메뉴 건너뛰기




Volumn 365, Issue 2, 2002, Pages 429-440

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

Author keywords

Adrenaline; Dimerization; Energy transfer; G protein; Opioid

Indexed keywords

CELLS; OLIGOMERS; PROTEINS;

EID: 0037101774     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20020251     Document Type: Article
Times cited : (189)

References (45)
  • 2
    • 0033118334 scopus 로고    scopus 로고
    • Molecular tinkering of G protein-coupled receptors: An evolutionary success
    • Bockaert, J. and Pin, J. P. (1999) Molecular tinkering of G protein-coupled receptors: an evolutionary success. EMBO J. 18, 1723-1729
    • (1999) EMBO J. , vol.18 , pp. 1723-1729
    • Bockaert, J.1    Pin, J.P.2
  • 3
    • 0034464742 scopus 로고    scopus 로고
    • Uncovering molecular mechanisms involved in activation of G protein-coupled receptors
    • Gether, U. (2000) Uncovering molecular mechanisms involved in activation of G protein-coupled receptors. Endocrin. Rev. 21, 90-113
    • (2000) Endocrin. Rev. , vol.21 , pp. 90-113
    • Gether, U.1
  • 4
    • 0034948696 scopus 로고    scopus 로고
    • Structural mimicry in G protein-coupled receptors: Implications of the high-resolution structure of rhodopsin for structure-function analysis of rhodopsin-like receptors
    • Ballesteros, J. A., Shi, L. and Javitch, J. A. (2001) Structural mimicry in G protein-coupled receptors: implications of the high-resolution structure of rhodopsin for structure-function analysis of rhodopsin-like receptors. Mol. Pharmacol. 60, 1-19
    • (2001) Mol. Pharmacol. , vol.60 , pp. 1-19
    • Ballesteros, J.A.1    Shi, L.2    Javitch, J.A.3
  • 5
    • 0035318509 scopus 로고    scopus 로고
    • Oligomerization of G-protein-coupled transmitter receptors
    • Bouvier, M. (2001) Oligomerization of G-protein-coupled transmitter receptors. Nat. Rev. Neurosci. 2, 274-286
    • (2001) Nat. Rev. Neurosci. , vol.2 , pp. 274-286
    • Bouvier, M.1
  • 6
    • 0035478438 scopus 로고    scopus 로고
    • Heterodimerization of G protein-coupled receptors: Pharmacology, signaling and trafficking
    • Devi, L. A. (2001) Heterodimerization of G protein-coupled receptors: pharmacology, signaling and trafficking. Trends Pharmacol. Sci. 22, 532-537
    • (2001) Trends Pharmacol. Sci. , vol.22 , pp. 532-537
    • Devi, L.A.1
  • 7
    • 0035032316 scopus 로고    scopus 로고
    • Oligomerisation of G-protein-coupled receptors
    • Milligan, G. (2001) Oligomerisation of G-protein-coupled receptors. J. Cell Sci. 114, 1265-1271
    • (2001) J. Cell Sci. , vol.114 , pp. 1265-1271
    • Milligan, G.1
  • 8
    • 0029666267 scopus 로고    scopus 로고
    • A peptide derived from a β-adrenergic receptor transmembrane domain inhibits both receptor dimerization and activation
    • Herbert, T. E., Moffett, S., Morello, J.-P., Loisel, T. P., Bichet, D. G., Barret, C. and Bouvier, M. (1996) A peptide derived from a β-adrenergic receptor transmembrane domain inhibits both receptor dimerization and activation. J. Biol. Chem. 271, 16384-16392
    • (1996) J. Biol. Chem. , vol.271 , pp. 16384-16392
    • Herbert, T.E.1    Moffett, S.2    Morello, J.-P.3    Loisel, T.P.4    Bichet, D.G.5    Barret, C.6    Bouvier, M.7
  • 9
    • 0030760634 scopus 로고    scopus 로고
    • Dimerization of the δ opioid receptor: Implication for a role in receptor internalization
    • Cvejic, S. and Devi, L. A. (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
  • 10
    • 0033516576 scopus 로고    scopus 로고
    • Identification and molecular characterization of m3 muscarinic receptor dimers
    • Zeng, F-Y. and Wess, J. (1999) Identification and molecular characterization of m3 muscarinic receptor dimers. J. Biol. Chem. 274, 19487-19497
    • (1999) J. Biol. Chem. , vol.274 , pp. 19487-19497
    • Zeng, F.-Y.1    Wess, J.2
  • 11
    • 0033578005 scopus 로고    scopus 로고
    • G-protein-coupled receptor heterodimerization modulates receptor function
    • Jordan, B. A. and Devi, L. A. (1999) G-protein-coupled receptor heterodimerization modulates receptor function. Nature (London) 399, 697-700
    • (1999) Nature (London) , vol.399 , pp. 697-700
    • Jordan, B.A.1    Devi, L.A.2
  • 13
    • 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
  • 15
    • 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, K. M., Hanyaloglu, A. C., Seeber, R. M., Miles, L. E. and Eidne, K. A. (2001) Constitutive and agonist-dependent homo-oligomerization of the thyrotropin-releasing hormone receptor. Detection in living cells using bioluminescence resonance energy transfer. J. Biol. Chem. 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
  • 16
    • 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, A. J. 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
  • 17
    • 0034704906 scopus 로고    scopus 로고
    • G-protein-coupled receptors function as oligomers in vivo
    • Overton, M. C. and Blumer, K. J. (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
  • 18
    • 0034677745 scopus 로고    scopus 로고
    • Subtypes of the somatostatin receptor assemble as functional homo- and heterodimers
    • Rocheville, M., Lange, D. C., Kumar, U., Sasi, R., Patel, R. C. and Patel, Y. C. (2000) Subtypes of the somatostatin receptor assemble as functional homo- and heterodimers. J. Biol. Chem. 276, 7862-7869
    • (2000) J. Biol. Chem. , vol.276 , pp. 7862-7869
    • Rocheville, M.1    Lange, D.C.2    Kumar, U.3    Sasi, R.4    Patel, R.C.5    Patel, Y.C.6
  • 19
    • 0034616021 scopus 로고    scopus 로고
    • Receptors for dopamine and somatostatin: Formation of hetero-oligomers with enhanced functional activity
    • Rocheville, M., Lange, D. C., Kumar, U., Patel, S. C., Patel, R. C. and Patel, Y. C. (2000) Receptors for dopamine and somatostatin: formation of hetero-oligomers with enhanced functional activity. Science (Washington, D.C.) 288, 154-157
    • (2000) Science (Washington, D.C.) , 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
  • 20
    • 0035910464 scopus 로고    scopus 로고
    • Gonadotropin releasing hormone microaggregation: Rate monitored by fluorescence resonance energy transfer
    • Cornea, A., Janovick, J. A., Maya-Nunez, G. and Conn, P. M. (2001) Gonadotropin releasing hormone microaggregation: rate monitored by fluorescence resonance energy transfer. J. Biol. Chem. 276, 2153-2158
    • (2001) J. Biol. Chem. , vol.276 , pp. 2153-2158
    • Cornea, A.1    Janovick, J.A.2    Maya-Nunez, G.3    Conn, P.M.4
  • 21
    • 0035958027 scopus 로고    scopus 로고
    • Homo- and heterodimerization of somatostatin receptor subtypes. Inactivation of sst(3) receptor function by heterodimerization with sst(2A)
    • Pfeiffer, M., Koch, T., Schroder, H., Klutzny, M., Kirscht, S., Kreienkamp, H. J., Hollt, V. and Schulz, S. (2001) Homo- and heterodimerization of somatostatin receptor subtypes. Inactivation of sst(3) receptor function by heterodimerization with sst(2A). J. Biol. Chem. 276, 14027-14036
    • (2001) J. Biol. Chem. , vol.276 , pp. 14027-14036
    • Pfeiffer, M.1    Koch, T.2    Schroder, H.3    Klutzny, M.4    Kirscht, S.5    Kreienkamp, H.J.6    Hollt, V.7    Schulz, S.8
  • 22
    • 0035912846 scopus 로고    scopus 로고
    • Heteromeric association creates a P2Y-like adenosine receptor
    • Yoshioka, K., Saitoh, O. and Nakata, H. (2001) Heteromeric association creates a P2Y-like adenosine receptor. Proc. Natl. Acad. Sci. U.S.A. 98, 7617-7622
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 7617-7622
    • Yoshioka, K.1    Saitoh, O.2    Nakata, H.3
  • 24
    • 0034723169 scopus 로고    scopus 로고
    • Structural implication for receptor oligomerization from functional reconstitution studies of mutant V2 vasopressin receptors
    • Schulz, A., Grosse, R., Schultz, G., Gudermann, T. and Schoneberg, T. (2000) Structural implication for receptor oligomerization from functional reconstitution studies of mutant V2 vasopressin receptors. J. Biol. Chem. 276, 2381-2389
    • (2000) J. Biol. Chem. , vol.276 , pp. 2381-2389
    • Schulz, A.1    Grosse, R.2    Schultz, G.3    Gudermann, T.4    Schoneberg, T.5
  • 27
    • 0032508587 scopus 로고    scopus 로고
    • Real time visualisation of agonist-mediated redistribution and internalisation of a green fluorescent protein-tagged form of the thyrotropin-releasing hormone receptor
    • Drmota, T., Gould, G. W. and Milligan, G. (1998) Real time visualisation of agonist-mediated redistribution and internalisation of a green fluorescent protein-tagged form of the thyrotropin-releasing hormone receptor. J. Biol. Chem. 273, 24000-24008
    • (1998) J. Biol. Chem. , vol.273 , pp. 24000-24008
    • Drmota, T.1    Gould, G.W.2    Milligan, G.3
  • 30
    • 0035914405 scopus 로고    scopus 로고
    • Heterodimerization of calcium sensing receptors with metabotropic glutamate receptors in neurons
    • Gama, L., Wilt, S. G. and Breitwieser, G. E. (2001) Heterodimerization of calcium sensing receptors with metabotropic glutamate receptors in neurons. J. Biol. Chem. 276, 39053-39059
    • (2001) J. Biol. Chem. , vol.276 , pp. 39053-39059
    • Gama, L.1    Wilt, S.G.2    Breitwieser, G.E.3
  • 32
    • 0034618268 scopus 로고    scopus 로고
    • 1-receptor heterodimers show enhanced G-protein activation and altered receptor sequestration
    • 1-receptor heterodimers show enhanced G-protein activation and altered receptor sequestration. Nature (London) 407, 94-98
    • (2000) Nature (London) , vol.407 , pp. 94-98
    • AbdAlla, S.1    Lother, H.2    Quitterer, U.3
  • 37
    • 0033842644 scopus 로고    scopus 로고
    • 2-adrenoceptors: Comparisons with the unmodified receptors
    • 2-adrenoceptors: comparisons with the unmodified receptors. Br. J. Pharmacol. 130, 1825-1832
    • (2000) Br. J. Pharmacol. , vol.130 , pp. 1825-1832
    • McLean, A.J.1    Milligan, G.2
  • 39
    • 0027424642 scopus 로고
    • The disaggregation theory of signal transduction revisited: Further evidence that G proteins are multimeric and disaggregate to monomers when activated
    • Jahangeer, S. and Rodbell, M. (1993) The disaggregation theory of signal transduction revisited: further evidence that G proteins are multimeric and disaggregate to monomers when activated. Proc. Natl. Acad. Sci. U.S.A. 90, 8782-8786
    • (1993) Proc. Natl. Acad. Sci. U.S.A. , vol.90 , pp. 8782-8786
    • Jahangeer, S.1    Rodbell, M.2
  • 41
    • 0031446639 scopus 로고    scopus 로고
    • Inhibition of gonadotrophin-releasing hormone receptor signaling by expression of a splice variant of the human receptor
    • Grosse, R., Schoneberg, T., Schultz, G. and Gudermann, T. (1997) Inhibition of gonadotrophin-releasing hormone receptor signaling 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
  • 42
    • 0033924207 scopus 로고    scopus 로고
    • Inhibitation of cell surface expression by mutant receptors demonstrates that D2 dopamine receptors exist as oligomers in the cell
    • Lee, S. P., O'Dowd, B. F., Ng, G. Y. K., Varghese, G., Akil, H., Mansour, A., Nguyen, T. and George, S. R. (2000) Inhibitation of cell surface expression by mutant receptors demonstrates that D2 dopamine receptors exist as oligomers in the cell. Mol. Pharmacol. 58, 120-128
    • (2000) Mol. Pharmacol. , vol.58 , pp. 120-128
    • Lee, S.P.1    O'Dowd, B.F.2    Ng, G.Y.K.3    Varghese, G.4    Akil, H.5    Mansour, A.6    Nguyen, T.7    George, S.R.8
  • 43
    • 0033798153 scopus 로고    scopus 로고
    • The dopamine D3 receptor interacts with itself and the truncated D3 splice variant D3nf: D3-D3nf interaction causes mislocalization of D3 receptors
    • Karpa, K. D., Lin, R., Kabbani, N. and Levenson, R. (2000) The dopamine D3 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
  • 44
    • 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, Z. J. and Miller, L. J. (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
  • 45
    • 0034986205 scopus 로고    scopus 로고
    • Detection of receptor ligands by monitoring selective stabilization of a Renilla luciferase-tagged, constitutively active mutant, G protein-coupled receptor
    • Ramsay, D., Bevan, N., Rees, S. and Milligan, G. (2001) Detection of receptor ligands by monitoring selective stabilization of a Renilla luciferase-tagged, constitutively active mutant, G protein-coupled receptor. Br. J. Pharmacol. 133, 315-323
    • (2001) Br. J. Pharmacol. , vol.133 , pp. 315-323
    • Ramsay, D.1    Bevan, N.2    Rees, S.3    Milligan, G.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.