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Volumn 5, Issue 5, 2002, Pages 756-763

Formation of oligomers by G protein-coupled receptors

Author keywords

G protein coupled receptors; Hetero oligomer; Homo oligomer; Ligand binding; Receptor trafficking; Signaling

Indexed keywords

4 AMINOBUTYRIC ACID B RECEPTOR; 4 AMINOBUTYRIC ACID RECEPTOR; ALPHA 2 ADRENERGIC RECEPTOR; ANGIOTENSIN 1 RECEPTOR; BETA 2 ADRENERGIC RECEPTOR; BETA ADRENERGIC RECEPTOR; BRADYKININ B2 RECEPTOR; CHEMOKINE RECEPTOR; CHEMOKINE RECEPTOR CCR2; CHEMOKINE RECEPTOR CCR5; DOPAMINE 2 RECEPTOR; ENDOMORPHIN 1; ENKEPHALIN[2 DEXTRO ALANINE 4 METHYLPHENYLALANINE 5 GLYCINE]; G PROTEIN COUPLED RECEPTOR; GLUTAMATE RECEPTOR; GONADORELIN RECEPTOR; LEUCINE ENKEPHALIN; MU OPIATE RECEPTOR AGONIST; MUSCARINIC M3 RECEPTOR; MUSCARINIC RECEPTOR; OPIATE RECEPTOR; PROTIRELIN RECEPTOR; RACLOPRIDE; RADIOLIGAND; RECEPTOR SUBTYPE; SEROTONIN RECEPTOR; SOMATOSTATIN RECEPTOR; SPIPERONE; TRITIUM; UNINDEXED DRUG;

EID: 0036771040     PISSN: 13676733     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Review
Times cited : (31)

References (50)
  • 2
    • 0036174608 scopus 로고    scopus 로고
    • DIMERIZATION: An emerging concept for G protein-coupled receptor ontogeny and function
    • Angers S, Salahpour A, Bouvier M: DIMERIZATION: An emerging concept for G protein-coupled receptor ontogeny and function. Annu Rev Pharmacol Toxicol (2002) 42:409-435. •• An exhaustive and comprehensive review that gives an update of the GPCR oligomerization concept. Readers will find interesting information on diverse receptors, including work from the authors' laboratory.
    • (2002) Annu Rev Pharmacol Toxicol , vol.42 , pp. 409-435
    • Angers, S.1    Salahpour, A.2    Bouvier, M.3
  • 3
    • 0033947541 scopus 로고    scopus 로고
    • Functional significance of oligomerization of G-protein-coupled receptors
    • Salahpour A, Angers S, Bouvier M: Functional significance of oligomerization of G-protein-coupled receptors. Trends Endocrinol Metab (2000) 11:163-168.
    • (2000) Trends Endocrinol Metab , vol.11 , pp. 163-168
    • Salahpour, A.1    Angers, S.2    Bouvier, M.3
  • 5
    • 0029903640 scopus 로고    scopus 로고
    • Metabotropic glutamate receptor 5 is a disulfide-linked dimer
    • Romano C, Yang WL, O'Malley KL: Metabotropic glutamate receptor 5 is a disulfide-linked dimer. J Biol Chem (1996) 271:28612-28616.
    • (1996) J Biol Chem , vol.271 , pp. 28612-28616
    • Romano, C.1    Yang, W.L.2    O'Malley, K.L.3
  • 6
    • 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
    • 3+ - and XL665-derivatized antibodies as FRET partners to analyze GPCR oligomerization using time-resolved FRET.
    • (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
  • 7
    • 0033516576 scopus 로고    scopus 로고
    • Identification and molecular characterization of m, muscarinic receptor dimers
    • Zeng FY, Wess J: Identification and molecular characterization of m, muscarinic receptor dimers. J Biol Chem (1999) 274:19487-19497.
    • (1999) J Biol Chem , vol.274 , pp. 19487-19497
    • Zeng, F.Y.1    Wess, J.2
  • 8
    • 0032483541 scopus 로고    scopus 로고
    • Dimerization of the extracellular calcium-sensing receptor (CaR) on the cell surface of CaR-transfected HEK293 cells
    • Bai M, Trivedi S, Brown EM: Dimerization of the extracellular calcium-sensing receptor (CaR) on the cell surface of CaR-transfected HEK293 cells. J Biol Chem (1998) 273:23605-23610.
    • (1998) J Biol Chem , vol.273 , pp. 23605-23610
    • Bai, M.1    Trivedi, S.2    Brown, E.M.3
  • 13
    • 0033578005 scopus 로고    scopus 로고
    • G-protein-coupled receptor heterodimerization modulates receptor function
    • Jordan BA, Devi LA: G-protein-coupled receptor heterodimerization modulates receptor function. Nature (1999) 399:697-700.
    • (1999) Nature , vol.399 , pp. 697-700
    • Jordan, B.A.1    Devi, L.A.2
  • 15
    • 0034618268 scopus 로고    scopus 로고
    • AT1-receptor heterodimers show enhanced G-protein activation and altered receptor sequestration
    • AbdAlla S, Lother H, Quitterer U: AT1-receptor heterodimers show enhanced G-protein activation and altered receptor sequestration. Nature (2000) 407:94-98.
    • (2000) Nature , vol.407 , pp. 94-98
    • AbdAlla, S.1    Lother, H.2    Quitterer, U.3
  • 17
    • 0027467848 scopus 로고
    • Coexpression studies with mutant muscarinic/adrenergic receptors provide evidence for intermolecular "cross-talk" between G-protein-linked receptors
    • Maggio R, Vogel Z, Wess J: Coexpression studies with mutant muscarinic/adrenergic receptors provide evidence for intermolecular "cross-talk" between G-protein-linked receptors. Proc Natl Acad Sci USA (1993) 90:3103-3107.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 3103-3107
    • Maggio, R.1    Vogel, Z.2    Wess, J.3
  • 18
    • 0033020243 scopus 로고    scopus 로고
    • Intermolecular interactions between dimeric calcium-sensing receptor monomers are important for its normal function
    • Bai M,Trivedi S, Kifor O, Quinn SJ, Brown EM: Intermolecular interactions between dimeric calcium-sensing receptor monomers are important for its normal function. Proc Natl Acad Sci USA (1999) 96:2834-2839.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 2834-2839
    • Bai, M.1    Trivedi, S.2    Kifor, O.3    Quinn, S.J.4    Brown, E.M.5
  • 19
    • 0030028756 scopus 로고    scopus 로고
    • Polar residues in the transmembrane domains of the type 1 angiotensin II receptor are required for binding and coupling. Reconstitution of the binding site by co-expreseion of two deficient mutants
    • Monnot C, Bihoreau C, Conchon S, Cumow KM, Corvol P, Clauser E: Polar residues in the transmembrane domains of the type 1 angiotensin II receptor are required for binding and coupling. Reconstitution of the binding site by co-expreseion of two deficient mutants. J Biol Chem (1996) 271:1507-1513.
    • (1996) J Biol Chem , vol.271 , pp. 1507-1513
    • Monnot, C.1    Bihoreau, C.2    Conchon, S.3    Cumow, K.M.4    Corvol, P.5    Clauser, E.6
  • 20
    • 0034677745 scopus 로고    scopus 로고
    • Subtypes of the somatostatin receptor assemble as functional homo- and heterodimers
    • Rocheville M, Lange DC, Kumar U, Sasi R, Patel RC, Patel YC: Subtypes of the somatostatin receptor assemble as functional homo- and heterodimers. J Biol Chem (2000) 275:7862-7869.
    • (2000) J Biol Chem , vol.275 , pp. 7862-7869
    • Rocheville, M.1    Lange, D.C.2    Kumar, U.3    Sasi, R.4    Patel, R.C.5    Patel, Y.C.6
  • 22
    • 0032506160 scopus 로고    scopus 로고
    • 2 receptor function
    • 2 receptor function. Biochemistry (1998) 37:15773-15784.
    • (1998) Biochemistry , vol.37 , pp. 15773-15784
    • Zhu, X.1    Wess, J.2
  • 24
    • 0035918215 scopus 로고    scopus 로고
    • Constitutive and agonist-dependent homo-oligomerization of the thyrotropin-releasing hormone receptor. Detection in living cells using bioluminescence resonance energy transfer
    • Kroeger KM, Hanyaloglu AC, Seeber RM, Miles LE, Eidne KA: Constitutive and agonist-dependent homo-oligomerization of the thyrotropin-releasing hormone receptor. Detection in living cells using bioluminescence resonance energy transfer. J Biol Chem (2001) 276:12736-12743.
    • (2001) J Biol Chem , vol.276 , pp. 12736-12743
    • Kroeger, K.M.1    Hanyaloglu, A.C.2    Seeber, R.M.3    Miles, L.E.4    Eidne, K.A.5
  • 25
    • 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
    • 2R, suggesting that this increase is more likely due to conformational changes than an increase in receptor oligomerization. The paper also describes the first possibility of distinguishing between monomer, dimer and higher order oligomers.
    • (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
  • 26
    • 0034704906 scopus 로고    scopus 로고
    • G-protein-coupled receptors function as oligomers in vivo
    • Overton MC, Blumer KJ: G-protein-coupled receptors function as oligomers in vivo. Curr Biol (2000) 10:341-344.
    • (2000) Curr Biol , vol.10 , pp. 341-344
    • Overton, M.C.1    Blumer, K.J.2
  • 27
    • 0035910464 scopus 로고    scopus 로고
    • Gonadotropin-releasing hormone receptor microaggregation. Rate monitored by fluorescence resonance energy transfer
    • Comea A, Janovick JA, Maya-Nunez G, Conn PM: Gonadotropin-releasing hormone receptor microaggregation. Rate monitored by fluorescence resonance energy transfer. J Biol Chem (2001) 276:2153-2158.
    • (2001) J Biol Chem , vol.276 , pp. 2153-2158
    • Comea, A.1    Janovick, J.A.2    Maya-Nunez, G.3    Conn, P.M.4
  • 28
    • 0035002343 scopus 로고    scopus 로고
    • Binding of agonist but not antagonist leads to fluorescence resonance energy transfer between intrinsically fluorescent gonadotropin-releasing hormone receptors
    • Horvat RD, Roess DA, Nelson SE, Barisas BG, Clay CM: Binding of agonist but not antagonist leads to fluorescence resonance energy transfer between intrinsically fluorescent gonadotropin-releasing hormone receptors. Mol Endocrinol (2001) 15:695-703.
    • (2001) Mol Endocrinol , vol.15 , pp. 695-703
    • Horvat, R.D.1    Roess, D.A.2    Nelson, S.E.3    Barisas, B.G.4    Clay, C.M.5
  • 30
    • 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, Patel YC: Receptors for dopamine and somatostatin: Formation of hetero-oligomers with enhanced functional activity. Science (2000) 288:154-157.
    • (2000) Science , 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
  • 31
    • 0034522937 scopus 로고    scopus 로고
    • Luteinizing hormone receptors are self-associated in the plasma membrane
    • Roess DA, Horvat RD, Munnelly H, Barisas BG: Luteinizing hormone receptors are self-associated in the plasma membrane. Endocrinology (2000) 141:4518-4523. • An interesting example of the use of fluorescence-labeled ligands to monitor receptor oligomerization.
    • (2000) Endocrinology , vol.141 , pp. 4518-4523
    • Roess, D.A.1    Horvat, R.D.2    Munnelly, H.3    Barisas, B.G.4
  • 34
    • 0030760634 scopus 로고    scopus 로고
    • Dimerization of the delta opioid receptor: Implication for a role in receptor internalization
    • Cvejic S, Devi LA: Dimerization of the delta opioid receptor: Implication for a role in receptor internalization. J Biol Chem (1997) 272:26959-26964.
    • (1997) J Biol Chem , vol.272 , pp. 26959-26964
    • Cvejic, S.1    Devi, L.A.2
  • 35
    • 0017190266 scopus 로고
    • Negative cooperativity among β-adrenergic receptors in frog erythrocyte membranes
    • Limbird LE, Lefkowitz RJ: Negative cooperativity among β-adrenergic receptors in frog erythrocyte membranes. J Biol Chem (1976) 251:5007-5014.
    • (1976) J Biol Chem , vol.251 , pp. 5007-5014
    • Limbird, L.E.1    Lefkowitz, R.J.2
  • 36
    • 0032030621 scopus 로고    scopus 로고
    • Rethinking receptor-G protein-effector interactions
    • Chidiac P: Rethinking receptor-G protein-effector interactions. Biochem Pharmacol (1998) 55:549-556.
    • (1998) Biochem Pharmacol , vol.55 , pp. 549-556
    • Chidiac, P.1
  • 37
    • 0037197663 scopus 로고    scopus 로고
    • Cooperativity and oligomeric status of cardiac muscarinic cholinergic receptors
    • Park PS, Sum CS, Pawagi AB, Wells JW: Cooperativity and oligomeric status of cardiac muscarinic cholinergic receptors. Biochemistry (2002) 41:5588-5604. •• An excellent example of very detailed and carefully controlled ligand binding studies, combined with mathematical modeling, leading to conclusions of oligomerization of this GPCR.
    • (2002) Biochemistry , vol.41 , pp. 5588-5604
    • Park, P.S.1    Sum, C.S.2    Pawagi, A.B.3    Wells, J.W.4
  • 38
    • 0035933747 scopus 로고    scopus 로고
    • 2 receptor dimer formation: Evidence from ligand binding
    • 2 receptor dimer formation: Evidence from ligand binding. J Biol Chem (2001) 276:22621-22629.
    • (2001) J Biol Chem , vol.276 , pp. 22621-22629
    • Armstrong, D.1    Strange, P.G.2
  • 40
    • 0035057221 scopus 로고    scopus 로고
    • Interaction of co-expressed μ- and δ-opioid receptors in transfected rat pituitary GH, cells
    • Martin NA, Prather PL: Interaction of co-expressed μ- and δ-opioid receptors in transfected rat pituitary GH, cells. Mol Pharmacol (2001) 59:774-783.
    • (2001) Mol Pharmacol , vol.59 , pp. 774-783
    • Martin, N.A.1    Prather, P.L.2
  • 42
    • 0034714335 scopus 로고    scopus 로고
    • Oligomerization of μ- and δ-opioid receptors. Generation of novel functional properties
    • George SR, Fan T, Xie Z, Tse R, Tam V, Varghese G, O'Dowd BF: Oligomerization of μ- and δ-opioid receptors. Generation of novel functional properties. J Biol Chem (2000) 275:26128-26135.
    • (2000) J Biol Chem , vol.275 , pp. 26128-26135
    • George, S.R.1    Fan, T.2    Xie, Z.3    Tse, R.4    Tam, V.5    Varghese, G.6    O'Dowd, B.F.7
  • 46
    • 0037169345 scopus 로고    scopus 로고
    • Regulation of opioid receptor trafficking and morphine tolerance by receptor oligomerization
    • He L, Fong J, von Zastrow M, Whistler JL: Regulation of opioid receptor trafficking and morphine tolerance by receptor oligomerization. Cell (2002) 108:271-282. •• The study proposes that homo-oligomerization of opioid receptors alters the endocytosis of the receptor, resulting in a reduction of tolerance to morphine. This may provide an important new means for the treatment of chronic pain without induction of tolerance.
    • (2002) Cell , vol.108 , pp. 271-282
    • He, L.1    Fong, J.2    Von Zastrow, M.3    Whistler, J.L.4
  • 49
    • 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, Milligan G: 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 (2002) 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
  • 50
    • 0030712312 scopus 로고    scopus 로고
    • Mechanism of transdominant inhibition of CCR5-mediated HIV-1 infection by CCR5Δ32
    • Benkirane M, Jin DY, Chun RF, Koup RA, Jeang KT: Mechanism of transdominant inhibition of CCR5-mediated HIV-1 infection by CCR5Δ32. J Biol Chem (1997) 272:30603-30606.
    • (1997) J Biol Chem , vol.272 , pp. 30603-30606
    • Benkirane, M.1    Jin, D.Y.2    Chun, R.F.3    Koup, R.A.4    Jeang, K.T.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.