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Volumn 50, Issue 4, 1996, Pages 985-993

Identification of the critical domains of the δ-opioid receptor involved in G protein coupling using site-specific synthetic peptides

Author keywords

[No Author keywords available]

Indexed keywords

DELTA OPIATE RECEPTOR; GUANINE NUCLEOTIDE BINDING PROTEIN; GUANOSINE 5' O (3 THIOTRIPHOSPHATE); GUANOSINE TRIPHOSPHATASE; LEUCINE ENKEPHALIN[2 DEXTRO SERINE 6 THREONINE]; OPIATE AGONIST; SYNTHETIC PEPTIDE;

EID: 0029955446     PISSN: 0026895X     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (49)

References (36)
  • 1
    • 0025758191 scopus 로고
    • Opioid receptor-coupled second messengers systems
    • Childers. S. R. Opioid receptor-coupled second messengers systems. Life Sci. 48:1991-2003 (1991).
    • (1991) Life Sci. , vol.48 , pp. 1991-2003
    • Childers, S.R.1
  • 3
    • 0027052952 scopus 로고
    • The δ-opioid receptor: Isolation of a cDNA by expression cloning and pharmacological characterization
    • Kieffer, B. L., K Befort, C. Gaveriaux-Ruff, and C. G. Hirth. The δ-opioid receptor: isolation of a cDNA by expression cloning and pharmacological characterization. Proc. Natl. Acad. Sci. USA 89:12048-12052 (1992).
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 12048-12052
    • Kieffer, B.L.1    Befort, K.2    Gaveriaux-Ruff, C.3    Hirth, C.G.4
  • 6
    • 0028985047 scopus 로고
    • Immunoprecipitation of opioid receptor-Go-protein complexes using specific GTP-binding protein antisera
    • Georgoussi, Z., G. Milligan, and C. Zioudrou. Immunoprecipitation of opioid receptor-Go-protein complexes using specific GTP-binding protein antisera. Biochem. J. 306:71-75 (1995).
    • (1995) Biochem. J. , vol.306 , pp. 71-75
    • Georgoussi, Z.1    Milligan, G.2    Zioudrou, C.3
  • 7
    • 0027403710 scopus 로고
    • μ and δ opioid receptors differentially couple to G protein subtypes in membranes of human neuroblastoma SH-SY5Y cells
    • Laugwitz, K.-L., S. Offermanns, K. Spicher, and G. Schultz. μ and δ opioid receptors differentially couple to G protein subtypes in membranes of human neuroblastoma SH-SY5Y cells. Neuron 10:233-242 (1993).
    • (1993) Neuron , vol.10 , pp. 233-242
    • Laugwitz, K.-L.1    Offermanns, S.2    Spicher, K.3    Schultz, G.4
  • 8
    • 0026071908 scopus 로고
    • Structure/function relationship of proteins belonging to the family of receptors coupled to GTP-binding proteins
    • Strosberg, A. D. Structure/function relationship of proteins belonging to the family of receptors coupled to GTP-binding proteins. Eur. J. Biochem. 196:1-10 (1991).
    • (1991) Eur. J. Biochem. , vol.196 , pp. 1-10
    • Strosberg, A.D.1
  • 9
    • 0026548156 scopus 로고
    • In vitro mutagenesis and the search for structure-function relationships among G protein-coupled receptors
    • Savarase, T. M., and C. M. Fraser. In vitro mutagenesis and the search for structure-function relationships among G protein-coupled receptors. Biochem. J. 283:1-19 (1992).
    • (1992) Biochem. J. , vol.283 , pp. 1-19
    • Savarase, T.M.1    Fraser, C.M.2
  • 10
    • 0026575003 scopus 로고
    • Discrete amino acid sequences of the α1-adrenergic receptor determine the selectivity of coupling to phosphatidylinositol hydrolysis
    • Cotecchia, S., J. Ostrowski, M. A. Kjelsberg, M. G. Caron, and R. J. Lefkowitz. Discrete amino acid sequences of the α1-adrenergic receptor determine the selectivity of coupling to phosphatidylinositol hydrolysis. J. Biol. Chem. 267:1633-1639 (1992).
    • (1992) J. Biol. Chem. , vol.267 , pp. 1633-1639
    • Cotecchia, S.1    Ostrowski, J.2    Kjelsberg, M.A.3    Caron, M.G.4    Lefkowitz, R.J.5
  • 11
    • 0025212680 scopus 로고
    • Regions of the α1-adrenergic receptor involved in coupling to phosphatidylinositol hydrolysis and enhanced sensitivity of biological function
    • Cotecchia, S., S. Exum, M. G. Caron, and R. J. Lefkowitz. Regions of the α1-adrenergic receptor involved in coupling to phosphatidylinositol hydrolysis and enhanced sensitivity of biological function. Proc. Natl. Acad. Sci. USA 87:2896-2900 (1990).
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 2896-2900
    • Cotecchia, S.1    Exum, S.2    Caron, M.G.3    Lefkowitz, R.J.4
  • 12
    • 0028013155 scopus 로고
    • Domains of the human neutrophil N-formyl peptide receptor involved in G protein coupling
    • Schreider, R. E., E. R. Prossnitz, R. D. Ye, C. G. Cochrane, and G. M. Bokoch. Domains of the human neutrophil N-formyl peptide receptor involved in G protein coupling. J. Biol. Chem. 269:326-331 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 326-331
    • Schreider, R.E.1    Prossnitz, E.R.2    Ye, R.D.3    Cochrane, C.G.4    Bokoch, G.M.5
  • 14
    • 0028172426 scopus 로고
    • Binding of an α2-adrenergic receptor third intracellular loop peptide to Gβ and the amino terminus of Ga
    • Taylor, J. M., G. G. Jacob-Mosier, R. G. Lawton, A. E. Remmers, and R. R. Neubig. Binding of an α2-adrenergic receptor third intracellular loop peptide to Gβ and the amino terminus of Ga. J. Biol. Chem. 269:27618-27624 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 27618-27624
    • Taylor, J.M.1    Jacob-Mosier, G.G.2    Lawton, R.G.3    Remmers, A.E.4    Neubig, R.R.5
  • 15
    • 0025882303 scopus 로고
    • Multisite contacts involved in coupling of the β-adrenergic receptor with the stimulatory guanine nucleotide binding regulatory protein
    • Munch, G., C. Dees, M. Hekman, and D. Palm. Multisite contacts involved in coupling of the β-adrenergic receptor with the stimulatory guanine nucleotide binding regulatory protein. Eur. J. Biochem. 198:357-364 (1991).
    • (1991) Eur. J. Biochem. , vol.198 , pp. 357-364
    • Munch, G.1    Dees, C.2    Hekman, M.3    Palm, D.4
  • 16
    • 0025817671 scopus 로고
    • Two peptides from the α2A-adrenergic receptor alter receptor G protein coupling by distinct mechanisms
    • Dalman, H. M., and R. R Neubig. Two peptides from the α2A-adrenergic receptor alter receptor G protein coupling by distinct mechanisms. J. Biol. Chem. 266:11025-11029 (1991).
    • (1991) J. Biol. Chem. , vol.266 , pp. 11025-11029
    • Dalman, H.M.1    Neubig, R.R.2
  • 19
    • 0029958767 scopus 로고    scopus 로고
    • Analysis of inverse agonism at the δ-opioid receptor following expression in Rat 1 fibroblasts
    • Mullaney, I., C. Carr, and G. Milligan. Analysis of inverse agonism at the δ-opioid receptor following expression in Rat 1 fibroblasts. Biochem. J. 315:227-234 (1996).
    • (1996) Biochem. J. , vol.315 , pp. 227-234
    • Mullaney, I.1    Carr, C.2    Milligan, G.3
  • 20
    • 0023655416 scopus 로고
    • Foetal-calf serum stimulates a pertussis-toxin-sensitive highaffinity GTPase activity in rat glioma C6 BU1 cells
    • Milligan, G. Foetal-calf serum stimulates a pertussis-toxin-sensitive highaffinity GTPase activity in rat glioma C6 BU1 cells. Biochem. J. 245:501-505 (1987).
    • (1987) Biochem. J. , vol.245 , pp. 501-505
    • Milligan, G.1
  • 21
    • 0025239605 scopus 로고
    • 8δ-Opioid receptor-mediated inhibition of adenylate cyclase is transduced specifically by the guanine-nucleotide-binding protein Gi2
    • McKenzie, F. R., and G. Milligan. 8δ-Opioid receptor-mediated inhibition of adenylate cyclase is transduced specifically by the guanine-nucleotide-binding protein Gi2. Biochem. J. 267:391-398 (1990).
    • (1990) Biochem. J. , vol.267 , pp. 391-398
    • McKenzie, F.R.1    Milligan, G.2
  • 22
    • 0021039424 scopus 로고
    • A practical computer based approach to the analysis of radioligand binding experiments
    • McPherson, G. A. A practical computer based approach to the analysis of radioligand binding experiments. Comput. Programs Biomed. 17:107-113 (1983).
    • (1983) Comput. Programs Biomed. , vol.17 , pp. 107-113
    • McPherson, G.A.1
  • 23
    • 0025925067 scopus 로고
    • Identification of a Gs activator region of the β2-adrenergic receptor that is autoregulated via protein kinase A-dependent phosphorylation
    • E
    • Okamoto, T., Y. Murayama, Y. Hayashi, M. Inagaki, E. Ogata, E, and I. Nishimoto. Identification of a Gs activator region of the β2-adrenergic receptor that is autoregulated via protein kinase A-dependent phosphorylation. Cell 67:723-730 (1991).
    • (1991) Cell , vol.67 , pp. 723-730
    • Okamoto, T.1    Murayama, Y.2    Hayashi, Y.3    Inagaki, M.4    Ogata, E.5    Nishimoto, I.6
  • 24
    • 0024787617 scopus 로고
    • Muscarinic acetylcholine receptor-stimulated binding of guanosine-5′-O-(3-thiotriphosphate) to guaninenucleotide-binding proteins in cardiac membranes
    • Hilf, G., P. Gierschik, and K. H. Jacobs. Muscarinic acetylcholine receptor-stimulated binding of guanosine-5′-O-(3-thiotriphosphate) to guaninenucleotide-binding proteins in cardiac membranes. Biochem. J. 186:725-731 (1989).
    • (1989) Biochem. J. , vol.186 , pp. 725-731
    • Hilf, G.1    Gierschik, P.2    Jacobs, K.H.3
  • 25
    • 0025644753 scopus 로고
    • Inhibition of calcium currents by noradrenaline, somatostatin and opioids in quinea-pig submucosal neurones
    • Surprenant, A., K. Z. Shen, A. R North, and H. Tatsumi. Inhibition of calcium currents by noradrenaline, somatostatin and opioids in quinea-pig submucosal neurones. J. Physiol. (LOnd.) 431:585-608 (1990).
    • (1990) J. Physiol. (LOnd.) , vol.431 , pp. 585-608
    • Surprenant, A.1    Shen, K.Z.2    North, A.R.3    Tatsumi, H.4
  • 26
    • 0024414931 scopus 로고
    • Mapping of β-adrenoceptor coupling domains to Gs-protein by site-specific synthetic peptides
    • Palm, D., G. Münch, C. Dees, and M. Hekman. Mapping of β-adrenoceptor coupling domains to Gs-protein by site-specific synthetic peptides. FEBS Lett. 254:89-93 (1989).
    • (1989) FEBS Lett. , vol.254 , pp. 89-93
    • Palm, D.1    Münch, G.2    Dees, C.3    Hekman, M.4
  • 27
    • 0026630552 scopus 로고
    • Detection of G protein-activator regions in M4 subtype muscarinic cholinergic, and α2-adrenergic receptors based upon characteristics in primary structure
    • Okamoto, T., and I. Nishimoto. Detection of G protein-activator regions in M4 subtype muscarinic cholinergic, and α2-adrenergic receptors based upon characteristics in primary structure. J. Biol. Chem. 267:8342-8346 (1992).
    • (1992) J. Biol. Chem. , vol.267 , pp. 8342-8346
    • Okamoto, T.1    Nishimoto, I.2
  • 28
    • 0027379660 scopus 로고
    • Hydrophobic amino acid in the i2 loop plays a key role in receptor-G protein coupling
    • Moro, O., J. Lameh, P. Hogger, and W. Sadee. Hydrophobic amino acid in the i2 loop plays a key role in receptor-G protein coupling. J. Biol. Chem. 268:22273-22276 (1993).
    • (1993) J. Biol. Chem. , vol.268 , pp. 22273-22276
    • Moro, O.1    Lameh, J.2    Hogger, P.3    Sadee, W.4
  • 29
    • 0028296886 scopus 로고
    • A C-terminal peptide of bovine thodopsin binds to the transducin and facilitates its activation
    • Phillips, W. J., and R. A. Cerione. A C-terminal peptide of bovine thodopsin binds to the transducin and facilitates its activation. Biochem. J. 299:351-357 (1994).
    • (1994) Biochem. J. , vol.299 , pp. 351-357
    • Phillips, W.J.1    Cerione, R.A.2
  • 31
    • 0027352613 scopus 로고
    • Interaction of rhodopsin with the G-protein transducin
    • Hargrave, P. A., H. E. Hamm, and K. P. Hofmann. Interaction of rhodopsin with the G-protein transducin. Bioassays 15:43-50 (1993).
    • (1993) Bioassays , vol.15 , pp. 43-50
    • Hargrave, P.A.1    Hamm, H.E.2    Hofmann, K.P.3
  • 32
    • 0027456328 scopus 로고
    • Amphipathic α-helical structure does not predict the ability of receptor-derived synthetic peptides to interact with guanine nucleotide-binding regulatory proteins
    • Voss, T., E. Wallner, A. P. Czernilofsky, and M. Freissmuth. Amphipathic α-helical structure does not predict the ability of receptor-derived synthetic peptides to interact with guanine nucleotide-binding regulatory proteins. J. Biol Chem. 268:4637-4642 (1993).
    • (1993) J. Biol Chem. , vol.268 , pp. 4637-4642
    • Voss, T.1    Wallner, E.2    Czernilofsky, A.P.3    Freissmuth, M.4
  • 33
    • 0027422737 scopus 로고
    • Specificity of receptor-G protein interactions: Searching for the structure behind the signal
    • Hedin, K. E., K. Duerson, and D. E. Clapham. Specificity of receptor-G protein interactions: searching for the structure behind the signal. Cell. Signal. 5:505-518 (1993).
    • (1993) Cell. Signal. , vol.5 , pp. 505-518
    • Hedin, K.E.1    Duerson, K.2    Clapham, D.E.3
  • 34
    • 0023859049 scopus 로고
    • Two adjacent cysteine residues in the C-terminal cytoplasmic fragment of bovine rhodopsin are palmitylated
    • Ovchinnikov, V. A., N. G. Abdulaev, and A. S. Bogachuk. Two adjacent cysteine residues in the C-terminal cytoplasmic fragment of bovine rhodopsin are palmitylated. FEBS Lett. 230:1-5 (1988).
    • (1988) FEBS Lett. , vol.230 , pp. 1-5
    • Ovchinnikov, V.A.1    Abdulaev, N.G.2    Bogachuk, A.S.3
  • 36
    • 0027248974 scopus 로고
    • The role of the third intracellular loop of the neutrophil N-formyl peptide receptor in G protein coupling
    • Prossnitz, E. R., O. Quehenberger, C. G. Cochrane, and R. D. Ye. The role of the third intracellular loop of the neutrophil N-formyl peptide receptor in G protein coupling. Biochem. J. 294:581-587 (1993).
    • (1993) Biochem. J. , vol.294 , pp. 581-587
    • Prossnitz, E.R.1    Quehenberger, O.2    Cochrane, C.G.3    Ye, R.D.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.