메뉴 건너뛰기




Volumn 439, Issue 1, 2011, Pages 171-183

The orexin OX 1 receptor exists predominantly as a homodimer in the basal state: Potential regulation of receptor organization by both agonist and antagonist ligands

Author keywords

Blue native PAGE (BN PAGE); Homodimer; Orexin OX 1 receptor; Receptor organization

Indexed keywords

EPITOPE; G PROTEIN COUPLED RECEPTOR; LIGAND; OREXIN 1 RECEPTOR; YELLOW FLUORESCENT PROTEIN;

EID: 80052756132     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20110230     Document Type: Article
Times cited : (31)

References (50)
  • 1
    • 21844441860 scopus 로고    scopus 로고
    • Monomeric G-protein-coupled receptor as a functional unit
    • DOI 10.1021/bi050720o
    • Chabre, M. and le Maire, M. (2005) Monomeric G-protein-coupled receptor as a functional unit. Biochemistry 44, 9395-9403 (Pubitemid 40962038)
    • (2005) Biochemistry , vol.44 , Issue.27 , pp. 9395-9403
    • Chabre, M.1    Le, M.M.2
  • 2
    • 40349085622 scopus 로고    scopus 로고
    • A day in the life of a G protein-coupled receptor: The contribution to function of G protein-coupled receptor dimerization
    • Milligan, G. (2008) A day in the life of a G protein-coupled receptor: the contribution to function of G protein-coupled receptor dimerization. Br. J. Pharmacol. 153 (Suppl. 1), S216-S229
    • (2008) Br. J. Pharmacol. , vol.153 , Issue.SUPPL. 1
    • Milligan, G.1
  • 3
    • 33947369500 scopus 로고    scopus 로고
    • G protein-coupled receptor dimerisation: Molecular basis and relevance to function
    • Milligan, G. (2007) G protein-coupled receptor dimerisation: molecular basis and relevance to function. Biochim. Biophys. Acta 1768, 825-835
    • (2007) Biochim. Biophys. Acta , vol.1768 , pp. 825-835
    • Milligan, G.1
  • 4
    • 21344446100 scopus 로고    scopus 로고
    • Allosteric functioning of dimeric class C G-protein-coupled receptors
    • DOI 10.1111/j.1742-4658.2005.04728.x
    • Pin, J. P., Kniazeff, J., Liu, J., Binet, V., Goudet, C., Rondard, P. and Prézeau, L. (2005) Allosteric functioning of dimeric class C G-protein-coupled receptors. FEBS J. 272, 2947-2955 (Pubitemid 40904683)
    • (2005) FEBS Journal , vol.272 , Issue.12 , pp. 2947-2955
    • Pin, J.-P.1    Kniazeff, J.2    Liu, J.3    Binet, V.4    Goudet, C.5    Rondard, P.6    Prezeau, L.7
  • 7
    • 11144301817 scopus 로고    scopus 로고
    • Reverse pharmacology of orexin: From an orphan GPCR to integrative physiology
    • Sakurai, T. (2005) Reverse pharmacology of orexin: from an orphan GPCR to integrative physiology. Regul. Pept. 126, 3-10
    • (2005) Regul. Pept. , vol.126 , pp. 3-10
    • Sakurai, T.1
  • 8
    • 33748597939 scopus 로고    scopus 로고
    • Eating, sleeping and rewarding: Orexin receptors and their antagonists
    • Bingham, M. J., Cai, J. and Deehan, M. R. (2006) Eating, sleeping and rewarding: orexin receptors and their antagonists. Curr. Opin. Drug Discovery Dev. 9, 551-559
    • (2006) Curr. Opin. Drug Discovery Dev. , vol.9 , pp. 551-559
    • Bingham, M.J.1    Cai, J.2    Deehan, M.R.3
  • 10
    • 74549127520 scopus 로고    scopus 로고
    • Almorexant, a dual orexin receptor antagonist for the treatment of insomnia
    • Neubauer, D. N. (2010) Almorexant, a dual orexin receptor antagonist for the treatment of insomnia. Curr. Opin. Invest. Drugs 11, 101-110
    • (2010) Curr. Opin. Invest. Drugs , vol.11 , pp. 101-110
    • Neubauer, D.N.1
  • 11
    • 33846030175 scopus 로고    scopus 로고
    • Orexin-1 receptor-cannabinoid CB1 receptor heterodimerization results in both ligand-dependent and -independent coordinated alterations of receptor localization and function
    • Ellis, J., Pediani, J. D., Canals, M., Milasta, S. and Milligan, G. (2006) Orexin-1 receptor-cannabinoid CB1 receptor heterodimerization results in both ligand-dependent and -independent coordinated alterations of receptor localization and function. J. Biol. Chem. 281, 38812-38824
    • (2006) J. Biol. Chem. , vol.281 , pp. 38812-38824
    • Ellis, J.1    Pediani, J.D.2    Canals, M.3    Milasta, S.4    Milligan, G.5
  • 12
    • 33747377849 scopus 로고    scopus 로고
    • Blue native polyacrylamide gel electrophoresis (BN-PAGE) for the identification and analysis of multiprotein complexes
    • Swamy, M., Siegers, G. M., Minguet, S., Wollscheid, B. and Schamel, W. W. (2006) Blue native polyacrylamide gel electrophoresis (BN-PAGE) for the identification and analysis of multiprotein complexes. Sci. STKE 2006, pl4
    • (2006) Sci. STKE , vol.2006
    • Swamy, M.1    Siegers, G.M.2    Minguet, S.3    Wollscheid, B.4    Schamel, W.W.5
  • 13
    • 33750303540 scopus 로고    scopus 로고
    • Analysis of membrane protein complexes by blue native PAGE
    • Reisinger, V. and Eichacker, L. A. (2006) Analysis of membrane protein complexes by blue native PAGE. Proteomics 6 (Suppl. 2), 6-15
    • (2006) Proteomics , vol.6 , Issue.SUPPL. 2 , pp. 6-15
    • Reisinger, V.1    Eichacker, L.A.2
  • 14
    • 77955982118 scopus 로고    scopus 로고
    • Applications of fluorescence and bioluminescence resonance energy transfer to drug discovery at G protein coupled receptors
    • Alvarez-Curto, E., Pediani, J. D. and Milligan, G. (2010) Applications of fluorescence and bioluminescence resonance energy transfer to drug discovery at G protein coupled receptors. Anal. Bioanal. Chem. 398, 167-180
    • (2010) Anal. Bioanal. Chem. , vol.398 , pp. 167-180
    • Alvarez-Curto, E.1    Pediani, J.D.2    Milligan, G.3
  • 15
    • 77954917965 scopus 로고    scopus 로고
    • 3 muscarinic acetylcholine receptors analyzed by fluorescence resonance energy transfer (FRET) imaging and homogeneous time-resolved FRET
    • 3 muscarinic acetylcholine receptors analyzed by fluorescence resonance energy transfer (FRET) imaging and homogeneous time-resolved FRET. J. Biol. Chem. 285, 23318-23330
    • (2010) J. Biol. Chem. , vol.285 , pp. 23318-23330
    • Alvarez-Curto, E.1    Ward, R.J.2    Pediani, J.D.3    Milligan, G.4
  • 16
    • 0141985986 scopus 로고    scopus 로고
    • Enzyme fragment complementation: A flexible high throughput screening assay technology
    • Eglen, R. M. (2002) Enzyme fragment complementation: a flexible high throughput screening assay technology. Assay Drug Dev. Technol. 1, 97-104
    • (2002) Assay Drug Dev. Technol. , vol.1 , pp. 97-104
    • Eglen, R.M.1
  • 17
    • 68849115309 scopus 로고    scopus 로고
    • BRET3: A red-shifted bioluminescence resonance energy transfer (BRET)-based integrated platform for imaging protein-protein interactions from single live cells and living animals
    • De, A., Ray, P., Loening, A. M. and Gambhir, S. S. (2009) BRET3: a red-shifted bioluminescence resonance energy transfer (BRET)-based integrated platform for imaging protein-protein interactions from single live cells and living animals. FASEB J. 23, 2702-2709
    • (2009) FASEB J. , vol.23 , pp. 2702-2709
    • De, A.1    Ray, P.2    Loening, A.M.3    Gambhir, S.S.4
  • 19
    • 6944234943 scopus 로고    scopus 로고
    • 1b-adrenoceptor
    • DOI 10.1124/mol.104.001586
    • Carrillo, J. J., López-Gimenez, J. F. and Milligan, G. (2004) Multiple interactions between transmembrane helices generate the oligomeric α1b-adrenoceptor. Mol. Pharmacol. 66, 1123-1137 (Pubitemid 39411053)
    • (2004) Molecular Pharmacology , vol.66 , Issue.5 , pp. 1123-1137
    • Carrillo, J.J.1    Lopez-Gimenez, J.F.2    Milligan, G.3
  • 20
    • 18844411824 scopus 로고    scopus 로고
    • The sustainability of interactions between the orexin-1 receptor and β-arrestin-2 is defined by a single C-terminal cluster of hydroxy amino acids and modulates the kinetics of ERK MAPK regulation
    • Milasta, S., Evans, N. A., Ormiston, L., Wilson, S., Lefkowitz, R. J. and Milligan, G. (2005) The sustainability of interactions between the orexin-1 receptor and β-arrestin-2 is defined by a single C-terminal cluster of hydroxy amino acids and modulates the kinetics of ERK MAPK regulation. Biochem. J. 387, 573-584
    • (2005) Biochem. J. , vol.387 , pp. 573-584
    • Milasta, S.1    Evans, N.A.2    Ormiston, L.3    Wilson, S.4    Lefkowitz, R.J.5    Milligan, G.6
  • 21
    • 33845923854 scopus 로고    scopus 로고
    • BRET analysis of GPCR oligomerization: Newer does not mean better [1]
    • DOI 10.1038/nmeth0107-3, PII NMETH0107-3
    • Bouvier, M., Heveker, N., Jockers, R., Marullo, S. and Milligan, G. (2007) BRET analysis of GPCR oligomerization: newer does not mean better. Nat. Methods 4, 3-4 (Pubitemid 46029461)
    • (2007) Nature Methods , vol.4 , Issue.1 , pp. 3-4
    • Bouvier, M.1    Heveker, N.2    Jockers, R.3    Marullo, S.4    Milligan, G.5
  • 22
    • 77950496251 scopus 로고    scopus 로고
    • Practical considerations of membrane protein instability during purification and crystallisation
    • Tate, C. G. (2010) Practical considerations of membrane protein instability during purification and crystallisation. Methods Mol. Biol. 601, 187-203
    • (2010) Methods Mol. Biol. , vol.601 , pp. 187-203
    • Tate, C.G.1
  • 23
    • 77950460037 scopus 로고    scopus 로고
    • Spatial control of EGF receptor activation by reversible dimerization on living cells
    • Chung, I., Akita, R., Vandlen, R., Toomre, D., Schlessinger, J. and Mellman, I. (2010) Spatial control of EGF receptor activation by reversible dimerization on living cells. Nature 464, 783-787
    • (2010) Nature , vol.464 , pp. 783-787
    • Chung, I.1    Akita, R.2    Vandlen, R.3    Toomre, D.4    Schlessinger, J.5    Mellman, I.6
  • 24
    • 74449093106 scopus 로고    scopus 로고
    • Reversible dimerization of EGFR revealed by single-molecule fluorescence imaging using quantum dots
    • Kawashima, N., Nakayama, K., Itoh, K., Itoh, T., Ishikawa, M. and Biju, V. (2010) Reversible dimerization of EGFR revealed by single-molecule fluorescence imaging using quantum dots. Chemistry 16, 1186-1192
    • (2010) Chemistry , vol.16 , pp. 1186-1192
    • Kawashima, N.1    Nakayama, K.2    Itoh, K.3    Itoh, T.4    Ishikawa, M.5    Biju, V.6
  • 25
    • 67650533801 scopus 로고    scopus 로고
    • The action and mode of binding of thiazolidinedione ligands at free fatty acid receptor 1
    • Smith, N. J., Stoddart, L. A., Devine, N. M., Jenkins, L. and Milligan, G. (2009) The action and mode of binding of thiazolidinedione ligands at free fatty acid receptor 1. J. Biol. Chem. 284, 17527-17539
    • (2009) J. Biol. Chem. , vol.284 , pp. 17527-17539
    • Smith, N.J.1    Stoddart, L.A.2    Devine, N.M.3    Jenkins, L.4    Milligan, G.5
  • 27
    • 80052730390 scopus 로고    scopus 로고
    • Ligand regulation of GPCR quaternary structure
    • Giraldo, J. and Pin, J. P., eds, Royal Society of Chemistry, London
    • Saenz del Burgo, L. and Milligan, G. (2011) Ligand regulation of GPCR quaternary structure. In G Protein-Coupled Receptors: from Structure to Function (Giraldo, J. and Pin, J. P., eds), pp. 111-152, Royal Society of Chemistry, London
    • (2011) G Protein-Coupled Receptors: From Structure to Function , pp. 111-152
    • Saenz Del Burgo, L.1    Milligan, G.2
  • 28
    • 38049061740 scopus 로고    scopus 로고
    • Light resonance energy transfer-based methods in the study of G protein-coupled receptor oligomerization
    • Gandía, J., Lluís, C., Ferré, S., Franco, R. and Ciruela, F. (2008) Light resonance energy transfer-based methods in the study of G protein-coupled receptor oligomerization. BioEssays 30, 82-89
    • (2008) BioEssays , vol.30 , pp. 82-89
    • Gandía, J.1    Lluís, C.2    Ferré, S.3    Franco, R.4    Ciruela, F.5
  • 29
    • 77952757509 scopus 로고    scopus 로고
    • Oligomeric size of the M2 muscarinic receptor in live cells as determined by quantitative fluorescence resonance energy transfer
    • Pisterzi, L. F., Jansma, D. B., Georgiou, J., Woodside, M. J., Chou, J. T., Angers, S., Raicu, V. and Wells, J. W. (2010) Oligomeric size of the M2 muscarinic receptor in live cells as determined by quantitative fluorescence resonance energy transfer. J. Biol. Chem. 285, 16723-16738
    • (2010) J. Biol. Chem. , vol.285 , pp. 16723-16738
    • Pisterzi, L.F.1    Jansma, D.B.2    Georgiou, J.3    Woodside, M.J.4    Chou, J.T.5    Angers, S.6    Raicu, V.7    Wells, J.W.8
  • 30
    • 79251591614 scopus 로고    scopus 로고
    • A new approach to analyze cell surface protein complexes reveals specific heterodimeric metabotropic glutamate receptors
    • Doumazane, E., Scholler, P., Zwier, J. M., Trinquet, E., Rondard, P. and Pin, J. P. (2011) A new approach to analyze cell surface protein complexes reveals specific heterodimeric metabotropic glutamate receptors. FASEB J. 25, 66-77
    • (2011) FASEB J. , vol.25 , pp. 66-77
    • Doumazane, E.1    Scholler, P.2    Zwier, J.M.3    Trinquet, E.4    Rondard, P.5    Pin, J.P.6
  • 32
    • 66849132354 scopus 로고    scopus 로고
    • Instability of a class a G protein-coupled receptor oligomer interface
    • Fonseca, J. M. and Lambert, N. A. (2009) Instability of a class a G protein-coupled receptor oligomer interface. Mol. Pharmacol. 75, 1296-1299
    • (2009) Mol. Pharmacol. , vol.75 , pp. 1296-1299
    • Fonseca, J.M.1    Lambert, N.A.2
  • 33
    • 69249158290 scopus 로고    scopus 로고
    • Allosteric communication between protomers of dopamine class A GPCR dimers modulates activation
    • Han, Y., Moreira, I. S., Urizar, E., Weinstein, H. and Javitch, J. A. (2009) Allosteric communication between protomers of dopamine class A GPCR dimers modulates activation. Nat. Chem. Biol. 5, 688-695
    • (2009) Nat. Chem. Biol. , vol.5 , pp. 688-695
    • Han, Y.1    Moreira, I.S.2    Urizar, E.3    Weinstein, H.4    Javitch, J.A.5
  • 34
    • 79952113692 scopus 로고    scopus 로고
    • The split luciferase complementation assay
    • Kato, N. and Jones, J. (2010) The split luciferase complementation assay. Methods Mol. Biol. 655, 359-376
    • (2010) Methods Mol. Biol. , vol.655 , pp. 359-376
    • Kato, N.1    Jones, J.2
  • 35
    • 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
  • 38
    • 34250666273 scopus 로고    scopus 로고
    • A monomeric G protein-coupled receptor isolated in a high-density lipoprotein particle efficiently activates its G protein
    • Whorton, M. R., Bokoch, M. P., Rasmussen, S. G., Huang, B., Zare, R. N., Kobilka, B. and Sunahara, R. K. (2007) A monomeric G protein-coupled receptor isolated in a high-density lipoprotein particle efficiently activates its G protein. Proc. Natl. Acad. Sci. U.S.A. 104, 7682-7687
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 7682-7687
    • Whorton, M.R.1    Bokoch, M.P.2    Rasmussen, S.G.3    Huang, B.4    Zare, R.N.5    Kobilka, B.6    Sunahara, R.K.7
  • 39
    • 66249144426 scopus 로고    scopus 로고
    • The structure and function of G-protein-coupled receptors
    • Rosenbaum, D. M., Rasmussen, S. G. and Kobilka, B. K. (2009) The structure and function of G-protein-coupled receptors. Nature 459, 356-363
    • (2009) Nature , vol.459 , pp. 356-363
    • Rosenbaum, D.M.1    Rasmussen, S.G.2    Kobilka, B.K.3
  • 40
    • 78049502261 scopus 로고    scopus 로고
    • Recent progress in the structure determination of GPCRs, a membrane protein family with high potential as pharmaceutical targets
    • Cherezov, V., Abola, E. and Stevens, R. C. (2010) Recent progress in the structure determination of GPCRs, a membrane protein family with high potential as pharmaceutical targets. Methods Mol. Biol. 654, 141-168
    • (2010) Methods Mol. Biol. , vol.654 , pp. 141-168
    • Cherezov, V.1    Abola, E.2    Stevens, R.C.3
  • 45
    • 77955058619 scopus 로고    scopus 로고
    • Lighting up multiprotein complexes: Lessons from GPCR oligomerization
    • Ciruela, F., Vilardaga, J. P. and Fernández-Dueñas, V. (2010) Lighting up multiprotein complexes: lessons from GPCR oligomerization. Trends Biotechnol. 28, 407-415
    • (2010) Trends Biotechnol. , vol.28 , pp. 407-415
    • Ciruela, F.1    Vilardaga, J.P.2    Fernández-Dueñas, V.3
  • 46
    • 70149112322 scopus 로고    scopus 로고
    • Semisynthetic fluorescent sensor proteins based on self-labeling protein tags
    • Brun, M. A., Tan, K. T., Nakata, E., Hinner, M. J. and Johnsson, K. (2009) Semisynthetic fluorescent sensor proteins based on self-labeling protein tags. J. Am. Chem. Soc. 131, 5873-5884
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 5873-5884
    • Brun, M.A.1    Tan, K.T.2    Nakata, E.3    Hinner, M.J.4    Johnsson, K.5
  • 49
    • 0346996806 scopus 로고    scopus 로고
    • Ligand specific up-regulation of a Renilla reniformis luciferase-tagged, structurally unstable muscarinic M3 chimeric G protein-coupled receptor
    • Zeng, F. Y., McLean, A. J., Milligan, G., Lerner, M., Chalmers, D. T. and Behan, D. P. (2003) Ligand specific up-regulation of a Renilla reniformis luciferase-tagged, structurally unstable muscarinic M3 chimeric G protein-coupled receptor. Mol. Pharmacol. 64, 1474-1484
    • (2003) Mol. Pharmacol. , vol.64 , pp. 1474-1484
    • Zeng, F.Y.1    McLean, A.J.2    Milligan, G.3    Lerner, M.4    Chalmers, D.T.5    Behan, D.P.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.