40 , pp. 8
    • Hibert, M.F.1    Trumpp-Kallmeyer, S.2    Bruinvels, A.3    Hoflack, J.4
  • 60
    • 0026660322 scopus 로고
    • Modeling of G-protein-coupled receptors: Application to dopamine, adrenaline, acetylcholine, and mammalian opsin receptors
    • Trumpp-Kallmeyer, S., Hoflack, J., Bruinvels, A., and Hibert, M., Modeling of G-protein-coupled receptors: application to dopamine, adrenaline, acetylcholine, and mammalian opsin receptors, J. Med. Chem., 35, 3448, 1992.
    • (1992) J. Med. Chem. , vol.35 , pp. 3448
    • Trumpp-Kallmeyer, S.1    Hoflack, J.2    Bruinvels, A.3    Hibert, M.4
  • 62
    • 0023053742 scopus 로고
    • Phosphocholine binding immunoglobulin Fab McPC603: An X-ray diffraction study at 2.7 Å
    • Satow, Y., Cohen, G.H., Padlan, E.A., and Davies, D., Phosphocholine binding immunoglobulin Fab McPC603: an X-ray diffraction study at 2.7 Å, J. Mol. Biol., 190, 593, 1986.
    • (1986) J. Mol. Biol. , vol.190 , pp. 593
    • Satow, Y.1    Cohen, G.H.2    Padlan, E.A.3    Davies, D.4
  • 63
    • 0025778840 scopus 로고
    • Atomic structure of acetylcholinesterase from Torpedo californica: A prototypic acetylcholine binding protein
    • Sussman, J. L., Harel, M., Frolow, F., Oefner, C., Goldman, A., Toker, L., and Silman, I., Atomic structure of acetylcholinesterase from Torpedo californica: a prototypic acetylcholine binding protein, Science, 253, 872, 1991.
    • (1991) Science , vol.253 , pp. 872
    • Sussman, J.L.1    Harel, M.2    Frolow, F.3    Oefner, C.4    Goldman, A.5    Toker, L.6    Silman, I.7
  • 64
    • 0025292355 scopus 로고
    • Model of the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy
    • Henderson, R., Baldwin, J. M., Ceska, T. A., Zemlin, F., Beckmann, E., and Downing, K. H., Model of the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy, J. Mol. Biol., 213, 899, 1990.
    • (1990) J. Mol. Biol. , vol.213 , pp. 899
    • Henderson, R.1    Baldwin, J.M.2    Ceska, T.A.3    Zemlin, F.4    Beckmann, E.5    Downing, K.H.6
  • 65
    • 0027278101 scopus 로고
    • Binding-site modeling of the muscarinic m1 receptor: A combination of homology-based and indirect approaches
    • Nordvall, G. and Hacksell, U., Binding-site modeling of the muscarinic m1 receptor: a combination of homology-based and indirect approaches, J. Med. Chem., 36, 967, 1993.
    • (1993) J. Med. Chem. , vol.36 , pp. 967
    • Nordvall, G.1    Hacksell, U.2
  • 66
    • 0028291618 scopus 로고
    • Functional role in ligand binding and receptor activation of an asparagine residue present in the sixth transmembrane domain of all muscarinic acetylcholine receptors
    • Blüml, K., Mutschler, E., and Wess, J., Functional role in ligand binding and receptor activation of an asparagine residue present in the sixth transmembrane domain of all muscarinic acetylcholine receptors, J. Biol. Chem., 269, 18870, 1994.
    • (1994) J. Biol. Chem. , vol.269 , pp. 18870
    • Blüml, K.1    Mutschler, E.2    Wess, J.3
  • 67
    • 0003799357 scopus 로고
    • Anticholinergics: Antispasmodic and antiulcer drugs. Cholinergics
    • Wolff, M. E., Ed., John Wiley & Sons, New York
    • Rama Sastry, B. V., Anticholinergics: antispasmodic and antiulcer drugs. Cholinergics, in Burger's Medicinal Chemistry, 4th ed, Wolff, M. E., Ed., John Wiley & Sons, New York, 1981, 361.
    • (1981) Burger's Medicinal Chemistry, 4th Ed , pp. 361
    • Rama Sastry, B.V.1
  • 68
    • 0025153423 scopus 로고
    • Delineation of muscarinic receptor selectivity of coupling to guanine-nucleotide binding proteins and second messengers
    • Wess, J., Bonner, T. I., Dörje, F., and Bonner, T. I., Delineation of muscarinic receptor selectivity of coupling to guanine-nucleotide binding proteins and second messengers, Mol. Pharmacol., 38, 517, 1990.
    • (1990) Mol. Pharmacol. , vol.38 , pp. 517
    • Wess, J.1    Bonner, T.I.2    Dörje, F.3    Bonner, T.I.4
  • 69
    • 0028103917 scopus 로고
    • 3 receptor: Chimeric receptors delineate a role for intracellular domains
    • 3 receptor: chimeric receptors delineate a role for intracellular domains, Mol. Pharmacol., 46, 352, 1994.
    • (1994) Mol. Pharmacol. , vol.46 , pp. 352
    • Robinson, S.W.1    Jarvie, K.R.2    Caron, M.G.3
  • 70
    • 0023916293 scopus 로고
    • Muscarinic receptor differentiation
    • Mitchelson, F., Muscarinic receptor differentiation, Pharmacol. Ther., 37, 357, 1988.
    • (1988) Pharmacol. Ther. , vol.37 , pp. 357
    • Mitchelson, F.1
  • 71
    • 0024507616 scopus 로고
    • Antagonist binding properties of five cloned muscarinic receptors expressed in CHO-K1 cells
    • Buckley, N. J., Bonner, T. I., Buckley, C. M., and Brann, M. R., Antagonist binding properties of five cloned muscarinic receptors expressed in CHO-K1 cells, Mol. Pharmacol., 35, 469, 1989.
    • (1989) Mol. Pharmacol. , vol.35 , pp. 469
    • Buckley, N.J.1    Bonner, T.I.2    Buckley, C.M.3    Brann, M.R.4
  • 73
    • 0026612960 scopus 로고
    • Chimeric M1/M2 muscarinic receptors: Correlation of ligand selectivity and functional coupling with structural modifications
    • Lai, J., Nunan, L., Waite, S. L., Ma, S.-W., Bloom, J. W., Roeske, W. R., and Yamamura, H. I., Chimeric M1/M2 muscarinic receptors: correlation of ligand selectivity and functional coupling with structural modifications, J. Pharmacol. Exp. Ther., 262, 173, 1992.
    • (1992) J. Pharmacol. Exp. Ther. , vol.262 , pp. 173
    • Lai, J.1    Nunan, L.2    Waite, S.L.3    Ma, S.-W.4    Bloom, J.W.5    Roeske, W.R.6    Yamamura, H.I.7
  • 74
    • 0025675412 scopus 로고
    • Chimeric m2/m3 muscarinic receptors: Role of carboxyl terminal receptor domains in selectivity of ligand binding and coupling to phosphoinositide hydrolysis
    • Wess, J., Bonner, T. I., and Brann, M. R., Chimeric m2/m3 muscarinic receptors: role of carboxyl terminal receptor domains in selectivity of ligand binding and coupling to phosphoinositide hydrolysis, Mol. Pharmacol., 38, 872, 1990.
    • (1990) Mol. Pharmacol. , vol.38 , pp. 872
    • Wess, J.1    Bonner, T.I.2    Brann, M.R.3
  • 75
    • 0026517079 scopus 로고
    • Structural basis of the subtype-selectivity of muscarinic antagonists: A study with chimeric m2/m5 muscarinic receptors
    • Wess, J., Gdula, D., and Brann, M. R., Structural basis of the subtype-selectivity of muscarinic antagonists: a study with chimeric m2/m5 muscarinic receptors, Mol. Pharmacol., 41, 369, 1992.
    • (1992) Mol. Pharmacol. , vol.41 , pp. 369
    • Wess, J.1    Gdula, D.2    Brann, M.R.3
  • 76
    • 0029055030 scopus 로고
    • Allosteric modulation of muscarinic acetylcholine receptors
    • Tucek, S. and Proska, J., Allosteric modulation of muscarinic acetylcholine receptors, Trends Pharmacol. Sci., 16, 205, 1995.
    • (1995) Trends Pharmacol. Sci. , vol.16 , pp. 205
    • Tucek, S.1    Proska, J.2
  • 77
    • 0026005728 scopus 로고
    • Allosteric regulation of cloned m1-m5 muscarinic receptor subtypes
    • Ellis, J., Huyler, J., and Brann, M. R., Allosteric regulation of cloned m1-m5 muscarinic receptor subtypes, Biochem. Pharmacol., 42, 1927, 1991.
    • (1991) Biochem. Pharmacol. , vol.42 , pp. 1927
    • Ellis, J.1    Huyler, J.2    Brann, M.R.3
  • 78
    • 0027172276 scopus 로고
    • Use of chimeric muscarinic receptors to investigate epitopes involved in allosteric interactions
    • Ellis, J., Seidenberg, M., and Brann, M. R., Use of chimeric muscarinic receptors to investigate epitopes involved in allosteric interactions, Mol. Pharmacol., 44, 583, 1993.
    • (1993) Mol. Pharmacol. , vol.44 , pp. 583
    • Ellis, J.1    Seidenberg, M.2    Brann, M.R.3
  • 79
    • 0028241381 scopus 로고
    • Role of acidic amino acids in the allosteric modulation by gallamine of antagonist binding at the m2 muscarinic acetylcholine receptor
    • Leppik, R. A., Miller R. C., Eck, M., and Paquet, J.-L., Role of acidic amino acids in the allosteric modulation by gallamine of antagonist binding at the m2 muscarinic acetylcholine receptor, Mol. Pharmacol., 45, 983, 1994.
    • (1994) Mol. Pharmacol. , vol.45 , pp. 983
    • Leppik, R.A.1    Miller, R.C.2    Eck, M.3    Paquet, J.-L.4
  • 80
    • 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., An arginine residue conserved in most G protein-coupled receptors is essential for the function of the m1 muscarinic receptor, Mol. Pharmacol., 45, 517, 1994.
    • (1994) Mol. Pharmacol. , vol.45 , pp. 517
    • Zhu, S.Z.1    Wang, S.Z.2    Hu, J.3    El-Fakahany, E.E.4
  • 84
    • 0028361809 scopus 로고
    • Chimeric muscarinic cholinergic: β-adrenergic receptors that are functionally promiscuous among G proteins
    • Wong, S. K.-F. and Ross, E. M., Chimeric muscarinic cholinergic: β-adrenergic receptors that are functionally promiscuous among G proteins, J. Biol. Chem., 269, 18968, 1994.
    • (1994) J. Biol. Chem. , vol.269 , pp. 18968
    • Wong, S.K.-F.1    Ross, E.M.2
  • 86
    • 0023773004 scopus 로고
    • Differential regulation of PI hydrolysis and adenylyl cyclase by muscarinic receptor subtypes
    • Peralta, E. G., Ashkenazi, A., Winslow, J. W., Ramachandran, J., and Capon, D. J., Differential regulation of PI hydrolysis and adenylyl cyclase by muscarinic receptor subtypes, Nature, 334, 434, 1988.
    • (1988) Nature , vol.334 , pp. 434
    • Peralta, E.G.1    Ashkenazi, A.2    Winslow, J.W.3    Ramachandran, J.4    Capon, D.J.5
  • 87
    • 0026086012 scopus 로고
    • Reconstitutively active G protein-coupled receptors purified from baculovirus-infected insect cells
    • Parker, E. M., Kameyama, K., Higashijima, T., and Ross, E. M., Reconstitutively active G protein-coupled receptors purified from baculovirus-infected insect cells, J. Biol. Chem., 266, 519, 1991.
    • (1991) J. Biol. Chem. , vol.266 , pp. 519
    • Parker, E.M.1    Kameyama, K.2    Higashijima, T.3    Ross, E.M.4
  • 89
    • 0028305892 scopus 로고
    • Differential regulation of cAMP-mediated gene transcription by m1 and m4 muscarinic acetylcholine receptors
    • Migeon, J. C. and Nathanson, N. M., Differential regulation of cAMP-mediated gene transcription by m1 and m4 muscarinic acetylcholine receptors, J. Biol. Chem., 269, 9767, 1994.
    • (1994) J. Biol. Chem. , vol.269 , pp. 9767
    • Migeon, J.C.1    Nathanson, N.M.2
  • 90
    • 0027976926 scopus 로고
    • A novel mechanism for coupling of m4 muscarinic acetylcholine receptors to calmodulin-sensitive adenylyl cyclase: Crossover from G protein-coupled inhibition to stimulation
    • Dittman, A. H., Weber, J. P., Hinds, T. R., Choi, E.-J., Migeon, J. C., Nathanson, N. M., and Storm, D. R., A novel mechanism for coupling of m4 muscarinic acetylcholine receptors to calmodulin-sensitive adenylyl cyclase: crossover from G protein-coupled inhibition to stimulation, Biochemistry, 33, 943, 1994.
    • (1994) Biochemistry , vol.33 , pp. 943
    • Dittman, A.H.1    Weber, J.P.2    Hinds, T.R.3    Choi, E.-J.4    Migeon, J.C.5    Nathanson, N.M.6    Storm, D.R.7
  • 91
    • 0025880464 scopus 로고
    • Assignment of G-protein subtypes to specific receptors inducing inhibition of calcium currents
    • Kleuss, C., Hescheler, J., Ewel, C., Rosenthal, W., Schultz, G., and Wittig, B., Assignment of G-protein subtypes to specific receptors inducing inhibition of calcium currents, Nature, 353, 43, 1991.
    • (1991) Nature , vol.353 , pp. 43
    • Kleuss, C.1    Hescheler, J.2    Ewel, C.3    Rosenthal, W.4    Schultz, G.5    Wittig, B.6
  • 92
    • 0026752495 scopus 로고
    • Different β-subunits determine G-protein interaction with transmembrane receptors
    • Kleuss, C., Scherübl, H., Hescheler, J., Schultz, G., and Wittig, B., Different β-subunits determine G-protein interaction with transmembrane receptors, Nature, 358, 424, 1992.
    • (1992) Nature , vol.358 , pp. 424
    • Kleuss, C.1    Scherübl, H.2    Hescheler, J.3    Schultz, G.4    Wittig, B.5
  • 93
    • 0027530916 scopus 로고
    • Selectivity in signal transduction determined by γ subunits of heterotrimeric G proteins
    • Kleuss, C., Scherübl, H., Hescheler, J., Schultz, G., and Wittig, B., Selectivity in signal transduction determined by γ subunits of heterotrimeric G proteins, Science, 259, 832, 1993.
    • (1993) Science , vol.259 , pp. 832
    • Kleuss, C.1    Scherübl, H.2    Hescheler, J.3    Schultz, G.4    Wittig, B.5
  • 94
    • 0026676807 scopus 로고
    • Subunits βγ of heterotrimeric G protein activate β2 isoform of phospholipase C
    • Katz, A., Wu, D., and Simon, M. I., Subunits βγ of heterotrimeric G protein activate β2 isoform of phospholipase C, Nature, 360, 686, 1992.
    • (1992) Nature , vol.360 , pp. 686
    • Katz, A.1    Wu, D.2    Simon, M.I.3
  • 95
    • 0028240869 scopus 로고
    • Signalling from heterotrimeric G proteins to MAP kinase involved βγ subunits acting on a rasdependent pathway
    • Crespo, P., Xu, N., Simonds, W. F., and Gutkind, J. S., Signalling from heterotrimeric G proteins to MAP kinase involved βγ subunits acting on a rasdependent pathway, Nature, 369, 418, 1994.
    • (1994) Nature , vol.369 , pp. 418
    • Crespo, P.1    Xu, N.2    Simonds, W.F.3    Gutkind, J.S.4
  • 97
    • 0028945487 scopus 로고
    • Acetylcholine muscarinic receptor regulation of the ras/ raf/MAP kinase pathway
    • Qian, N.-X., Russell, M., and Johnson, G. L., Acetylcholine muscarinic receptor regulation of the ras/ raf/MAP kinase pathway, Life Sci., 56, 945, 1995.
    • (1995) Life Sci. , vol.56 , pp. 945
    • Qian, N.-X.1    Russell, M.2    Johnson, G.L.3
  • 98
    • 9444285925 scopus 로고
    • Proliferative signaling through muscarinic receptors: A model for receptors coupled to heterotrimeric G proteins
    • Wess, J., Ed., Molecular Biology Intelligence Unit, R. G. Landes, Austin
    • Gutkind, J. S., Crespo, P., Coso, O.A., Kalinec, G., and Xu, N., Proliferative signaling through muscarinic receptors: a model for receptors coupled to heterotrimeric G proteins, in Molecular Mechanisms of Muscarinic Acetylcholine Receptor Function, Wess, J., Ed., Molecular Biology Intelligence Unit, R. G. Landes, Austin, 1995, 103.
    • (1995) Molecular Mechanisms of Muscarinic Acetylcholine Receptor Function , pp. 103
    • Gutkind, J.S.1    Crespo, P.2    Coso, O.A.3    Kalinec, G.4    Xu, N.5
  • 99
    • 0024204109 scopus 로고
    • Location of a region of the muscarinic acetylcholine receptor involved in selective effector coupling
    • Kubo, T., Bujo, H., Akiba, I., Nakai, J., Mishina, M., and Numa, S., Location of a region of the muscarinic acetylcholine receptor involved in selective effector coupling, FEBS Lett., 241, 119, 1988.
    • (1988) FEBS Lett. , vol.241 , pp. 119
    • Kubo, T.1    Bujo, H.2    Akiba, I.3    Nakai, J.4    Mishina, M.5    Numa, S.6
  • 100
    • 0024450129 scopus 로고
    • Deletion analysis of the mouse m1 muscarinic acetylcholine receptor: Effects on phosphoinositide metabolism and down-regulation
    • Shapiro, R. A. and Nathanson N. M., Deletion analysis of the mouse m1 muscarinic acetylcholine receptor: effects on phosphoinositide metabolism and down-regulation, Biochemistry, 28, 8946, 1989.
    • (1989) Biochemistry , vol.28 , pp. 8946
    • Shapiro, R.A.1    Nathanson, N.M.2
  • 101
    • 0026734744 scopus 로고
    • Hm1 muscarinic cholinergic receptor internalization requires a domain in the third cytoplasmic loop
    • Lameh, J., Philip, M., Sharma, Y. K., Moro, O., Ramachandran, J., and Sadee, W., Hm1 muscarinic cholinergic receptor internalization requires a domain in the third cytoplasmic loop, J. Biol. Chem., 267, 13406, 1992.
    • (1992) J. Biol. Chem. , vol.267 , pp. 13406
    • Lameh, J.1    Philip, M.2    Sharma, Y.K.3    Moro, O.4    Ramachandran, J.5    Sadee, W.6
  • 102
    • 0026464893 scopus 로고
    • Mutational analysis of third cytoplasmic loop domains in G-protein coupling of the Hm1 muscarinic receptor
    • Arden, J. R., Nagata, O., Shockley, M. S., Philip, M., Lameh, J., and Sadee, W., Mutational analysis of third cytoplasmic loop domains in G-protein coupling of the Hm1 muscarinic receptor, Biochem. Biophys. Res. Commun., 188, 1111, 1992.
    • (1992) Biochem. Biophys. Res. Commun. , vol.188 , pp. 1111
    • Arden, J.R.1    Nagata, O.2    Shockley, M.S.3    Philip, M.4    Lameh, J.5    Sadee, W.6
  • 103
    • 0027328071 scopus 로고
    • Charged amino acids required for signal transduction by the m3 muscarinic acetylcholine receptor
    • Kunkel, M. T. and Peralta E. G., Charged amino acids required for signal transduction by the m3 muscarinic acetylcholine receptor, EMBO J., 12, 3809, 1993.
    • (1993) EMBO J. , vol.12 , pp. 3809
    • Kunkel, M.T.1    Peralta, E.G.2
  • 104
    • 0024430081 scopus 로고
    • Identification of a small intracellular region of the muscarinic m3 receptor as a determinant of selective coupling to PI turnover
    • Wess, J., Brann, M. R., and Bonner, T. I., Identification of a small intracellular region of the muscarinic m3 receptor as a determinant of selective coupling to PI turnover, FEBS Lett., 258, 133, 1989.
    • (1989) FEBS Lett. , vol.258 , pp. 133
    • Wess, J.1    Brann, M.R.2    Bonner, T.I.3
  • 105
    • 0025600997 scopus 로고
    • Distinct sequence elements control the specificity of G protein activation by muscarinic acetylcholine receptor subtypes
    • Lechleiter, J., Hellmiss, R., Duerson, K., Ennulat, D., David, N., Clapham, D., and Peralta, E., Distinct sequence elements control the specificity of G protein activation by muscarinic acetylcholine receptor subtypes, EMBO J., 9, 4381, 1990.
    • (1990) EMBO J. , vol.9 , pp. 4381
    • Lechleiter, J.1    Hellmiss, R.2    Duerson, K.3    Ennulat, D.4    David, N.5    Clapham, D.6    Peralta, E.7
  • 106
    • 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., Identification of an intracellular tyrosine residue critical for muscarinic receptor-mediated stimulation of phosphatidyl inositol hydrolysis, J. Biol. Chem., 269, 402, 1994.
    • (1994) J. Biol. Chem. , vol.269 , pp. 402
    • Blüml, K.1    Mutschler, E.2    Wess, J.3
  • 108
    • 0027379660 scopus 로고
    • Hydrophobic amino acid in the i2 loop plays a key role in receptor-G protein coupling
    • Moro, O., Lameh, J., Högger, P., and Sadee, W., Hydrophobic amino acid in the i2 loop plays a key role in receptor-G protein coupling, J. Biol. Chem., 268, 22273, 1993.
    • (1993) J. Biol. Chem. , vol.268 , pp. 22273
    • Moro, O.1    Lameh, J.2    Högger, P.3    Sadee, W.4
  • 109
    • 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., Activating and inactivating mutations in N- and C-terminal i3 loop junctions of muscarinic acetylcholine Hm1 receptors, J. Biol. Chem., 270, 7405, 1995.
    • (1995) J. Biol. Chem. , vol.270 , pp. 7405
    • Högger, P.1    Shockley, M.S.2    Lameh, J.3    Sadee, W.4
  • 110
    • 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., Functional role of a cytoplasmic aromatic amino acid in muscarinic receptor-mediated activation of phospholipase C, J. Biol. Chem., 269, 11537, 1994.
    • (1994) J. Biol. Chem. , vol.269 , pp. 11537
    • Blüml, K.1    Mutschler, E.2    Wess, J.3
  • 111
    • 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., 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. U.S.A., 91, 7980, 1994.
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 7980
    • Blüml, K.1    Mutschler, E.2    Wess, J.3
  • 112
    • 0029059732 scopus 로고
    • q/11 by the m3 muscarinic acetylcholine receptor
    • q/11 by the m3 muscarinic acetylcholine receptor, J. Biol. Chem., 270, 17741, 1995.
    • (1995) J. Biol. Chem. , vol.270 , pp. 17741
    • Blin, N.1    Yun, J.2    Wess, J.3
  • 115
    • 0024519931 scopus 로고
    • Structural basis of β-adrenergic receptor function
    • Strader, C. D., Sigal, I. S., and Dixon, R. A. F., Structural basis of β-adrenergic receptor function, FASEB J., 3, 1825, 1989.
    • (1989) FASEB J. , vol.3 , pp. 1825
    • Strader, C.D.1    Sigal, I.S.2    Dixon, R.A.F.3
  • 116
  • 117
    • 0023716027 scopus 로고
    • Site of G protein binding to rhodopsin mapped with synthetic peptides from the α subunit
    • Hamm, H. E., Deretik, D., Arendt, A., Hargrave, P. A., Koenig, B., and Hofmann, K. P., Site of G protein binding to rhodopsin mapped with synthetic peptides from the α subunit, Science, 241, 832, 1988.
    • (1988) Science , vol.241 , pp. 832
    • Hamm, H.E.1    Deretik, D.2    Arendt, A.3    Hargrave, P.A.4    Koenig, B.5    Hofmann, K.P.6
  • 122
    • 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., Identification of a receptor/G protein contact site critical for signalling specificity and G protein activation, Proc. Natl. Acad. Sci. U.S.A., 92, 11642, 1995.
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 11642
    • Liu, J.1    Conklin, B.R.2    Blin, N.3    Yun, J.4    Wess, J.5
  • 123
    • 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, 1992.
    • (1992) J. Biol. Chem. , vol.267 , pp. 8342
    • Okamoto, T.1    Nishimoto, I.2
  • 125
    • 0028920668 scopus 로고
    • Protein kinases that phosphorylate activated G protein-coupled receptors
    • Premont, R. T., Inglese, J., and Lefkowitz, R. J., Protein kinases that phosphorylate activated G protein-coupled receptors, FASEB J., 9, 175, 1995.
    • (1995) FASEB J. , vol.9 , pp. 175
    • Premont, R.T.1    Inglese, J.2    Lefkowitz, R.J.3
  • 128
    • 0023585049 scopus 로고
    • Internalization and recycling of receptor-bound gonadotropin-releasing hormone agonist in pituitary gonadotropes
    • Schvartz, I. and Hazum, E., Internalization and recycling of receptor-bound gonadotropin-releasing hormone agonist in pituitary gonadotropes, J. Biol. Chem., 262, 17046, 1987.
    • (1987) J. Biol. Chem. , vol.262 , pp. 17046
    • Schvartz, I.1    Hazum, E.2
  • 129
    • 9444277951 scopus 로고
    • Determination of the pathway of muscarinic receptor internalization
    • abstract
    • Tolbert, L. M. and Lameh, J., Determination of the pathway of muscarinic receptor internalization, Life Sci., 56, 1025 (abstract), 1995.
    • (1995) Life Sci. , vol.56 , pp. 1025
    • Tolbert, L.M.1    Lameh, J.2
  • 130
    • 0025045754 scopus 로고
    • Internalization of the Hm1 muscarinic cholinergic receptor involves the third cytoplasmic loop
    • Maeda, S., Lameh, J., Mallet, W. G., Philip, M., Ramachandran, J., and Sadee, W., Internalization of the Hm1 muscarinic cholinergic receptor involves the third cytoplasmic loop, FEBS Lett., 269, 386, 1990.
    • (1990) FEBS Lett. , vol.269 , pp. 386
    • Maeda, S.1    Lameh, J.2    Mallet, W.G.3    Philip, M.4    Ramachandran, J.5    Sadee, W.6
  • 131
    • 0027479116 scopus 로고
    • Serine- and threonine-rich domain regulates internalization of muscarinic cholinergic receptors
    • Moro, O., Lameh, J., and Sadée, W., Serine- and threonine-rich domain regulates internalization of muscarinic cholinergic receptors, J. Biol. Chem., 268, 6862, 1993.
    • (1993) J. Biol. Chem. , vol.268 , pp. 6862
    • Moro, O.1    Lameh, J.2    Sadée, W.3
  • 132
    • 0024450129 scopus 로고
    • Deletion analysis of the mouse m1 muscarinic acetylcholine receptor: Effects on phosphoinositide metabolism and down-regulation
    • Shapiro, R. A. and Nathanson, N. M., Deletion analysis of the mouse m1 muscarinic acetylcholine receptor: effects on phosphoinositide metabolism and down-regulation, Biochemistry, 28, 8946, 1989.
    • (1989) Biochemistry , vol.28 , pp. 8946
    • Shapiro, R.A.1    Nathanson, N.M.2
  • 133
    • 0027419077 scopus 로고
    • Cross-talk between m1 muscarinic acetylcholine receptors and β2-adrenergic receptors. cAMP and the third intracellular loop of the m1 muscarinic receptor confer heterologous regulation
    • Lee, N. H. and Fraser, C. M., Cross-talk between m1 muscarinic acetylcholine receptors and β2-adrenergic receptors. cAMP and the third intracellular loop of the m1 muscarinic receptor confer heterologous regulation, J. Biol. Chem., 268, 7949, 1993.
    • (1993) J. Biol. Chem. , vol.268 , pp. 7949
    • Lee, N.H.1    Fraser, C.M.2
  • 134
    • 0345662087 scopus 로고
    • Structural basis of muscarinic receptor sequestration and down-regulation
    • Wess, J., Ed., Molecular Biology Intelligence Unit, R. G. Landes, Austin
    • Shockley, M. S., Lameh J., and Sadée, W., Structural basis of muscarinic receptor sequestration and down-regulation, in Molecular Mechanisms of Muscarinic Acetylcholine Receptor Function, Wess, J., Ed., Molecular Biology Intelligence Unit, R. G. Landes, Austin, 1995, 183.
    • (1995) Molecular Mechanisms of Muscarinic Acetylcholine Receptor Function , pp. 183
    • Shockley, M.S.1    Lameh, J.2    Sadée, W.3
  • 135
    • 0028270707 scopus 로고
    • Overlapping multi-site domains of the muscarinic cholinergic Hm1 receptor involved in signal transduction and sequestration
    • Moro, O., Shockley, M. S., Lameh J., and Sadée, W., Overlapping multi-site domains of the muscarinic cholinergic Hm1 receptor involved in signal transduction and sequestration, J. Biol. Chem., 269, 6651, 1994.
    • (1994) J. Biol. Chem. , vol.269 , pp. 6651
    • Moro, O.1    Shockley, M.S.2    Lameh, J.3    Sadée, W.4
  • 136
    • 0038751147 scopus 로고
    • Genetic analysis of β-adrenergic receptor internalization and down-regulation
    • Mahan, L. H., Koachman, A. M., and Insel, P. A., Genetic analysis of β-adrenergic receptor internalization and down-regulation, Proc. Natl. Acad. Sci. U.S.A., 82, 129, 1985.
    • (1985) Proc. Natl. Acad. Sci. U.S.A. , vol.82 , pp. 129
    • Mahan, L.H.1    Koachman, A.M.2    Insel, P.A.3
  • 137
    • 0024460485 scopus 로고
    • β2-adrenergic receptor regulation after transfection into a cell line deficient in the cAMP-dependent protein kinase
    • Allen, J. M., Abrass, I. B., and Palmiter, R. D., β2-adrenergic receptor regulation after transfection into a cell line deficient in the cAMP-dependent protein kinase, Mol. Pharmacol., 36, 244, 1989.
    • (1989) Mol. Pharmacol. , vol.36 , pp. 244
    • Allen, J.M.1    Abrass, I.B.2    Palmiter, R.D.3
  • 138
    • 0025316096 scopus 로고
    • Separation of the structural requirements for agonist-promoted activation and sequestration of the β-adrenergic receptor
    • Cheung, A. H., Dixon, R. A. F., Hill, W. S., Sigal, I. S., and Strader, C. D., Separation of the structural requirements for agonist-promoted activation and sequestration of the β-adrenergic receptor, Mol. Pharmacol., 37, 775, 1990.
    • (1990) Mol. Pharmacol. , vol.37 , pp. 775
    • Cheung, A.H.1    Dixon, R.A.F.2    Hill, W.S.3    Sigal, I.S.4    Strader, C.D.5
  • 139
    • 0025959676 scopus 로고
    • Mutations of the human β2-adrenergic receptor that impair coupling to Gs interfere with receptor down-regulation but not sequestration
    • Campbell, P. T., Hnatowich, M., O'Dowd, B. F., Caron, M. G., Lefkowitz, R. J., and Hausdorff, W. P., Mutations of the human β2-adrenergic receptor that impair coupling to Gs interfere with receptor down-regulation but not sequestration, Mol. Pharmacol., 39, 192, 1991.
    • (1991) Mol. Pharmacol. , vol.39 , pp. 192
    • Campbell, P.T.1    Hnatowich, M.2    O'Dowd, B.F.3    Caron, M.G.4    Lefkowitz, R.J.5    Hausdorff, W.P.6
  • 141
    • 0028000662 scopus 로고
    • A highly conserved tyrosine residue in G-protein coupled receptors is required for agonist-mediated β2-adrenergic receptor sequestration
    • Barak, L. S., Tiberi, M., Freedman, N. J., Kwatra, M. M., Lefkowitz, R. J., and Caron, M. G., A highly conserved tyrosine residue in G-protein coupled receptors is required for agonist-mediated β2-adrenergic receptor sequestration, J. Biol. Chem., 269, 2790, 1994.
    • (1994) J. Biol. Chem. , vol.269 , pp. 2790
    • Barak, L.S.1    Tiberi, M.2    Freedman, N.J.3    Kwatra, M.M.4    Lefkowitz, R.J.5    Caron, M.G.6
  • 142
    • 0028224959 scopus 로고
    • Differential role of the carboxyl-terminal tyrosine in down-regulation and sequestration of the m2 muscarinic acetylcholine receptor
    • Goldman, P. S. and Nathanson, N. M., Differential role of the carboxyl-terminal tyrosine in down-regulation and sequestration of the m2 muscarinic acetylcholine receptor, J. Biol. Chem., 269, 15640, 1994.
    • (1994) J. Biol. Chem. , vol.269 , pp. 15640
    • Goldman, P.S.1    Nathanson, N.M.2
  • 143
    • 0018729657 scopus 로고
    • Muscarinic acetylcholine receptor regulation by accelerated rate of receptor loss
    • Klein, W. L., Nathanson, N. M., and Nirenberg, M., Muscarinic acetylcholine receptor regulation by accelerated rate of receptor loss, Biochem. Biophys. Res. Commun., 90, 506, 1979.
    • (1979) Biochem. Biophys. Res. Commun. , vol.90 , pp. 506
    • Klein, W.L.1    Nathanson, N.M.2    Nirenberg, M.3
  • 144
    • 0019838290 scopus 로고
    • Recovery of β-adrenergic receptors following long term exposure of astrocytoma cells to catecholamines. Role of protein synthesis
    • Doss, R. C., Perkins, J. P., and Harden, T. K., Recovery of β-adrenergic receptors following long term exposure of astrocytoma cells to catecholamines. Role of protein synthesis, J. Biol. Chem., 256, 12281, 1981.
    • (1981) J. Biol. Chem. , vol.256 , pp. 12281
    • Doss, R.C.1    Perkins, J.P.2    Harden, T.K.3
  • 145
    • 0028067186 scopus 로고
    • Agonist-mediated destabilization of m1 muscarinic acetylcholine receptor mRNA. Elements involved in mRNA stability are localized in the 3′-untranslated region
    • Lee, N. H., Earle-Hughes, J., and Fraser, C. M., Agonist-mediated destabilization of m1 muscarinic acetylcholine receptor mRNA. Elements involved in mRNA stability are localized in the 3′-untranslated region, J. Biol. Chem., 269, 4291, 1994.
    • (1994) J. Biol. Chem. , vol.269 , pp. 4291
    • Lee, N.H.1    Earle-Hughes, J.2    Fraser, C.M.3
  • 146
    • 0027723648 scopus 로고
    • Human m3 muscarinic acetylcholine receptor carboxyl-terminal threonine residues are required for agonist-induced receptor down-regulation
    • Yang, J., Logsdon, C. D., Johansen, T. E., and Williams, J. A., Human m3 muscarinic acetylcholine receptor carboxyl-terminal threonine residues are required for agonist-induced receptor down-regulation, Mol. Pharmacol., 44, 1158, 1993.
    • (1993) Mol. Pharmacol. , vol.44 , pp. 1158
    • Yang, J.1    Logsdon, C.D.2    Johansen, T.E.3    Williams, J.A.4
  • 147
    • 0026735236 scopus 로고
    • Regulation of muscarinic acetylcholine receptor mRNA expression by activation of homologous and heterologous receptors
    • Habecker, B. A. and Nathanson, N. M., Regulation of muscarinic acetylcholine receptor mRNA expression by activation of homologous and heterologous receptors, Proc. Natl. Acad. Sci. U.S.A., 89, 5035, 1992.
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 5035
    • Habecker, B.A.1    Nathanson, N.M.2
  • 148
    • 0026015948 scopus 로고
    • Expression and agonist-induced down-regulation of mRNAs of m2- and m3-muscarinic acetylcholine receptors in cultured cerebellar granule cells
    • Fukamauchi, F., Hough, C., and Chuang, D.-M., Expression and agonist-induced down-regulation of mRNAs of m2- and m3-muscarinic acetylcholine receptors in cultured cerebellar granule cells, J. Neurochem., 56, 716, 1991.
    • (1991) J. Neurochem. , vol.56 , pp. 716
    • Fukamauchi, F.1    Hough, C.2    Chuang, D.-M.3
  • 149
    • 0027361173 scopus 로고
    • Agonist-induced down-regulation and antagonist-induced up-regulation of m2- and m3-muscarinic acetylcholine receptor mRNA and protein in cultured cerebellar granule cells
    • Fukamauchi, F., Saunders, P. A., Hough, C., and Chuang, D.-M., Agonist-induced down-regulation and antagonist-induced up-regulation of m2- and m3-muscarinic acetylcholine receptor mRNA and protein in cultured cerebellar granule cells, Mol. Pharmacol., 44, 940, 1993.
    • (1993) Mol. Pharmacol. , vol.44 , pp. 940
    • Fukamauchi, F.1    Saunders, P.A.2    Hough, C.3    Chuang, D.-M.4
  • 150
    • 0028920563 scopus 로고
    • Transcriptional down-regulation of m2 muscarinic receptor gene expression in human embryonic lung (HEL 299) cells by protein kinase C
    • 149a. Rousell, J., Haddad, E.-B., Mak, J. C. W., and Barnes, P. J., Transcriptional down-regulation of m2 muscarinic receptor gene expression in human embryonic lung (HEL 299) cells by protein kinase C, J. Biol. Chem., 270, 7213, 1995.
    • (1995) J. Biol. Chem. , vol.270 , pp. 7213
    • Rousell, J.1    Haddad, E.-B.2    Mak, J.C.W.3    Barnes, P.J.4
  • 151
    • 0028913071 scopus 로고
    • Multiple mechanisms involving protein phosphorylation are linked to desensitization of muscarinic receptors
    • Hosey, M. M., Benovic, J. L., DebBurman, S. K., and Richardson, R. M., Multiple mechanisms involving protein phosphorylation are linked to desensitization of muscarinic receptors, Life Sci., 56, 951, 1995.
    • (1995) Life Sci. , vol.56 , pp. 951
    • Hosey, M.M.1    Benovic, J.L.2    Debburman, S.K.3    Richardson, R.M.4
  • 152
    • 0004941049 scopus 로고
    • Phosphorylation and sequestration of muscarinic receptors
    • Wess, J., Ed., Molecular Biology Intelligence Unit, R. G. Landes, Austin
    • Haga, T., Haga, K., Kameyama, K., and Tsuga, H., Phosphorylation and sequestration of muscarinic receptors, in Molecular Mechanisms of Muscarinic Acetylcholine Receptor Function, Wess, J., Ed., Molecular Biology Intelligence Unit, R. G. Landes, Austin, 1995, 227.
    • (1995) Molecular Mechanisms of Muscarinic Acetylcholine Receptor Function , pp. 227
    • Haga, T.1    Haga, K.2    Kameyama, K.3    Tsuga, H.4
  • 153
    • 0027399999 scopus 로고
    • Phosphorylation of muscarinic receptors: Regulation by G proteins
    • Haga, T., Haga, K., Kameyama, K., and Nakata, H., Phosphorylation of muscarinic receptors: regulation by G proteins, Life Sci., 52, 421, 1993.
    • (1993) Life Sci. , vol.52 , pp. 421
    • Haga, T.1    Haga, K.2    Kameyama, K.3    Nakata, H.4
  • 155
  • 156
    • 0025025929 scopus 로고
    • Agonist-independent phosphorylation of purified cardiac muscarinic cholinergic receptors by protein kinase C
    • Richardson, R. M. and Hosey M. M., Agonist-independent phosphorylation of purified cardiac muscarinic cholinergic receptors by protein kinase C, Biochemistry, 29, 8555, 1990.
    • (1990) Biochemistry , vol.29 , pp. 8555
    • Richardson, R.M.1    Hosey, M.M.2
  • 157
    • 0026730334 scopus 로고
    • Functional effects of protein kinase C-mediated phosphorylation of chick heart muscarinic cholinergic receptors
    • Richardson, R. M., Ptasienski, J., and Hosey, M. M., Functional effects of protein kinase C-mediated phosphorylation of chick heart muscarinic cholinergic receptors, J. Biol. Chem., 267, 10127, 1992.
    • (1992) J. Biol. Chem. , vol.267 , pp. 10127
    • Richardson, R.M.1    Ptasienski, J.2    Hosey, M.M.3
  • 158
    • 0027278632 scopus 로고
    • Rapid agonist-mediated phosphorylation of m3-muscarinic receptors revealed by immunoprecipitation
    • Tobin, A. B. and Nahorski, S. R., Rapid agonist-mediated phosphorylation of m3-muscarinic receptors revealed by immunoprecipitation, J. Biol. Chem., 268, 9817, 1993.
    • (1993) J. Biol. Chem. , vol.268 , pp. 9817
    • Tobin, A.B.1    Nahorski, S.R.2
  • 159
    • 0023657034 scopus 로고
    • Phosphorylation of the porcine atrial muscarinic acetylcholine receptor by cyclic AMP dependent protein kinase
    • Rosenbaum, L. C., Malencik, D. A., Anderson, S. R., Tota, M. R., and Schimerlik, M. I., Phosphorylation of the porcine atrial muscarinic acetylcholine receptor by cyclic AMP dependent protein kinase, Biochemistry, 26, 8183, 1987.
    • (1987) Biochemistry , vol.26 , pp. 8183
    • Rosenbaum, L.C.1    Malencik, D.A.2    Anderson, S.R.3    Tota, M.R.4    Schimerlik, M.I.5
  • 160
    • 9444227110 scopus 로고
    • Regulation of expression and function of muscarinic receptors
    • Wess, J., Ed., Molecular Biology Intelligence Unit, R. G. Landes, Austin
    • Goldman, P. S. and Nathanson, N. M., Regulation of expression and function of muscarinic receptors, in Molecular Mechanisms of Muscarinic Acetylcholine Receptor Function, Wess, J., Ed., Molecular Biology Intelligence Unit, R. G. Landes, Austin, 1995, 197.
    • (1995) Molecular Mechanisms of Muscarinic Acetylcholine Receptor Function , pp. 197
    • Goldman, P.S.1    Nathanson, N.M.2
  • 161
    • 0024998843 scopus 로고
    • Differential regulation by agonist and phorbol ester of cloned m1 and m2 muscarinic acetylcholine receptors in mouse Y1 adrenal cells and in Y1 cells deficient in cAMP-dependent protein kinase
    • Scherer, N. M. and Nathanson, N. M., Differential regulation by agonist and phorbol ester of cloned m1 and m2 muscarinic acetylcholine receptors in mouse Y1 adrenal cells and in Y1 cells deficient in cAMP-dependent protein kinase, Biochemistry, 29, 8475, 1990.
    • (1990) Biochemistry , vol.29 , pp. 8475
    • Scherer, N.M.1    Nathanson, N.M.2
  • 163
    • 0027981478 scopus 로고
    • G protein-coupled receptor kinases
    • Haga, T., Haga K., and Kameyama, K., G protein-coupled receptor kinases, J. Neurochem., 63, 400, 1994.
    • (1994) J. Neurochem. , vol.63 , pp. 400
    • Haga, T.1    Haga, K.2    Kameyama, K.3
  • 164
    • 0025742855 scopus 로고
    • Role of acidic amino acids in peptide substrates of the β-adrenergic receptor kinase and rhodopsin kinase
    • Onorato, J. J., Palczewski, K., Regan, J. W., Caron, M. G., Lefkowitz, R. J., and Benovic, J. L., Role of acidic amino acids in peptide substrates of the β-adrenergic receptor kinase and rhodopsin kinase, Biochemistry, 30, 5118, 1991.
    • (1991) Biochemistry , vol.30 , pp. 5118
    • Onorato, J.J.1    Palczewski, K.2    Regan, J.W.3    Caron, M.G.4    Lefkowitz, R.J.5    Benovic, J.L.6
  • 166
  • 167
    • 0028089039 scopus 로고
    • Expression, purification, and characterization of the G protein-coupled receptor kinase GRK5
    • Kunapuli, P., Onorato, J. J., Hosey, M. M., and Benovic, J. L., Expression, purification, and characterization of the G protein-coupled receptor kinase GRK5, J. Biol. Chem., 269, 1099, 1994.
    • (1994) J. Biol. Chem. , vol.269 , pp. 1099
    • Kunapuli, P.1    Onorato, J.J.2    Hosey, M.M.3    Benovic, J.L.4
  • 168
    • 0027992129 scopus 로고
    • Expression, purification, and characterization of the G protein-coupled receptor kinase GRK6
    • London, R. P. and Benovic, J. L., Expression, purification, and characterization of the G protein-coupled receptor kinase GRK6, J. Biol. Chem., 269, 22691, 1994.
    • (1994) J. Biol. Chem. , vol.269 , pp. 22691
    • London, R.P.1    Benovic, J.L.2
  • 170
    • 0022971472 scopus 로고
    • Phosphorylation of the cardiac muscarinic receptor in intact chick heart and its regulation by a muscarinic agonist
    • Kwatra, M. M. and Hosey, M. M., Phosphorylation of the cardiac muscarinic receptor in intact chick heart and its regulation by a muscarinic agonist, J. Biol. Chem., 261, 12429, 1986.
    • (1986) J. Biol. Chem. , vol.261 , pp. 12429
    • Kwatra, M.M.1    Hosey, M.M.2
  • 171
    • 0023645967 scopus 로고
    • Correlation of agonist-induced phosphorylation of chick heart muscarinic receptors with receptor desensitization
    • Kwatra, M. M., Leung, E., Maan, A. C., McMahon, K. K., Ptasienski, J., Green, R. D., and Hosey, M. M., Correlation of agonist-induced phosphorylation of chick heart muscarinic receptors with receptor desensitization, J. Biol. Chem., 262, 16314, 1987.
    • (1987) J. Biol. Chem. , vol.262 , pp. 16314
    • Kwatra, M.M.1    Leung, E.2    Maan, A.C.3    McMahon, K.K.4    Ptasienski, J.5    Green, R.D.6    Hosey, M.M.7
  • 172
    • 0024411428 scopus 로고
    • The porcine heart M2 muscarinic receptor: Agonist-induced phosphorylation and comparison of properties with the chick heart receptor
    • Kwatra, M. M., Ptasienski, J., and Hosey, M. M., The porcine heart M2 muscarinic receptor: agonist-induced phosphorylation and comparison of properties with the chick heart receptor, Mol. Pharmacol., 35, 553, 1989.
    • (1989) Mol. Pharmacol. , vol.35 , pp. 553
    • Kwatra, M.M.1    Ptasienski, J.2    Hosey, M.M.3
  • 173
    • 0026540133 scopus 로고
    • Agonist-induced phosphorylation and desensitization of human m2 muscarinic cholinergic receptors in Sf9 insect cells
    • Richardson, R. M. and Hosey M. M., Agonist-induced phosphorylation and desensitization of human m2 muscarinic cholinergic receptors in Sf9 insect cells, J. Biol. Chem., 267, 22249, 1992.
    • (1992) J. Biol. Chem. , vol.267 , pp. 22249
    • Richardson, R.M.1    Hosey, M.M.2
  • 174
    • 0027490599 scopus 로고
    • Phosphorylation and desensitization of human m2 muscarinic cholinergic receptors by two isoforms of the β-adrenergic receptor kinase
    • Richardson, R. M., Kim, C., Benovic, J. L., and Hosey, M. M., Phosphorylation and desensitization of human m2 muscarinic cholinergic receptors by two isoforms of the β-adrenergic receptor kinase, J. Biol. Chem., 268, 13650, 1993.
    • (1993) J. Biol. Chem. , vol.268 , pp. 13650
    • Richardson, R.M.1    Kim, C.2    Benovic, J.L.3    Hosey, M.M.4
  • 175
    • 0026793617 scopus 로고
    • Activation by G protein βγ subunits of agonist- Or light-dependent phosphorylation of muscarinic acetylcholine receptors and rhodopsin
    • Haga, K. and Haga, T., Activation by G protein βγ subunits of agonist- or light-dependent phosphorylation of muscarinic acetylcholine receptors and rhodopsin, J. Biol. Chem., 267, 2222, 1992.
    • (1992) J. Biol. Chem. , vol.267 , pp. 2222
    • Haga, K.1    Haga, T.2
  • 176
    • 0028036138 scopus 로고
    • Location of agonist-dependent-phosphorylation sites in the third intracellular loop of muscarinic acetylcholine receptors (m2 subtype)
    • Nakata, H., Kameyama, K., Haga, K., and Haga, T., Location of agonist-dependent-phosphorylation sites in the third intracellular loop of muscarinic acetylcholine receptors (m2 subtype), Eur. J. Biochem., 220, 29, 1994.
    • (1994) Eur. J. Biochem. , vol.220 , pp. 29
    • Nakata, H.1    Kameyama, K.2    Haga, K.3    Haga, T.4
  • 177
    • 0028079889 scopus 로고
    • Activation of a GTP-binding protein and a GTP-binding-protein-coupled receptor kinase (β-adrenergic-receptor kinase-1) by a muscarinic receptor m2 mutant lacking phosphorylation sites
    • Kameyama, K., Haga, K., Haga, T., Moro, O, and Sadee, W., Activation of a GTP-binding protein and a GTP-binding-protein-coupled receptor kinase (β-adrenergic-receptor kinase-1) by a muscarinic receptor m2 mutant lacking phosphorylation sites, Eur. J. Biochem., 226, 267, 1994.
    • (1994) Eur. J. Biochem. , vol.226 , pp. 267
    • Kameyama, K.1    Haga, K.2    Haga, T.3    Moro, O.4    Sadee, W.5
  • 180
    • 0028568644 scopus 로고
    • Sequestration of muscarinic acetylcholine receptor m2 subtypes. Facilitation by G protein-coupled receptor kinase (GRK2) and attenuation by a dominant-negative mutant of GRK2
    • Tsuga, H., Kameyama, K., Haga, T., Kurose, H., and Nagao, T., Sequestration of muscarinic acetylcholine receptor m2 subtypes. Facilitation by G protein-coupled receptor kinase (GRK2) and attenuation by a dominant-negative mutant of GRK2, J. Biol. Chem., 269, 32522, 1994.
    • (1994) J. Biol. Chem. , vol.269 , pp. 32522
    • Tsuga, H.1    Kameyama, K.2    Haga, T.3    Kurose, H.4    Nagao, T.5
  • 181
    • 0027339673 scopus 로고
    • Muscarinic m2 receptors in cerebellar granule cell cultures from rat: Mechanism of short-term desensitization
    • Contrera, J. G., Mcleskey, S. W., Holopainen, I., Xu, J., and Wojcik, W. J., Muscarinic m2 receptors in cerebellar granule cell cultures from rat: mechanism of short-term desensitization, J. Pharmacol. Exp. Ther., 265, 433, 1993.
    • (1993) J. Pharmacol. Exp. Ther. , vol.265 , pp. 433
    • Contrera, J.G.1    Mcleskey, S.W.2    Holopainen, I.3    Xu, J.4    Wojcik, W.J.5
  • 182
    • 0027185782 scopus 로고
    • Mechanism of β-adrenergic receptor kinase activation by G proteins
    • Kim, C. M., Dion, S. B., and Benovic, J. L., Mechanism of β-adrenergic receptor kinase activation by G proteins, J. Biol. Chem., 268, 15412, 1993.
    • (1993) J. Biol. Chem. , vol.268 , pp. 15412
    • Kim, C.M.1    Dion, S.B.2    Benovic, J.L.3
  • 183
    • 0027418322 scopus 로고
    • Activation by G protein βγ subunits of β-adrenergic and muscarinic receptor kinase
    • Kameyama, K., Haga, K., Haga, T., Kontani., K., Katada, T., and Fukada, Y., Activation by G protein βγ subunits of β-adrenergic and muscarinic receptor kinase, J Biol. Chem., 268, 7753, 1993.
    • (1993) J Biol. Chem. , vol.268 , pp. 7753
    • Kameyama, K.1    Haga, K.2    Haga, T.3    Kontani, K.4    Katada, T.5    Fukada, Y.6
  • 184
    • 0027368165 scopus 로고
    • Structure and mechanism of the G protein-coupled receptor kinases
    • Inglese, J., Freedman, N. J., Koch, W. J., and Lefkowitz, R. J., Structure and mechanism of the G protein-coupled receptor kinases, J. Biol. Chem., 268, 23735, 1993.
    • (1993) J. Biol. Chem. , vol.268 , pp. 23735
    • Inglese, J.1    Freedman, N.J.2    Koch, W.J.3    Lefkowitz, R.J.4
  • 185
    • 0027481032 scopus 로고
    • The binding site for the βγ subunits of heterotrimeric G proteins on the β-adrenergic receptor kinase
    • Koch, W. J., Inglese, J., Stone, W. C., and Lefkowitz, R. J., The binding site for the βγ subunits of heterotrimeric G proteins on the β-adrenergic receptor kinase, J. Biol. Chem., 268, 8256, 1993.
    • (1993) J. Biol. Chem. , vol.268 , pp. 8256
    • Koch, W.J.1    Inglese, J.2    Stone, W.C.3    Lefkowitz, R.J.4
  • 187
    • 0028199059 scopus 로고
    • Synergistic activation of a G protein-coupled receptor kinase by G protein βγ subunits and mastoparan or related peptides
    • Haga, K., Kameyama, K., and Haga, T., Synergistic activation of a G protein-coupled receptor kinase by G protein βγ subunits and mastoparan or related peptides, J. Biol. Chem., 269, 12594, 1994.
    • (1994) J. Biol. Chem. , vol.269 , pp. 12594
    • Haga, K.1    Kameyama, K.2    Haga, T.3
  • 188
    • 0025352299 scopus 로고
    • β-Arrestin: A protein that regulates β-adrenergic receptor function
    • Lohse, M. J., Benovic, J. L., Codina, J., Caron, M. G., Lefkowitz, R. J., β-Arrestin: a protein that regulates β-adrenergic receptor function, Science, 248, 1547, 1990.
    • (1990) Science , vol.248 , pp. 1547
    • Lohse, M.J.1    Benovic, J.L.2    Codina, J.3    Caron, M.G.4    Lefkowitz, R.J.5
  • 190
    • 0028924953 scopus 로고
    • Arrestin interactions with G protein-coupled receptors. Direct binding studies of wild type and mutant arrestins with rhodopsin, β2-adrenergic, and m2 muscarinic cholinergic receptors
    • Gurevich, V. V., Dion, S. B., Onorato, J. J., Ptasienski, J., Kim C. M., Sterne-Marr, R., Hosey, M. M., and Benovic, J. L., Arrestin interactions with G protein-coupled receptors. Direct binding studies of wild type and mutant arrestins with rhodopsin, β2-adrenergic, and m2 muscarinic cholinergic receptors, J. Biol. Chem., 270, 720, 1995.
    • (1995) J. Biol. Chem. , vol.270 , pp. 720
    • Gurevich, V.V.1    Dion, S.B.2    Onorato, J.J.3    Ptasienski, J.4    Kim, C.M.5    Sterne-Marr, R.6    Hosey, M.M.7    Benovic, J.L.8
  • 191
    • 0027284218 scopus 로고
    • Binding of wild type and chimeric arrestins to the m2 muscarinic cholinergic receptor
    • Gurevich, V. V., Richardson, R. M., Kim, C. M., Hosey, M. M., and Benovic, J. L., Binding of wild type and chimeric arrestins to the m2 muscarinic cholinergic receptor, J. Biol. Chem., 268, 16879, 1993.
    • (1993) J. Biol. Chem. , vol.268 , pp. 16879
    • Gurevich, V.V.1    Richardson, R.M.2    Kim, C.M.3    Hosey, M.M.4    Benovic, J.L.5
  • 192
    • 0028937671 scopus 로고
    • Agonist-dependent phosphorylation of human muscarinic receptors in Spodoptera frugiperda insect cell membranes by G protein-coupled receptor kinases
    • Debburman, S. K., Kunapuli, P., Benovic, J. L., and Hosey, M. M., Agonist-dependent phosphorylation of human muscarinic receptors in Spodoptera frugiperda insect cell membranes by G protein-coupled receptor kinases, Mol. Pharmacol., 47, 224, 1995.
    • (1995) Mol. Pharmacol. , vol.47 , pp. 224
    • Debburman, S.K.1    Kunapuli, P.2    Benovic, J.L.3    Hosey, M.M.4
  • 193
    • 9444230642 scopus 로고
    • Isolation of two novel G-protein-linked receptor kinases, MRK-1 and MRK-2, that phosphorylate the m3-muscarinic receptor
    • abstract
    • Tobin, A. B. and Nahorski, S. R., Isolation of two novel G-protein-linked receptor kinases, MRK-1 and MRK-2, that phosphorylate the m3-muscarinic receptor, Life Sci., 56, 1029 (abstract), 1995.
    • (1995) Life Sci. , vol.56 , pp. 1029
    • Tobin, A.B.1    Nahorski, S.R.2
  • 194
    • 0027086823 scopus 로고
    • Rapid desensitization of muscarinic m3 receptor-stimulated polyphosphoinositide responses
    • Tobin, A. B., Lambert, D. G., and Nahorski, S. R., Rapid desensitization of muscarinic m3 receptor-stimulated polyphosphoinositide responses, Mol. Pharmacol., 42, 1042, 1992.
    • (1992) Mol. Pharmacol. , vol.42 , pp. 1042
    • Tobin, A.B.1    Lambert, D.G.2    Nahorski, S.R.3
  • 196
    • 0007667725 scopus 로고
    • Mutational analysis of muscarinic receptors: Structural basis of ligand binding and G protein recognition
    • Wess, J., Ed., Molecular Biology Intelligence Unit, R. G. Landes, Austin
    • Wess, J., Liu, J., Blüml, K., Yun, J., Schöneberg, T., and Blin, N., Mutational analysis of muscarinic receptors: structural basis of ligand binding and G protein recognition, in Molecular Mechanisms of Muscarinic Acetylcholine Receptor Function, Wess, J., Ed., Molecular Biology Intelligence Unit, R. G. Landes, Austin, 1995, 1.
    • (1995) Molecular Mechanisms of Muscarinic Acetylcholine Receptor Function , pp. 1
    • Wess, J.1    Liu, J.2    Blüml, K.3    Yun, J.4    Schöneberg, T.5    Blin, N.6
  • 197
    • 9444235691 scopus 로고    scopus 로고
    • Molecular aspects of muscarinic receptor assembly and function
    • Löffelholz, K. and Klein, J., Eds., Progress in Brain Research, Elsevier, Amsterdam, in press
    • Wess, J., Blin, N., Yun, J., Schöneberg, T., and Liu, J., Molecular aspects of muscarinic receptor assembly and function, in Cholinergic Mechanisms: From Molecular Biology to Clinical Significance, Löffelholz, K. and Klein, J., Eds., Progress in Brain Research, Elsevier, Amsterdam, 1996, in press.
    • (1996) Cholinergic Mechanisms: From Molecular Biology to Clinical Significance
    • Wess, J.1    Blin, N.2    Yun, J.3    Schöneberg, T.4    Liu, J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.