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Volumn 26, Issue 2, 2012, Pages 604-616

Structural aspects of M3 muscarinic acetylcholine receptor dimer formation and activation

Author keywords

Disulfidescanning mutagenesis; G protein coupled receptor; GPCR

Indexed keywords

CARBACHOL; CYSTEINE; DIMER; DISULFIDE; HETEROTRIMERIC GUANINE NUCLEOTIDE BINDING PROTEIN; MUSCARINIC M3 RECEPTOR;

EID: 84863045698     PISSN: 08926638     EISSN: 15306860     Source Type: Journal    
DOI: 10.1096/fj.11-191510     Document Type: Article
Times cited : (35)

References (38)
  • 2
    • 42149181885 scopus 로고    scopus 로고
    • Structural diversity of G protein-coupled receptors and significance for drug discovery
    • Lagerström, M. C., and Schiöth, H. B. (2008) Structural diversity of G protein-coupled receptors and significance for drug discovery. Nat. Rev. Drug Discov. 7, 339-357
    • (2008) Nat. Rev. Drug Discov. , vol.7 , pp. 339-357
    • Lagerström, M.C.1    Schiöth, H.B.2
  • 3
    • 0036174608 scopus 로고    scopus 로고
    • Dimerization: An emerging concept for G protein-coupled receptor ontogeny and function
    • DOI 10.1146/annurev.pharmtox.42.091701.082314
    • Angers, S., Salahpour, A., and Bouvier, M. (2002) Dimerization: an emerging concept for G protein-coupled receptor ontogeny and function. Annu. Rev. Pharmacol. Toxicol. 42, 409-435 (Pubitemid 34160532)
    • (2002) Annual Review of Pharmacology and Toxicology , vol.42 , pp. 409-435
    • Angers, S.1    Salahpour, A.2    Bouvier, M.3
  • 4
    • 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
  • 5
    • 78049281844 scopus 로고    scopus 로고
    • Oligomeric forms of G protein-coupled receptors (GPCRs)
    • Palczewski, K. (2010) Oligomeric forms of G protein-coupled receptors (GPCRs). Trends Biochem. Sci. 35, 595-600
    • (2010) Trends Biochem. Sci. , vol.35 , pp. 595-600
    • Palczewski, K.1
  • 11
    • 73049085563 scopus 로고    scopus 로고
    • The asymmetric/symmetric activation of GPCR dimers as a possible mechanistic rationale for multiple signalling pathways
    • Rovira, X., Pin, J. P., and Giraldo, J. (2010) The asymmetric/symmetric activation of GPCR dimers as a possible mechanistic rationale for multiple signalling pathways. Trends Pharmacol. Sci. 31, 15-21
    • (2010) Trends Pharmacol. Sci. , vol.31 , pp. 15-21
    • Rovira, X.1    Pin, J.P.2    Giraldo, J.3
  • 12
    • 1942468189 scopus 로고    scopus 로고
    • The G protein-coupled receptor rhodopsin in the native membrane
    • DOI 10.1016/S0014-5793(04)00194-2, PII S0014579304001942
    • Fotiadis, D., Liang, Y., Filipek, S., Saperstein, D. A., Engel, A., and Palczewski, K. (2004) The G protein-coupled receptor rhodopsin in the native membrane. FEBS Lett. 564, 281-288 (Pubitemid 38520934)
    • (2004) FEBS Letters , vol.564 , Issue.3 , pp. 281-288
    • Fotiadis, D.1    Liang, Y.2    Filipek, S.3    Saperstein, D.A.4    Engel, A.5    Palczewski, K.6
  • 13
    • 21344467203 scopus 로고    scopus 로고
    • The study of G-protein coupled receptor oligomerization with computational modeling and bioinformatics
    • DOI 10.1111/j.1742-4658.2005.04730.x
    • Filizola, M., and Weinstein, H. (2005) The study of G-protein coupled receptor oligomerization with computational modeling and bioinformatics. FEBS J. 272, 2926-2938 (Pubitemid 40904681)
    • (2005) FEBS Journal , vol.272 , Issue.12 , pp. 2926-2938
    • Filizola, M.1    Weinstein, H.2
  • 14
    • 80051480604 scopus 로고    scopus 로고
    • Structural basis of M3 muscarinic receptor dimer/oligomer formation
    • McMillin, S. M., Heusel, M., Liu, T., Costanzi, S., and Wess, J. (2011) Structural basis of M3 muscarinic receptor dimer/oligomer formation. J. Biol. Chem. 286, 28584-28598
    • (2011) J. Biol. Chem. , vol.286 , pp. 28584-28598
    • McMillin, S.M.1    Heusel, M.2    Liu, T.3    Costanzi, S.4    Wess, J.5
  • 15
    • 0029789994 scopus 로고    scopus 로고
    • Molecular biology of muscarinic acetylcholine receptors
    • Wess, J. (1996) Molecular biology of muscarinic acetylcholine receptors. Crit. Rev. Neurobiol. 10, 69-99
    • (1996) Crit. Rev. Neurobiol. , vol.10 , pp. 69-99
    • Wess, J.1
  • 16
    • 0032402450 scopus 로고    scopus 로고
    • Molecular basis of receptor/G-protein-coupling selectivity
    • Wess, J. (1998) Molecular basis of receptor/G-protein-coupling selectivity. Pharmacol. Ther. 80, 231-264
    • (1998) Pharmacol. Ther. , vol.80 , pp. 231-264
    • Wess, J.1
  • 19
  • 21
    • 0035120732 scopus 로고    scopus 로고
    • i/o activation profiles in CHO cells expressing human muscarinic acetylcholine receptors: Dependence on agonist as well as receptor-subtype
    • Akam, E. C., Challiss, R. A. J., and Nahorski, S. R. (2001) Gq/11 and Gi/o activation profiles in CHO cells expressing human muscarinic acetylcholine receptors: dependence on agonist as well as receptor-subtype. Br. J. Pharmacol. 132, 950-958 (Pubitemid 32193653)
    • (2001) British Journal of Pharmacology , vol.132 , Issue.4 , pp. 950-958
    • Akam, E.C.1    Challiss, R.A.J.2    Nahorski, S.R.3
  • 22
    • 0033522912 scopus 로고    scopus 로고
    • Use of a disulfide cross-linking strategy to study muscarinic receptor structure and mechanisms of activation
    • Zeng, F. Y., Hopp, A., Soldner, A., and Wess, J. (1999) Use of a disulfide cross-linking strategy to study muscarinic receptor structure and mechanisms of activation. J. Biol. Chem. 274, 16629-16640
    • (1999) J. Biol. Chem. , vol.274 , pp. 16629-16640
    • Zeng, F.Y.1    Hopp, A.2    Soldner, A.3    Wess, J.4
  • 23
  • 24
    • 0037127315 scopus 로고    scopus 로고
    • 3 muscarinic acetylcholine receptor activation probed by the use of an in situ disulfide cross-linking strategy
    • DOI 10.1074/jbc.M107647200
    • Ward, S. D., Hamdan, F. F., Bloodworth, L. M., and Wess, J. (2002) Conformational changes that occur during M3 muscarinic acetylcholine receptor activation probed by the use of an in situ disulfide cross-linking strategy. J. Biol. Chem. 277, 2247-2257 (Pubitemid 34968812)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.3 , pp. 2247-2257
    • Ward, S.D.C.1    Hamdan, F.F.2    Bloodworth, L.M.3    Wess, J.4
  • 25
  • 28
    • 43949095157 scopus 로고    scopus 로고
    • 2-adrenergic receptor
    • 2-adrenergic receptor. J. Med. Chem. 51, 2907-2914
    • (2008) J. Med. Chem. , vol.51 , pp. 2907-2914
    • Costanzi, S.1
  • 29
    • 67349088738 scopus 로고    scopus 로고
    • Community-wide assessment of GPCR structure modelling and ligand docking: GPCR Dock 2008
    • 2008 Participants, G., Brooks, C. R., Dixon, J., Moult, J., and Stevens, R.
    • Michino, M., Abola, E., 2008 Participants, G., Brooks, C. R., Dixon, J., Moult, J., and Stevens, R. (2009) Community-wide assessment of GPCR structure modelling and ligand docking: GPCR Dock 2008. Nat. Rev. Drug Discov. 8, 455- 463
    • (2009) Nat. Rev. Drug Discov. , vol.8 , pp. 455-463
    • Michino, M.1    Abola, E.2
  • 30
    • 77955113796 scopus 로고    scopus 로고
    • Modelling G protein-coupled receptors: A concrete possibility
    • Costanzi, S. (2010) Modelling G protein-coupled receptors: a concrete possibility. Chim. Oggi. 28, 26-30
    • (2010) Chim. Oggi. , vol.28 , pp. 26-30
    • Costanzi, S.1
  • 31
    • 84855757480 scopus 로고    scopus 로고
    • version 2010.10. Chemical Computing Group, Montreal, QC, Canada
    • Chemical Computing Group (2010) The molecular operating environment (MOE), version 2010.10. Chemical Computing Group, Montreal, QC, Canada, http://www.chemcomp.com
    • (2010) The Molecular Operating Environment (MOE)
  • 34
    • 33646500642 scopus 로고    scopus 로고
    • Quantitative analysis of muscarinic acetylcholine receptor homo- and heterodimerization in live cells: Regulation of receptor down-regulation by heterodimerization
    • DOI 10.1074/jbc.M507476200
    • Goin, J. C., and Nathanson, N. M. (2006) Quantitative analysis of muscarinic acetylcholine receptor homo- and heterodimerization in live cells: regulation of receptor downregulation by heterodimerization. J. Biol. Chem. 281, 5416-5425 (Pubitemid 43847636)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.9 , pp. 5416-5425
    • Goin, J.C.1    Nathanson, N.M.2
  • 35
    • 0038576278 scopus 로고    scopus 로고
    • The fourth transmembrane segment forms the interface of the dopamine D2 receptor homodimer
    • DOI 10.1074/jbc.C200679200
    • Guo, W., Shi, L., and Javitch, J. A. (2003) The fourth transmembrane segment forms the interface of the dopamine D2 receptor homodimer. J. Biol. Chem. 278, 4385-4388 (Pubitemid 36800928)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.7 , pp. 4385-4388
    • Guo, W.1    Shi, L.2    Javitch, J.A.3
  • 37
    • 0030041761 scopus 로고    scopus 로고
    • Amino acid side chains that define muscarinic receptor/G-protein coupling: Studies of the third intracellular loop
    • DOI 10.1074/jbc.271.6.2882
    • Burstein, E. S., Spalding, T. A., and Brann, M. R. (1996) Amino acid side chains that define muscarinic receptor/G-protein coupling. Studies of the third intracellular loop. J. Biol. Chem. 271, 2882-2885 (Pubitemid 26055585)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.6 , pp. 2882-2885
    • Burstein, E.S.1    Spalding, T.A.2    Brann, M.R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.