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Volumn 66, Issue 5, 2004, Pages 1123-1137

Multiple interactions between transmembrane helices generate the oligomeric α1b-adrenoceptor

Author keywords

[No Author keywords available]

Indexed keywords

ADRENERGIC RECEPTOR; ALPHA1B ADRENORECEPTOR; GLYCOPHORIN A; MEMBRANE PROTEIN; UNCLASSIFIED DRUG;

EID: 6944234943     PISSN: 0026895X     EISSN: None     Source Type: Journal    
DOI: 10.1124/mol.104.001586     Document Type: Article
Times cited : (93)

References (47)
  • 3
    • 0035933747 scopus 로고    scopus 로고
    • 2 receptor dimer formation: Evidence from ligand binding
    • 2 receptor dimer formation: evidence from ligand binding. J Biol Chem 276:22621-22629.
    • (2001) J Biol Chem , vol.276 , pp. 22621-22629
    • Armstrong, D.1    Strange, P.G.2
  • 4
    • 0037077208 scopus 로고    scopus 로고
    • Monitoring of ligand-independent dimerization and ligand-induced conformational changes of melatonin receptors in living cells by bioluminescence resonance energy transfer
    • Ayoub MA, Couturier C, Lucas-Meunier E, Angers S, Fossier P, Bouvier M, and Jockers R (2002) Monitoring of ligand-independent dimerization and ligand-induced conformational changes of melatonin receptors in living cells by bioluminescence resonance energy transfer. J Biol Chem 277:21522-21528.
    • (2002) J Biol Chem , vol.277 , pp. 21522-21528
    • Ayoub, M.A.1    Couturier, C.2    Lucas-Meunier, E.3    Angers, S.4    Fossier, P.5    Bouvier, M.6    Jockers, R.7
  • 5
    • 0038392702 scopus 로고    scopus 로고
    • Structure-based analysis of GPCR function: Evidence for a novel pentameric assembly between the dimeric leukotriene B4 receptor BLT1 and the G-protein
    • Baneres JL and Parello J (2003) Structure-based analysis of GPCR function: evidence for a novel pentameric assembly between the dimeric leukotriene B4 receptor BLT1 and the G-protein. J Mol Biol 329:815-829.
    • (2003) J Mol Biol , vol.329 , pp. 815-829
    • Baneres, J.L.1    Parello, J.2
  • 7
    • 0142149074 scopus 로고    scopus 로고
    • Dimers of class A G protein-coupled receptors function via agonist-mediated trans-activation of associated G proteins
    • Carrillo JJ, Pediani J, and Milligan G (2003) Dimers of class A G protein-coupled receptors function via agonist-mediated trans-activation of associated G proteins. J Biol Chem 278:42578-42587.
    • (2003) J Biol Chem , vol.278 , pp. 42578-42587
    • Carrillo, J.J.1    Pediani, J.2    Milligan, G.3
  • 8
    • 0035930602 scopus 로고    scopus 로고
    • Agonist-dependent dissociation of oligomeric complexes of G protein-coupled cholecystokinin receptors demonstrated in living cells using bioluminescence resonance energy transfer
    • Cheng ZJ and Miller LJ (2001) Agonist-dependent dissociation of oligomeric complexes of G protein-coupled cholecystokinin receptors demonstrated in living cells using bioluminescence resonance energy transfer. J Biol Chem 276:48040-48047.
    • (2001) J Biol Chem , vol.276 , pp. 48040-48047
    • Cheng, Z.J.1    Miller, L.J.2
  • 10
    • 0030760634 scopus 로고    scopus 로고
    • Dimerization of the δ opioid receptor: Implication for a role in receptor internalization
    • Cvejic S and Devi LA (1997) Dimerization of the δ opioid receptor: implication for a role in receptor internalization. J Biol Chem 273:26959-26964.
    • (1997) J Biol Chem , vol.273 , pp. 26959-26964
    • Cvejic, S.1    Devi, L.A.2
  • 11
    • 0037105663 scopus 로고    scopus 로고
    • Silencing of secretin receptor function by dimerization with a misspliced variant secretin receptor in ductal pancreatic adenocarcinoma
    • Ding WQ, Cheng ZJ, McElhiney J, Kuntz SM, and Miller LJ (2002) Silencing of secretin receptor function by dimerization with a misspliced variant secretin receptor in ductal pancreatic adenocarcinoma. Cancer Res 62:5223-5229.
    • (2002) Cancer Res , vol.62 , pp. 5223-5229
    • Ding, W.Q.1    Cheng, Z.J.2    McElhiney, J.3    Kuntz, S.M.4    Miller, L.J.5
  • 12
    • 0038170289 scopus 로고    scopus 로고
    • Applications of novel resonance energy transfer techniques to study dynamic hormone receptor interactions in living cells
    • Eidne KA, Kroeger KM, and Hanyaloglu AC (2002) Applications of novel resonance energy transfer techniques to study dynamic hormone receptor interactions in living cells. Trends Endocrinol Metabol 13:415-421.
    • (2002) Trends Endocrinol Metabol , vol.13 , pp. 415-421
    • Eidne, K.A.1    Kroeger, K.M.2    Hanyaloglu, A.C.3
  • 13
    • 0036997276 scopus 로고    scopus 로고
    • Structural models for dimerization of G-protein coupled receptors: The opioid receptor homodimers
    • Filizola M and Weinstein H (2002) Structural models for dimerization of G-protein coupled receptors: the opioid receptor homodimers. Biopolymers 68:317-325.
    • (2002) Biopolymers , vol.68 , pp. 317-325
    • Filizola, M.1    Weinstein, H.2
  • 14
    • 0036780743 scopus 로고    scopus 로고
    • G-protein-coupled receptor oligomerization and its potential for drug discovery
    • George SR, O'Dowd BF, and Lee SP (2002) G-protein-coupled receptor oligomerization and its potential for drug discovery. Nat Rev Drug Discov 1:808-820.
    • (2002) Nat Rev Drug Discov , vol.1 , pp. 808-820
    • George, S.R.1    O'Dowd, B.F.2    Lee, S.P.3
  • 15
    • 0038576278 scopus 로고    scopus 로고
    • The fourth transmembrane segment forms the interface of the dopamine d2 receptor homodimer
    • Guo W, Shi L, and Javitch JA (2003) The fourth transmembrane segment forms the interface of the dopamine d2 receptor homodimer. J Biol Chem 278:4385-4388.
    • (2003) J Biol Chem , vol.278 , pp. 4385-4388
    • Guo, W.1    Shi, L.2    Javitch, J.A.3
  • 17
    • 0033578005 scopus 로고    scopus 로고
    • G-protein-coupled receptor heterodimerization modulates receptor function
    • Jordan BA and Devi LA (1999) G-protein-coupled receptor heterodimerization modulates receptor function. Nature (Lond) 399:697-700.
    • (1999) Nature (Lond) , vol.399 , pp. 697-700
    • Jordan, B.A.1    Devi, L.A.2
  • 18
    • 0033798153 scopus 로고    scopus 로고
    • 3 receptor interacts with itself and the truncated D3 splice variant d3nf: D3-D3nf interaction causes mislocalization of D3 receptors
    • 3 receptor interacts with itself and the truncated D3 splice variant d3nf: D3-D3nf interaction causes mislocalization of D3 receptors. Mol Pharmacol 58:677-683.
    • (2000) Mol Pharmacol , vol.58 , pp. 677-683
    • Karpa, K.D.1    Lin, R.2    Kabbani, N.3    Levenson, R.4
  • 19
    • 0041315589 scopus 로고    scopus 로고
    • C5a receptor oligomerization. I. Disulfide trapping reveals oligomers and potential contact surfaces in a G protein-coupled receptor
    • Klco JM, Lassere TB, and Baranski TJ (2003) C5a receptor oligomerization. I. Disulfide trapping reveals oligomers and potential contact surfaces in a G protein-coupled receptor. J Biol Chem 278:35345-35353.
    • (2003) J Biol Chem , vol.278 , pp. 35345-35353
    • Klco, J.M.1    Lassere, T.B.2    Baranski, T.J.3
  • 20
    • 0023889603 scopus 로고
    • Chimeric alpha 2-,beta 2-adrenergic receptors: Delineation of domains involved in effector coupling and ligand binding specificity
    • Kobilka BK, Kobilka TS, Daniel K, Regan JW, Caron MG, and Lefkowitz RJ (1988) Chimeric alpha 2-,beta 2-adrenergic receptors: delineation of domains involved in effector coupling and ligand binding specificity. Science (Wash DC) 240:1310-1316.
    • (1988) Science (Wash DC) , vol.240 , pp. 1310-1316
    • Kobilka, B.K.1    Kobilka, T.S.2    Daniel, K.3    Regan, J.W.4    Caron, M.G.5    Lefkowitz, R.J.6
  • 22
    • 0037013328 scopus 로고    scopus 로고
    • Two defective heterozygous luteinizing hormone receptors can rescue hormone action
    • Lee C, Ji I, Ryu K, Song Y, Conn PM, and Ji TH (2002) Two defective heterozygous luteinizing hormone receptors can rescue hormone action. J Biol Chem 277:15795-15800.
    • (2002) J Biol Chem , vol.277 , pp. 15795-15800
    • Lee, C.1    Ji, I.2    Ryu, K.3    Song, Y.4    Conn, P.M.5    Ji, T.H.6
  • 24
    • 0141431029 scopus 로고    scopus 로고
    • D2 dopamine receptor homodimerization is mediated by multiple sites of interaction, including an intermolecular interaction involving transmembrane domain 4
    • Lee SP, O'Dowd BF, Rajaram RD, Nguyen T, and George SR (2003) D2 dopamine receptor homodimerization is mediated by multiple sites of interaction, including an intermolecular interaction involving transmembrane domain 4. Biochemistry 42:11023-11031.
    • (2003) Biochemistry , vol.42 , pp. 11023-11031
    • Lee, S.P.1    O'Dowd, B.F.2    Rajaram, R.D.3    Nguyen, T.4    George, S.R.5
  • 25
    • 0038159530 scopus 로고    scopus 로고
    • Organization of the G protein-coupled receptors rhodopsin and opsin in native membranes
    • Liang Y, Fotiadis D, Filipek S, Saperstein DA, Palczewski K, and Engel A (2003) Organization of the G protein-coupled receptors rhodopsin and opsin in native membranes. J Biol Chem 278:21655-21662.
    • (2003) J Biol Chem , vol.278 , pp. 21655-21662
    • Liang, Y.1    Fotiadis, D.2    Filipek, S.3    Saperstein, D.A.4    Palczewski, K.5    Engel, A.6
  • 26
    • 0033547819 scopus 로고    scopus 로고
    • Assembly of G protein-coupled receptors from fragments: Identification of functional receptors with discontinuities in each of the loops connecting transmembrane segments
    • Martin NP, Leavitt LM, Sommers CM, and Dumont ME (1999) Assembly of G protein-coupled receptors from fragments: identification of functional receptors with discontinuities in each of the loops connecting transmembrane segments. Biochemistry 38:682-695.
    • (1999) Biochemistry , vol.38 , pp. 682-695
    • Martin, N.P.1    Leavitt, L.M.2    Sommers, C.M.3    Dumont, M.E.4
  • 27
    • 0035958023 scopus 로고    scopus 로고
    • Monitoring receptor oligomerization using time-resolved fluorescence resonance energy transfer and bioluminescence resonance energy transfer: The human δ opioid receptor displays constitutive oligomerization at the cell surface which is not regulated by receptor occupancy
    • McVey M, Ramsay D, Kellett E, Rees S, Wilson S, Pope AJ, and Milligan G (2001) Monitoring receptor oligomerization using time-resolved fluorescence resonance energy transfer and bioluminescence resonance energy transfer: the human δ opioid receptor displays constitutive oligomerization at the cell surface which is not regulated by receptor occupancy. J Biol Chem 276:14092-14099.
    • (2001) J Biol Chem , vol.276 , pp. 14092-14099
    • McVey, M.1    Ramsay, D.2    Kellett, E.3    Rees, S.4    Wilson, S.5    Pope, A.J.6    Milligan, G.7
  • 28
    • 1942469334 scopus 로고    scopus 로고
    • The affinity of GxxxG motifs in transmembrane helix-helix interactions is modulated by long-range communication
    • Melnyk RA, Kim S, Curran R, Engelman DM, Bowie JU, and Deber CM (2004) The affinity of GxxxG motifs in transmembrane helix-helix interactions is modulated by long-range communication. J Biol Chem 279:16591-16597.
    • (2004) J Biol Chem , vol.279 , pp. 16591-16597
    • Melnyk, R.A.1    Kim, S.2    Curran, R.3    Engelman, D.M.4    Bowie, J.U.5    Deber, C.M.6
  • 29
    • 0037160105 scopus 로고    scopus 로고
    • Quantitative assessment of beta 1- and beta 2-adrenergic receptor homo- and heterodimerization by bioluminescence resonance energy transfer
    • Mercier JF, Salahpour A, Angers S, Breit A, and Bouvier M (2002) Quantitative assessment of beta 1- and beta 2-adrenergic receptor homo- and heterodimerization by bioluminescence resonance energy transfer. J Biol Chem 277:44925-44931.
    • (2002) J Biol Chem , vol.277 , pp. 44925-44931
    • Mercier, J.F.1    Salahpour, A.2    Angers, S.3    Breit, A.4    Bouvier, M.5
  • 30
    • 3042663287 scopus 로고    scopus 로고
    • G protein-coupled receptor dimerization: Function and ligand pharmacology
    • Milligan G (2004a) G protein-coupled receptor dimerization: function and ligand pharmacology. Mol Pharmacol 66:1-7.
    • (2004) Mol Pharmacol , vol.66 , pp. 1-7
    • Milligan, G.1
  • 31
    • 1442309077 scopus 로고    scopus 로고
    • Applications of bioluminescence and fluorescence resonance energy transfer to drug discovery at G protein-coupled receptors
    • Milligan G (2004b) Applications of bioluminescence and fluorescence resonance energy transfer to drug discovery at G protein-coupled receptors. Eur J Pharm Sci 21:397-405.
    • (2004) Eur J Pharm Sci , vol.21 , pp. 397-405
    • Milligan, G.1
  • 34
    • 0030868842 scopus 로고    scopus 로고
    • Co-expression of defective luteinizing hormone receptor fragments partially reconstitutes ligand-induced signal generation
    • Osuga Y, Hayashi M, Kudo M, Conti M, Kobilka B, and Hsueh AJW (1997) Co-expression of defective luteinizing hormone receptor fragments partially reconstitutes ligand-induced signal generation. J Biol Chem 272:25006-25012.
    • (1997) J Biol Chem , vol.272 , pp. 25006-25012
    • Osuga, Y.1    Hayashi, M.2    Kudo, M.3    Conti, M.4    Kobilka, B.5    Hsueh, A.J.W.6
  • 35
    • 0034704906 scopus 로고    scopus 로고
    • G-protein-coupled receptors function as oligomers in vivo
    • Overton MC and Blumer KJ (2000) G-protein-coupled receptors function as oligomers in vivo. Curr Biol 10:341-344.
    • (2000) Curr Biol , vol.10 , pp. 341-344
    • Overton, M.C.1    Blumer, K.J.2
  • 36
    • 0036829815 scopus 로고    scopus 로고
    • The extracellular N-terminal domain and transmembrane domains 1 and 2 mediate oligomerization of a yeast G protein-coupled receptor
    • Overton MC and Blumer KJ (2002) The extracellular N-terminal domain and transmembrane domains 1 and 2 mediate oligomerization of a yeast G protein-coupled receptor. J Biol Chem 277:41463-41472.
    • (2002) J Biol Chem , vol.277 , pp. 41463-41472
    • Overton, M.C.1    Blumer, K.J.2
  • 37
    • 1542467519 scopus 로고    scopus 로고
    • Oligomerization, biogenesis and signaling is promoted by a glycophorin A-like dimerization motif in transmembrane domain 1 of a yeast G protein-coupled receptor
    • Overton MC, Chinault SL, and Blumer KJ (2003) Oligomerization, biogenesis and signaling is promoted by a glycophorin A-like dimerization motif in transmembrane domain 1 of a yeast G protein-coupled receptor. J Biol Chem 278:49369-49377.
    • (2003) J Biol Chem , vol.278 , pp. 49369-49377
    • Overton, M.C.1    Chinault, S.L.2    Blumer, K.J.3
  • 40
    • 0037101774 scopus 로고    scopus 로고
    • Homo- and hetero-oligomeric interactions between G-protein-coupled receptors in living cells monitored by two variants of bioluminescence resonance energy transfer (BRET): Hetero-oligomers between receptor subtypes form more efficiently than between less closely related sequences
    • Ramsay D, Kellett E, McVey M, Rees S, and Milligan G (2002) Homo- and hetero-oligomeric interactions between G-protein-coupled receptors in living cells monitored by two variants of bioluminescence resonance energy transfer (BRET): hetero-oligomers between receptor subtypes form more efficiently than between less closely related sequences. Biochem J 365:429-440.
    • (2002) Biochem J , vol.365 , pp. 429-440
    • Ramsay, D.1    Kellett, E.2    McVey, M.3    Rees, S.4    Milligan, G.5
  • 41
    • 0034616021 scopus 로고    scopus 로고
    • Receptors for dopamine and somatostatin: Formation of hetero-oligomers with enhanced functional activity
    • Rocheville M, Lange DC, Kumar U, Patel SC, Patel RC, and Patel YC (2000) Receptors for dopamine and somatostatin: formation of hetero-oligomers with enhanced functional activity. Science (Wash DC) 288:154-157.
    • (2000) Science (Wash DC) , vol.288 , pp. 154-157
    • Rocheville, M.1    Lange, D.C.2    Kumar, U.3    Patel, S.C.4    Patel, R.C.5    Patel, Y.C.6
  • 44
    • 0346366929 scopus 로고    scopus 로고
    • Subtype-specific dimerization of α1-adrenoceptora: Effects on receptor expression and pharmacological properties
    • Uberti MA, Hall RA, and Minneman KP (2003) Subtype-specific dimerization of α1-adrenoceptora: effects on receptor expression and pharmacological properties. Mol Pharmacol 64:1379-1390.
    • (2003) Mol Pharmacol , vol.64 , pp. 1379-1390
    • Uberti, M.A.1    Hall, R.A.2    Minneman, K.P.3
  • 47
    • 0032506160 scopus 로고    scopus 로고
    • Truncated V2 vasopressin receptors as negative regulators of wild-type V2 receptor function
    • Zhu X and Wess J (1998) Truncated V2 vasopressin receptors as negative regulators of wild-type V2 receptor function. Biochemistry 37:15773-15784.
    • (1998) Biochemistry , vol.37 , pp. 15773-15784
    • Zhu, X.1    Wess, J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.