메뉴 건너뛰기




Volumn 109, Issue , 1996, Pages 153-162

Molecular aspects of muscarinic receptor assembly and function

Author keywords

[No Author keywords available]

Indexed keywords

CARBACHOL; GUANINE NUCLEOTIDE BINDING PROTEIN; MUSCARINIC RECEPTOR; RECEPTOR SUBTYPE;

EID: 0030463124     PISSN: 00796123     EISSN: None     Source Type: Book Series    
DOI: 10.1016/s0079-6123(08)62097-x     Document Type: Conference Paper
Times cited : (13)

References (46)
  • 1
    • 0027506471 scopus 로고
    • The probable arrangement of the helices in G protein-coupled receptors.
    • J.M. Baldwin The probable arrangement of the helices in G protein-coupled receptors. EMBO J. 1 1993 1693 1703
    • (1993) EMBO J. , vol.1 , pp. 1693-1703
    • Baldwin, J.M.1
  • 2
    • 0028227013 scopus 로고
    • Structure and function of receptors coupled to G proteins.
    • J.M. Baldwin Structure and function of receptors coupled to G proteins. Curr. Opin. Cell Biol. 1 1994 180 190
    • (1994) Curr. Opin. Cell Biol. , vol.1 , pp. 180-190
    • Baldwin, J.M.1
  • 4
    • 0029059732 scopus 로고
    • Mapping of single amino acid residues required for selective activation of Gq/11 by the m3 muscarinic acetylcholine receptor.
    • q/11 by the m3 muscarinic acetylcholine receptor. J. Biol. Chem. 1 1995 17741 17748
    • (1995) J. Biol. Chem. , vol.1 , pp. 17741-17748
    • Blin, N.1    Yun, J.2    Wess, J.3
  • 5
    • 0028158607 scopus 로고
    • Identification of an intracellular tyrosine residue critical for muscarinic receptor-mediated stimulation of phosphatidyl inositol hydrolysis.
    • K. Blüml E. Mutschler J. Wess Identification of an intracellular tyrosine residue critical for muscarinic receptor-mediated stimulation of phosphatidyl inositol hydrolysis. J. Biol. Chem. 1 1994 402 405
    • (1994) J. Biol. Chem. , vol.1 , pp. 402-405
    • Blüml, K.1    Mutschler, E.2    Wess, J.3
  • 6
    • 0028244065 scopus 로고
    • Functional role of a cytoplasmic aromatic amino acid in muscarinic receptor-mediated activation of phospholipaseC.
    • K. Blüml E. Mutschler J. Wess Functional role of a cytoplasmic aromatic amino acid in muscarinic receptor-mediated activation of phospholipase C. J. Biol. Chem. 1 1994 11537 11541
    • (1994) J. Biol. Chem. , vol.1 , pp. 11537-11541
    • Blüml, K.1    Mutschler, E.2    Wess, J.3
  • 7
    • 0027964847 scopus 로고
    • Insertion mutagenesis as a tool to predict the secondary structure of a muscarinic receptor domain determining specificity of G-protein coupling.
    • K. Blüml E. Mutschler J. Wess 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 1 1994 7980 7984
    • (1994) Proc. Natl. Acad. Sci. USA , vol.1 , pp. 7980-7984
    • Blüml, K.1    Mutschler, E.2    Wess, J.3
  • 8
    • 0024039146 scopus 로고
    • Cloning and expression of the human and rat m5 muscarinic acetylcholine receptor genes.
    • T.I. Bonner A.C. Young M.R. Brann N.J. Buckley Cloning and expression of the human and rat m5 muscarinic acetylcholine receptor genes. Neuron 1 1988 403 410
    • (1988) Neuron , vol.1 , pp. 403-410
    • Bonner, T.I.1    Young, A.C.2    Brann, M.R.3    Buckley, N.J.4
  • 9
    • 0027050417 scopus 로고
    • Involvement of specific hydrophobic, but not hydrophilic, amino acids in the third intracellular loop of the β-adrenergic receptor in the activation of Gs.
    • s. Mol. Pharmacol. 1 1992 1061 1065
    • (1992) Mol. Pharmacol. , vol.1 , pp. 1061-1065
    • Cheung, A.H.1    Huang, R.-R.C.2    Strader, C.D.3
  • 10
    • 0027318238 scopus 로고
    • Structural elements of Gα subunits that interact with Gβγ, receptors, and effectors.
    • B.R. Conklin H.R. Bourne Structural elements of Gα subunits that interact with Gβγ, receptors, and effectors. Cell 1 1993 631 641
    • (1993) Cell , vol.1 , pp. 631-641
    • Conklin, B.R.1    Bourne, H.R.2
  • 13
    • 0028800729 scopus 로고
    • Conversion of antagonist-binding site to metal-ion site in the tachykinin NK-1 receptor.
    • C.E. Elling S.M. Nielsen T.W. Schwartz Conversion of antagonist-binding site to metal-ion site in the tachykinin NK-1 receptor. Nature 1 1995 74 77
    • (1995) Nature , vol.1 , pp. 74-77
    • Elling, C.E.1    Nielsen, S.M.2    Schwartz, T.W.3
  • 14
    • 0023716027 scopus 로고
    • Site of G protein binding to rhodopsin mapped with synthetic peptides from the α subunit.
    • H.E. Hamm D. Deretik A. Arendt P.A. Hargrave B. Koenig K.P. Hofmann Site of G protein binding to rhodopsin mapped with synthetic peptides from the α subunit. Science 1 1988 832 835
    • (1988) Science , vol.1 , pp. 832-835
    • Hamm, H.E.1    Deretik, D.2    Arendt, A.3    Hargrave, P.A.4    Koenig, B.5    Hofmann, K.P.6
  • 15
    • 0027422737 scopus 로고
    • Specificity of receptor-G protein interactions: searching for the structure behind the signal.
    • K.E. Hedin K. Duerson D.E. Clapham Specificity of receptor-G protein interactions: searching for the structure behind the signal. Cell. Sig. 1 1993 505 518
    • (1993) Cell. Sig. , vol.1 , pp. 505-518
    • Hedin, K.E.1    Duerson, K.2    Clapham, D.E.3
  • 17
    • 0023889603 scopus 로고
    • Chimeric α2-, β2-adrenergic receptors: delineation of domains involved in effector coupling and ligand binding specificity.
    • B.K. Kobilka T.S. Kobilka K. Daniel J.W. Regan M.J. Caron R.J. Lefkowitz Chimeric α2-, β2-adrenergic receptors: delineation of domains involved in effector coupling and ligand binding specificity. Science 1 1988 1310 1316
    • (1988) Science , vol.1 , pp. 1310-1316
    • Kobilka, B.K.1    Kobilka, T.S.2    Daniel, K.3    Regan, J.W.4    Caron, M.J.5    Lefkowitz, R.J.6
  • 18
    • 0025600997 scopus 로고
    • Distinct sequence elements control the specificity of G protein activation by muscarinic acetylcholine receptor subtypes.
    • J. Lechleiter K. Duerson D. Ennulat N. David D. Clapham E. Peralta Distinct sequence elements control the specificity of G protein activation by muscarinic acetylcholine receptor subtypes. EMBO J. 1 1990 4381 4390
    • (1990) EMBO J. , vol.1 , pp. 4381-4390
    • Lechleiter, J.1    Duerson, K.2    Ennulat, D.3    David, N.4    Clapham, D.5    Peralta, E.6
  • 19
    • 0029096818 scopus 로고
    • Mutational analysis of the relative orientation of transmembrane helices I and VII in G protein-coupled receptors.
    • J. Liu T. Schöneberg M. van Rhee J. Wess Mutational analysis of the relative orientation of transmembrane helices I and VII in G protein-coupled receptors. J. Biol. Chem. 1 1995 19532 19539
    • (1995) J. Biol. Chem. , vol.1 , pp. 19532-19539
    • Liu, J.1    Schöneberg, T.2    van Rhee, M.3    Wess, J.4
  • 20
    • 0029589916 scopus 로고
    • Identification of a receptor/G-protein contact site critical for signaling specificity and G-protein activation.
    • J. Liu B.R. Conklin N. Blin J. Yun J. Wess Identification of a receptor/G-protein contact site critical for signaling specificity and G-protein activation. Proc. Natl. Acad. Sci. USA 1 1995 11642 11646
    • (1995) Proc. Natl. Acad. Sci. USA , vol.1 , pp. 11642-11646
    • Liu, J.1    Conklin, B.R.2    Blin, N.3    Yun, J.4    Wess, J.5
  • 21
    • 0027533276 scopus 로고
    • Reconstitution of functional muscarinic receptors by coexpression of amino and carboxyl terminal receptor fragments.
    • R. Maggio Z. Vogel J. Wess Reconstitution of functional muscarinic receptors by coexpression of amino and carboxyl terminal receptor fragments. FEBS Lett. 1 1993 195 200
    • (1993) FEBS Lett. , vol.1 , pp. 195-200
    • Maggio, R.1    Vogel, Z.2    Wess, J.3
  • 22
    • 0027467848 scopus 로고
    • Coexpression studies with mutant muscarinic/adrenergic receptors provide evidence for intermolecular crosstalk between G protein-linked receptors.
    • R. Maggio Z. Vogel J. Wess Coexpression studies with mutant muscarinic/adrenergic receptors provide evidence for intermolecular crosstalk between G protein-linked receptors. Proc. Natl. Acad. Sci. USA 1 1993 3103 3107
    • (1993) Proc. Natl. Acad. Sci. USA , vol.1 , pp. 3103-3107
    • Maggio, R.1    Vogel, Z.2    Wess, J.3
  • 23
    • 0028815463 scopus 로고
    • Probing of the location of the allosteric site on ml muscarinic receptors by site-directed mutagenesis.
    • H. Matsui S. Lazareno N.J.M. Birdsall Probing of the location of the allosteric site on ml muscarinic receptors by site-directed mutagenesis. Mol. Pharmacol. 1 1995 88 98
    • (1995) Mol. Pharmacol. , vol.1 , pp. 88-98
    • Matsui, H.1    Lazareno, S.2    Birdsall, N.J.M.3
  • 24
    • 0027479116 scopus 로고
    • Serine-and threonine-rich domain regulates internalization of muscarinic cholinergic receptors.
    • O. Moro J. Lameh W. Sadee Serine-and threonine-rich domain regulates internalization of muscarinic cholinergic receptors. J. Biol. Chem. 1 1993 6862 6865
    • (1993) J. Biol. Chem. , vol.1 , pp. 6862-6865
    • Moro, O.1    Lameh, J.2    Sadee, W.3
  • 26
    • 0026086012 scopus 로고
    • Reconstitutively active G protein-coupled receptors purified from baculovirus-infected insect cells.
    • E.M. Parker K. Kameyama T. Higashijima E.M. Ross Reconstitutively active G protein-coupled receptors purified from baculovirus-infected insect cells. J. Biol. Chem. 1 1991 519 527
    • (1991) J. Biol. Chem. , vol.1 , pp. 519-527
    • Parker, E.M.1    Kameyama, K.2    Higashijima, T.3    Ross, E.M.4
  • 27
    • 0023773004 scopus 로고
    • Differential regulation of PI hydrolysis and adenylyl cyclase by muscarinic receptor subtypes.
    • E.G. Peralta A. Ashkenazi J.W. Winslow J. Ramachandran D.J. Capon Differential regulation of PI hydrolysis and adenylyl cyclase by muscarinic receptor subtypes. Nature 1 1988 434 437
    • (1988) Nature , vol.1 , pp. 434-437
    • Peralta, E.G.1    Ashkenazi, A.2    Winslow, J.W.3    Ramachandran, J.4    Capon, D.J.5
  • 28
    • 0028012105 scopus 로고
    • Intramolecular interactions in muscarinic acetylcholine receptors studied with chimeric m2/m5 receptors.
    • Z. Pittel J. Wess Intramolecular interactions in muscarinic acetylcholine receptors studied with chimeric m2/m5 receptors. Mol. Pharmacol. 1 1994 61 64
    • (1994) Mol. Pharmacol. , vol.1 , pp. 61-64
    • Pittel, Z.1    Wess, J.2
  • 29
    • 0025249842 scopus 로고
    • Membrane protein folding and oligomerization: the two-stage model.
    • J.-L. Popot D.M. Engelman Membrane protein folding and oligomerization: the two-stage model. Biochemistry 1 1990 4031 4037
    • (1990) Biochemistry , vol.1 , pp. 4031-4037
    • Popot, J.-L.1    Engelman, D.M.2
  • 30
    • 0028125886 scopus 로고
    • Rhodopsin mutation G90D and a molecular mechanism for congenital night blindness.
    • V.R. Rao G.B. Cohen D.D. Oprian Rhodopsin mutation G90D and a molecular mechanism for congenital night blindness. Nature 1 1994 639 642
    • (1994) Nature , vol.1 , pp. 639-642
    • Rao, V.R.1    Cohen, G.B.2    Oprian, D.D.3
  • 31
    • 0028101036 scopus 로고
    • Synthetic peptides as probes for G protein function: carboxyl-terminal Gαs peptides mimic Gs and evoke high affinity agonist binding to β-adrenergic receptors.
    • s and evoke high affinity agonist binding to β-adrenergic receptors. J. Biol. Chem. 1 1994 21519 21525
    • (1994) J. Biol. Chem. , vol.1 , pp. 21519-21525
    • Rasenick, M.M.1    Watanabe, M.2    Lazarevic, M.B.3    Hatta, S.4    Hamm, H.E.5
  • 32
    • 0026548156 scopus 로고
    • In vitro mutagenesis and the search for structure-function relationships among G protein-coupled receptors.
    • T.M. Savarese C.M. Fraser In vitro mutagenesis and the search for structure-function relationships among G protein-coupled receptors. Biochem. J. 1 1992 1 19
    • (1992) Biochem. J. , vol.1 , pp. 1-19
    • Savarese, T.M.1    Fraser, C.M.2
  • 34
    • 0029077235 scopus 로고
    • Plasma membrane localization and functional rescue of truncated forms of a G protein-coupled receptor.
    • T. Schöneberg J. Liu J. Wess Plasma membrane localization and functional rescue of truncated forms of a G protein-coupled receptor. J. Biol. Chem. 1 1995 18000 18006
    • (1995) J. Biol. Chem. , vol.1 , pp. 18000-18006
    • Schöneberg, T.1    Liu, J.2    Wess, J.3
  • 35
    • 0027933763 scopus 로고
    • Locating ligand-binding sites in 7TM receptors by protein engineering.
    • T.W. Schwartz Locating ligand-binding sites in 7TM receptors by protein engineering. Curr. Opin. Biotechnol. 1 1994 434 444
    • (1994) Curr. Opin. Biotechnol. , vol.1 , pp. 434-444
    • Schwartz, T.W.1
  • 37
    • 0024519931 scopus 로고
    • Structural basis of β-adrenergic receptor function.
    • C.D. Strader I.S. Sigal R.A.F. Dixon Structural basis of β-adrenergic receptor function. FASEB J. 1 1989 1825 1832
    • (1989) FASEB J. , vol.1 , pp. 1825-1832
    • Strader, C.D.1    Sigal, I.S.2    Dixon, R.A.F.3
  • 39
    • 0026592867 scopus 로고
    • Identification of intramolecular interactions in adrenergic receptors.
    • S. Suryanarayana M. von Zastrow B.K. Kobilka Identification of intramolecular interactions in adrenergic receptors. J. Biol. Chem. 1 1992 21991 21994
    • (1992) J. Biol. Chem. , vol.1 , pp. 21991-21994
    • Suryanarayana, S.1    von Zastrow, M.2    Kobilka, B.K.3
  • 40
    • 0027278632 scopus 로고
    • Rapid agonist-mediated phosphorylation of m3--muscarinic receptors revealed by immunoprecipitation.
    • A.B. Tobin S.R. Nahorskl Rapid agonist-mediated phosphorylation of m3--muscarinic receptors revealed by immunoprecipitation. J. Biol. Chem. 1 1993 9817 9823
    • (1993) J. Biol. Chem. , vol.1 , pp. 9817-9823
    • Tobin, A.B.1    Nahorskl, S.R.2
  • 41
    • 0027328091 scopus 로고
    • Molecular basis of muscarinic acetylcholine receptor function.
    • J. Wess Molecular basis of muscarinic acetylcholine receptor function. Trends Pharmacol. Sci. 1 1993 308 313
    • (1993) Trends Pharmacol. Sci. , vol.1 , pp. 308-313
    • Wess, J.1
  • 42
    • 0024430081 scopus 로고
    • Identification of a small intracellular region of the muscarinic m3 receptor as a determinant of selective coupling to PI turnover.
    • J. Wess M.R. Brann T.I. Bonner Identification of a small intracellular region of the muscarinic m3 receptor as a determinant of selective coupling to PI turnover. FEBS Lett. 1 1989 133 136
    • (1989) FEBS Lett. , vol.1 , pp. 133-136
    • Wess, J.1    Brann, M.R.2    Bonner, T.I.3
  • 43
    • 0025153423 scopus 로고
    • Delineation of muscarinic receptor selectivity of coupling to guanine-nucleotide binding proteins and second messengers.
    • J. Wess T.I. Bonner F. Dorje M.R. Brann Delineation of muscarinic receptor selectivity of coupling to guanine-nucleotide binding proteins and second messengers. Mol. Pharmacol. 1 1990 517 523
    • (1990) Mol. Pharmacol. , vol.1 , pp. 517-523
    • Wess, J.1    Bonner, T.I.2    Dorje, F.3    Brann, M.R.4
  • 44
    • 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.
    • J. Wess D. Gdula M.R. Brann 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. 1 1991 3729 3734
    • (1991) EMBO J. , vol.1 , pp. 3729-3734
    • Wess, J.1    Gdula, D.2    Brann, M.R.3
  • 45
    • 0025216786 scopus 로고
    • Chimeric muscarinic cholinergic: β-adrenergic receptors that activate Gs in response to muscarinic agonists.
    • S.K.-F. Wong E.M. Parker E.M. Ross Chimeric muscarinic cholinergic: β-adrenergic receptors that activate Gs in response to muscarinic agonists. J. Biol. Chem. 1 1990 6219 6224
    • (1990) J. Biol. Chem. , vol.1 , pp. 6219-6224
    • Wong, S.K.-F.1    Parker, E.M.2    Ross, E.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.