메뉴 건너뛰기




Volumn 19, Issue 16, 2000, Pages 4265-4271

Dominant-negative activity of an α(1β)-adrenergic receptor signal-inactivating point mutation

Author keywords

Constitutive activity; G protein coupled receptor; Inositol phosphate signalling

Indexed keywords

ALPHA 1B ADRENERGIC RECEPTOR; ASPARAGINE; GLYCINE; GUANINE NUCLEOTIDE BINDING PROTEIN; PHENYLALANINE;

EID: 0034663812     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (34)

References (25)
  • 1
    • 0029815140 scopus 로고    scopus 로고
    • Modulation of GDP release from transducin by the conserved Glu134-Arg135 sequence in rhodopsin
    • Acharya, S. and Karnik, S.S. (1996) Modulation of GDP release from transducin by the conserved Glu134-Arg135 sequence in rhodopsin. J. Biol. Chem., 271, 25406-25411.
    • (1996) J. Biol. Chem. , vol.271 , pp. 25406-25411
    • Acharya, S.1    Karnik, S.S.2
  • 2
    • 0030949485 scopus 로고    scopus 로고
    • Markedly reduced activity of mutant calcium-sensing receptor with an inserted alu element from a kindred with familial hypocalciuric hypercalcemia and neonatal severe hyperparathyroidism
    • Bai, M., Janicic, N., Trivedi, S., Quinn, S.J., Cole, D.E.C., Brown, E.M. and Hendy, G.N. (1997) Markedly reduced activity of mutant calcium-sensing receptor with an inserted Alu element from a kindred with familial hypocalciuric hypercalcemia and neonatal severe hyperparathyroidism. J. Clin. Invest., 99, 1917-1925.
    • (1997) J. Clin. Invest. , vol.99 , pp. 1917-1925
    • Bai, M.1    Janicic, N.2    Trivedi, S.3    Quinn, S.J.4    Cole, D.E.C.5    Brown, E.M.6    Hendy, G.N.7
  • 3
    • 0028168350 scopus 로고
    • 2A-adrenergic receptor to multiple G-proteins. A simple approach for estimating receptor-g-protein coupling efficiency in a transient expression system
    • 2A-adrenergic receptor to multiple G-proteins. A simple approach for estimating receptor-G-protein coupling efficiency in a transient expression system. J. Biol. Chem., 269, 5730-5734.
    • (1994) J. Biol. Chem. , vol.269 , pp. 5730-5734
    • Chabre, O.1    Conklin, B.R.2    Brandon, S.3    Bourne, H.R.4    Limbird, L.E.5
  • 4
    • 0033522643 scopus 로고    scopus 로고
    • 1B-adrenergic receptor is a key switch residue involved in activation and catecholamine ring aromatic bonding
    • 1B-adrenergic receptor is a key switch residue involved in activation and catecholamine ring aromatic bonding. J. Biol. Chem., 274, 16320-16330.
    • (1999) J. Biol. Chem. , vol.274 , pp. 16320-16330
    • Chen, S.1    Xu, M.2    Lin, F.3    Lee, D.4    Riek, P.5    Graham, R.M.6
  • 5
    • 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
  • 7
    • 0029894423 scopus 로고    scopus 로고
    • 1 arrest response in cells expressing an inappropriate pheromone receptor
    • 1 arrest response in cells expressing an inappropriate pheromone receptor. Mol. Cell. Biol., 16, 4478-4485.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 4478-4485
    • Couve, A.1    Hirsch, J.P.2
  • 8
    • 0028235604 scopus 로고
    • The evolution and structure of aminergic G protein-coupled receptors
    • Donnelly, D., Findlay, J.B.C. and Blundell, T.L. (1994) The evolution and structure of aminergic G protein-coupled receptors. Receptors Channels, 2, 61-78.
    • (1994) Receptors Channels , vol.2 , pp. 61-78
    • Donnelly, D.1    Findlay, J.B.C.2    Blundell, T.L.3
  • 9
    • 0031705403 scopus 로고    scopus 로고
    • Dominant-negative mutations in the G-protein-coupled α-factor receptor map to the extracellular ends of the transmembrane segments
    • Dosil, M., Giot, L., Davis, C. and Konopka, J.B. (1998) Dominant-negative mutations in the G-protein-coupled α-factor receptor map to the extracellular ends of the transmembrane segments. Mol. Cell. Biol., 18, 5981-5991.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 5981-5991
    • Dosil, M.1    Giot, L.2    Davis, C.3    Konopka, J.B.4
  • 10
    • 0028946950 scopus 로고
    • Characterisation of rhodopsin mutants that bind tranducin but fail to induce GTP nucleotide uptake. Classification of mutant pigments by fluorescence, nucleotide release and flash-induced light-scattering assays
    • Ernst, O.P., Hofman, K.P. and Sakmar, T.P. (1995) Characterisation of rhodopsin mutants that bind tranducin but fail to induce GTP nucleotide uptake. Classification of mutant pigments by fluorescence, nucleotide release and flash-induced light-scattering assays. J. Biol. Chem., 270, 10580-10586.
    • (1995) J. Biol. Chem. , vol.270 , pp. 10580-10586
    • Ernst, O.P.1    Hofman, K.P.2    Sakmar, T.P.3
  • 11
    • 0029907599 scopus 로고    scopus 로고
    • Requirement of rigid-body motion of transmembrane helices for light activation of rhodopsin
    • Farrens, D.L., Altenhach, 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    Altenhach, C.2    Yang, K.3    Hubbell, W.L.4    Khorana, H.G.5
  • 12
    • 0025036350 scopus 로고
    • Rhodopsin mutants that bind hut fail to activate transducin
    • Franke, R.R., Konig, B., Sakmar, T.P., Khorana, H.G. and Hofmann, K.P. (1990) Rhodopsin mutants that bind hut fail to activate transducin. Science, 250, 123-125.
    • (1990) Science , vol.250 , pp. 123-125
    • Franke, R.R.1    Konig, B.2    Sakmar, T.P.3    Khorana, H.G.4    Hofmann, K.P.5
  • 14
    • 0029874397 scopus 로고    scopus 로고
    • 1-adrenergic receptor subtypes. Molecular structure, function and signalling
    • 1-Adrenergic receptor subtypes. Molecular structure, function and signalling. Circ. Res., 78, 737-749.
    • (1996) Circ. Res. , vol.78 , pp. 737-749
    • Graham, R.M.1    Perez, D.M.2    Hwa, J.3    Piascik, M.J.4
  • 15
    • 0031446639 scopus 로고    scopus 로고
    • Inhibition of gonadotropin-releasing hormone receptor signalling by expression of a splice variant of the human receptor
    • Grosse, R., Schoneberg, T., Schultz, G. and Gudermann, T. (1997) Inhibition of gonadotropin-releasing hormone receptor signalling by expression of a splice variant of the human receptor. Mol. Endocrinol., 11, 1305-1318.
    • (1997) Mol. Endocrinol. , vol.11 , pp. 1305-1318
    • Grosse, R.1    Schoneberg, T.2    Schultz, G.3    Gudermann, T.4
  • 16
    • 0029730779 scopus 로고    scopus 로고
    • Functional interaction of transmembrane helices 3 and 6 in rhodopsin. Replacement of phenylalanine 261 by alanine causes reversion of phenotype of a glycine 121 replacement mutant
    • Han, M., Lin, S.W., Minkova, M., Smith, S.O. and Sakmar, T.P. (1996) Functional interaction of transmembrane helices 3 and 6 in rhodopsin. Replacement of phenylalanine 261 by alanine causes reversion of phenotype of a glycine 121 replacement mutant. J. Biol. Chem., 271, 32337-32342.
    • (1996) J. Biol. Chem. , vol.271 , pp. 32337-32342
    • Han, M.1    Lin, S.W.2    Minkova, M.3    Smith, S.O.4    Sakmar, T.P.5
  • 17
    • 0032570306 scopus 로고    scopus 로고
    • A cluster of aromatic residues in the sixth membrane-spanning segment of the dopamine D2 receptor is accessible in the binding-site crevice
    • Javitch, J.A., Ballesteros, J.A., Weinstein, H. and Chen, J. (1998) A cluster of aromatic residues in the sixth membrane-spanning segment of the dopamine D2 receptor is accessible in the binding-site crevice. Biochemistry, 37, 998-1006.
    • (1998) Biochemistry , vol.37 , pp. 998-1006
    • Javitch, J.A.1    Ballesteros, J.A.2    Weinstein, H.3    Chen, J.4
  • 18
    • 0026058365 scopus 로고
    • A dominant negative mutation suppresses the function of normal epidermal growth factor receptors by heterodimerization
    • Kashles, O., Yarden, Y., Fischer, R., Ullrich, A. and Schlessinger, J. (1991) A dominant negative mutation suppresses the function of normal epidermal growth factor receptors by heterodimerization. Mol. Cell. Biol., 11, 1454-1463.
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 1454-1463
    • Kashles, O.1    Yarden, Y.2    Fischer, R.3    Ullrich, A.4    Schlessinger, J.5
  • 19
    • 0029900790 scopus 로고    scopus 로고
    • Mutation of Pro-258 in transmembrane domain 6 constitutively activates the G-protein-coupled α-factor receptor
    • Konopka, J.B., Margartt, S.M. and Dube, P. (1996) Mutation of Pro-258 in transmembrane domain 6 constitutively activates the G-protein-coupled α-factor receptor. Proc. Natl Acad. Sci. USA, 93, 6764-6769.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 6764-6769
    • Konopka, J.B.1    Margartt, S.M.2    Dube, P.3
  • 20
    • 0031037632 scopus 로고    scopus 로고
    • The role of the aspartate-arginine-tyrosine triad in the m1 muscarinic receptor: Mutations of aspartate 122 and tyrosine 124 decrease receptor expression hut do not abolish signalling
    • Lu, Z.L., Curtis, C.A., Jones, P.G., Pavia, J. and Hulme, E.C. (1997) The role of the aspartate-arginine-tyrosine triad in the m1 muscarinic receptor: mutations of aspartate 122 and tyrosine 124 decrease receptor expression hut do not abolish signalling. Mol. Pharmacol., 51, 234-241.
    • (1997) Mol. Pharmacol. , vol.51 , pp. 234-241
    • Lu, Z.L.1    Curtis, C.A.2    Jones, P.G.3    Pavia, J.4    Hulme, E.C.5
  • 22
    • 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
  • 23
    • 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
  • 24
    • 0030600396 scopus 로고    scopus 로고
    • Follitropin signal transduction: Alternative splicing of the FSH receptor gene produces a dominant negative form of receptor which inhibits hormone action
    • Sairam, M.R., Jiang, L.G., Yarney, T.A. and Khan, H. (1996) Follitropin signal transduction: alternative splicing of the FSH receptor gene produces a dominant negative form of receptor which inhibits hormone action. Biochem. Biophys. Res. Commun., 226, 717-722.
    • (1996) Biochem. Biophys. Res. Commun. , vol.226 , pp. 717-722
    • Sairam, M.R.1    Jiang, L.G.2    Yarney, T.A.3    Khan, H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.