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Volumn 25, Issue 8, 2011, Pages 1416-1430

The extreme C-terminal region of Gα s differentially couples to the luteinizing hormone and β 2-adrenergic receptors

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; BETA 2 ADRENERGIC RECEPTOR; GUANINE NUCLEOTIDE BINDING PROTEIN ALPHA SUBUNIT; LUTEINIZING HORMONE; LUTEINIZING HORMONE RECEPTOR;

EID: 79960981624     PISSN: 08888809     EISSN: None     Source Type: Journal    
DOI: 10.1210/me.2011-0009     Document Type: Article
Times cited : (10)

References (64)
  • 1
    • 34147137118 scopus 로고    scopus 로고
    • Seven transmembrane receptors: Something old, something new
    • Lefkowitz RJ 2007 Seven transmembrane receptors: something old, something new. Acta Physiol (Oxf) 190:9-19
    • (2007) Acta Physiol (Oxf) , vol.190 , pp. 9-19
    • Lefkowitz, R.J.1
  • 2
    • 0038024615 scopus 로고    scopus 로고
    • The G-protein-coupled receptors in the human genome form five main families. Phylogenetic analysis, paralogon groups, and fingerprints
    • Fredriksson R, Lagerström MC, Lundin LG, Schiöth HB 2003 The G-protein-coupled receptors in the human genome form five main families. Phylogenetic analysis, paralogon groups, and fingerprints. Mol Pharmacol 63:1256-1272
    • (2003) Mol Pharmacol , vol.63 , pp. 1256-1272
    • Fredriksson, R.1    Lagerström, M.C.2    Lundin, L.G.3    Schiöth, H.B.4
  • 4
    • 0037316238 scopus 로고    scopus 로고
    • A naive Bayes model to predict coupling between seven trans-membrane domain receptors and G-proteins
    • Cao J, Panetta R, Yue S, Steyaert A, Young-Bellido M, Ahmad S 2003 A naive Bayes model to predict coupling between seven trans-membrane domain receptors and G-proteins. Bioinformatics 19: 234-240
    • (2003) Bioinformatics , vol.19 , pp. 234-240
    • Cao, J.1    Panetta, R.2    Yue, S.3    Steyaert, A.4    Young-Bellido, M.5    Ahmad, S.6
  • 5
    • 27944445874 scopus 로고    scopus 로고
    • Prediction of the coupling specificity of GPCR to four families of G-proteins using hidden Markov models and artificial neural networks
    • Sgourakis NG, Bagos PG, Hamodrakas SJ 2005 Prediction of the coupling specificity of GPCR to four families of G-proteins using hidden Markov models and artificial neural networks. Bioinformat-ics 21:4101-4106
    • (2005) Bioinformat-ics , vol.21 , pp. 4101-4106
    • Sgourakis, N.G.1    Bagos, P.G.2    Hamodrakas, S.J.3
  • 6
    • 38049070335 scopus 로고    scopus 로고
    • Contributions of intracellular loops 2 and 3 of the lutropin receptor in Gs coupling
    • Angelova K, Fanelli F, Puett D 2008 Contributions of intracellular loops 2 and 3 of the lutropin receptor in Gs coupling. Mol Endo-crinol 22:126-138
    • (2008) Mol Endo-crinol , vol.22 , pp. 126-138
    • Angelova, K.1    Fanelli, F.2    Puett, D.3
  • 8
    • 3042798261 scopus 로고    scopus 로고
    • Molecular mechanisms of ligand binding, signaling, and regulation within the superfamily of G-protein-coupled receptors: Molecular modeling and mutagenesis approaches to receptor structure and function
    • Kristiansen K 2004 Molecular mechanisms of ligand binding, signaling, and regulation within the superfamily of G-protein-coupled receptors: molecular modeling and mutagenesis approaches to receptor structure and function. Pharmacol Ther 103:21-80
    • (2004) Pharmacol Ther , vol.103 , pp. 21-80
    • Kristiansen, K.1
  • 10
    • 77956635542 scopus 로고    scopus 로고
    • Differential association modes of the thrombin receptor PAR1 with Gαi1, Gα12, and β-arrestin 1
    • Ayoub MA, Trinquet E, Pfleger KD, Pin JP 2010 Differential association modes of the thrombin receptor PAR1 with Gαi1, Gα12, and β-arrestin 1. FASEB J 24:3522-3535
    • (2010) FASEB J , vol.24 , pp. 3522-3535
    • Ayoub, M.A.1    Trinquet, E.2    Pfleger, K.D.3    Pin, J.P.4
  • 11
    • 0030987069 scopus 로고    scopus 로고
    • How receptors talk to trimeric G proteins
    • Bourne HR 1997 How receptors talk to trimeric G proteins. Curr Opin Cell Biol 9:134-142
    • (1997) Curr Opin Cell Biol , vol.9 , pp. 134-142
    • Bourne, H.R.1
  • 13
    • 0030938936 scopus 로고    scopus 로고
    • G-protein-coupled receptors: Molecular mechanisms involved in receptor activation and selectivity of G-protein recognition
    • Wess J 1997 G-protein-coupled receptors: molecular mechanisms involved in receptor activation and selectivity of G-protein recognition. FASEB J 11:346-354
    • (1997) FASEB J , vol.11 , pp. 346-354
    • Wess, J.1
  • 14
    • 0027245830 scopus 로고
    • Substitution of three amino acids switches receptor specificity of Gqa to that of Gia
    • Conklin BR, Farfel Z, Lustig KD, Julius D, Bourne HR 1993 Substitution of three amino acids switches receptor specificity of Gqa to that of Gia. Nature 363:274-276
    • (1993) Nature , vol.363 , pp. 274-276
    • Conklin, B.R.1    Farfel, Z.2    Lustig, K.D.3    Julius, D.4    Bourne, H.R.5
  • 16
    • 0344609797 scopus 로고    scopus 로고
    • A dominant-negative strategy for studying roles of G proteins in vivo
    • Gilchrist A, Bünemann M, Li A, Hosey MM, Hamm HE 1999 A dominant-negative strategy for studying roles of G proteins in vivo. J Biol Chem 274:6610-6616
    • (1999) J Biol Chem , vol.274 , pp. 6610-6616
    • Gilchrist, A.1    Bünemann, M.2    Li, A.3    Hosey, M.M.4    Hamm, H.E.5
  • 17
    • 0025193724 scopus 로고
    • Identification of a Gs-protein coupling domain to the β-adrenoceptor using site-specific synthetic peptides. Carboxyl terminus of Gsa is involved in coupling to β-adrenoceptors
    • Palm D, Munch G, Malek D, Dees C, Hekman M 1990 Identification of a Gs-protein coupling domain to the β-adrenoceptor using site-specific synthetic peptides. Carboxyl terminus of Gsa is involved in coupling to β-adrenoceptors. FEBS Lett 261:294-298
    • (1990) FEBS Lett , vol.261 , pp. 294-298
    • Palm, D.1    Munch, G.2    Malek, D.3    Dees, C.4    Hekman, M.5
  • 21
    • 0028101036 scopus 로고
    • Synthetic peptides as probes for G protein function. Carboxyl-terminal Gas peptides mimic Gs and evoke high affinity agonist binding to β-adrenergic receptors
    • Rasenick MM, Watanabe M, Lazarevic MB, Hatta S, Hamm HE 1994 Synthetic peptides as probes for G protein function. Carboxyl-terminal Gas peptides mimic Gs and evoke high affinity agonist binding to β-adrenergic receptors. J Biol Chem 269:21519-21525
    • (1994) J Biol Chem , vol.269 , pp. 21519-21525
    • Rasenick, M.M.1    Watanabe, M.2    Lazarevic, M.B.3    Hatta, S.4    Hamm, H.E.5
  • 23
    • 21244464385 scopus 로고    scopus 로고
    • Distinct mechanisms of cAMP induction by constitutively activating LH receptor and wild-type LH receptor activated by hCG
    • Lee C, Ji I, Ji TH 2004 Distinct mechanisms of cAMP induction by constitutively activating LH receptor and wild-type LH receptor activated by hCG. Endocrine 25:111-115
    • (2004) Endocrine , vol.25 , pp. 111-115
    • Lee, C.1    Ji, I.2    Ji, T.H.3
  • 24
    • 79960983193 scopus 로고    scopus 로고
    • Signal transduction by G proteins: Basic principles, molecular diversity, and structural basis of their action
    • In: Bradshaw RA, Dennis EA, eds., MA: Academic Press/Elsevier
    • Birnbaumer L 2010 Signal transduction by G proteins: basic principles, molecular diversity, and structural basis of their action. In: Bradshaw RA, Dennis EA, eds. Handbook of cell signaling. Burlington, MA: Academic Press/Elsevier; 1597-1614
    • (2010) Handbook of Cell Signaling. Burlington , pp. 1597-1614
    • Birnbaumer, L.1
  • 25
    • 79960980146 scopus 로고    scopus 로고
    • Structures of heterotrimeric G proteins and their complexes
    • In: Bradshaw RA, Dennis EA, eds., 2nd ed. Burlington, MA: Academic Press/Elsevier
    • Sprang SR 2010 Structures of heterotrimeric G proteins and their complexes. In: Bradshaw RA, Dennis EA, eds. Handbook of cell signaling. 2nd ed. Burlington, MA: Academic Press/Elsevier; 119-128
    • (2010) Handbook of Cell Signaling , pp. 119-128
    • Sprang, S.R.1
  • 26
    • 0034098381 scopus 로고    scopus 로고
    • sa in which substitutions decrease receptor-mediated activation and increase receptor affinity
    • Grishina G, Berlot CH 2000 A surface-exposed region of Gsa in which substitutions decrease receptor-mediated activation and increase receptor affinity. Mol Pharmacol 57:1081-1092
    • (2000) Mol Pharmacol , vol.57 , pp. 1081-1092
    • Grishina, G.1    Berlot, C.H.2
  • 27
  • 28
    • 0031842511 scopus 로고    scopus 로고
    • Receptor-mediated activation of Gsa: Evidence for intramolecular signal transduction
    • Marsh SR, Grishina G, Wilson PT, Berlot CH 1998 Receptor-mediated activation of Gsa: evidence for intramolecular signal transduction. Mol Pharmacol 53:981-990
    • (1998) Mol Pharmacol , vol.53 , pp. 981-990
    • Marsh, S.R.1    Grishina, G.2    Wilson, P.T.3    Berlot, C.H.4
  • 30
    • 0032475966 scopus 로고    scopus 로고
    • Extreme C terminus of G protein a-subunits contains a site that discriminates between Gi-coupled metabotropic glutamate receptors
    • Blahos 2nd J, Mary S, Perroy J, de Colle C, Brabet I, Bockaert J, Pin JP 1998 Extreme C terminus of G protein a-subunits contains a site that discriminates between Gi-coupled metabotropic glutamate receptors. J Biol Chem 273:25765-25769
    • (1998) J Biol Chem , vol.273 , pp. 25765-25769
    • Blahos, J.1    Mary, S.2    Perroy, J.3    de Colle, C.4    Brabet, I.5    Bockaert, J.6    Pin, J.P.7
  • 33
    • 0031436245 scopus 로고    scopus 로고
    • Crystal structure of the adenylyl cyclase activator Gsa
    • Sunahara RK, Tesmer JJ, Gilman AG, Sprang SR 1997 Crystal structure of the adenylyl cyclase activator Gsa. Science 278:1943-1947
    • (1997) Science , vol.278 , pp. 1943-1947
    • Sunahara, R.K.1    Tesmer, J.J.2    Gilman, A.G.3    Sprang, S.R.4
  • 34
    • 2642689663 scopus 로고    scopus 로고
    • Crystal structure of the catalytic domains of adenylyl cyclase in a complex with Gsa.GTP7S
    • Tesmer JJ, Sunahara RK, Gilman AG, Sprang SR 1997 Crystal structure of the catalytic domains of adenylyl cyclase in a complex with Gsa.GTP7S. Science 278:1907-1916
    • (1997) Science , vol.278 , pp. 1907-1916
    • Tesmer, J.J.1    Sunahara, R.K.2    Gilman, A.G.3    Sprang, S.R.4
  • 36
    • 0030753197 scopus 로고    scopus 로고
    • Identification of common and distinct residues involved in the interaction of ai2 and as with adenylyl cyclase
    • Grishina G, Berlot CH 1997 Identification of common and distinct residues involved in the interaction of ai2 and as with adenylyl cyclase. J Biol Chem 272:20619-20626
    • (1997) J Biol Chem , vol.272 , pp. 20619-20626
    • Grishina, G.1    Berlot, C.H.2
  • 37
    • 0026552077 scopus 로고
    • Identification of effector-activating residues of Gsa
    • Berlot CH, Bourne HR 1992 Identification of effector-activating residues of Gsa. Cell 68:911-922
    • (1992) Cell , vol.68 , pp. 911-922
    • Berlot, C.H.1    Bourne, H.R.2
  • 39
    • 84884013649 scopus 로고    scopus 로고
    • The gonadotropins and their receptors
    • In: Strauss III JF, Barbieri R, eds., 6th ed. Philadelphia: Elsevier
    • Ascoli M, Puett D 2009 The gonadotropins and their receptors. In: Strauss III JF, Barbieri R, eds. Yen and Jaffee's reproductive endocrinology. 6th ed. Philadelphia: Elsevier; 35-55
    • (2009) Yen and Jaffee's Reproductive Endocrinology , pp. 35-55
    • Ascoli, M.1    Puett, D.2
  • 41
    • 0016772772 scopus 로고
    • Cyclic AMP-dependent protein kinase: Pivotal role in regulation of enzyme induction and growth
    • Insel PA, Bourne HR, Coffino P, Tomkins GM 1975 Cyclic AMP-dependent protein kinase: pivotal role in regulation of enzyme induction and growth. Science 190:896-898
    • (1975) Science , vol.190 , pp. 896-898
    • Insel, P.A.1    Bourne, H.R.2    Coffino, P.3    Tomkins, G.M.4
  • 42
    • 0016669563 scopus 로고
    • Selection of a variant lymphoma cell deficient in adenylate cyclase
    • Bourne HR, Coffino P, Tomkins GM 1975 Selection of a variant lymphoma cell deficient in adenylate cyclase. Science 187:750-752
    • (1975) Science , vol.187 , pp. 750-752
    • Bourne, H.R.1    Coffino, P.2    Tomkins, G.M.3
  • 43
    • 0036217072 scopus 로고    scopus 로고
    • The lutropin/choriogonado-tropin receptor, a 2002 perspective
    • Ascoli M, Fanelli F, Segaloff DL 2002 The lutropin/choriogonado-tropin receptor, a 2002 perspective. Endocr Rev 23:141-174
    • (2002) Endocr Rev , vol.23 , pp. 141-174
    • Ascoli, M.1    Fanelli, F.2    Segaloff, D.L.3
  • 44
    • 0038783679 scopus 로고    scopus 로고
    • The luteinizing hormone receptor: Influence of buffer composition on ligand binding and signaling of wild type and mutant receptors
    • Angelova K, Narayan P, Puett D 2003 The luteinizing hormone receptor: influence of buffer composition on ligand binding and signaling of wild type and mutant receptors. Mol Cell Endocrinol 204:1-9
    • (2003) Mol Cell Endocrinol , vol.204 , pp. 1-9
    • Angelova, K.1    Narayan, P.2    Puett, D.3
  • 45
    • 0024854388 scopus 로고
    • Mutations of GSa designed to alter the reactivity of the protein with bacterial toxins. Substitutions at ARG187 result in loss of GTPase activity
    • Freissmuth M, Gilman AG 1989 Mutations of GSa designed to alter the reactivity of the protein with bacterial toxins. Substitutions at ARG187 result in loss of GTPase activity. J Biol Chem 264: 21907-21914
    • (1989) J Biol Chem , vol.264 , pp. 21907-21914
    • Freissmuth, M.1    Gilman, A.G.2
  • 46
    • 79960981992 scopus 로고    scopus 로고
    • Heterotrimeric G-protein signaling at atomic resolution
    • In: Bradshaw RA, Dennis EA, eds., 2nd ed. Burlington, MA: Academic Press/Elsevier
    • Lambright DG 2010 Heterotrimeric G-protein signaling at atomic resolution. In: Bradshaw RA, Dennis EA, eds. Handbook of cell signaling. 2nd ed. Burlington, MA: Academic Press/Elsevier; 1615-1619
    • (2010) Handbook of Cell Signaling , pp. 1615-1619
    • Lambright, D.G.1
  • 47
    • 0027456404 scopus 로고
    • Functional domains of the Gsa sub-unit: Role of the C-terminus in the receptor-dependent and receptor-independent activation
    • Pantaloni C, Audigier Y 1993 Functional domains of the Gsa sub-unit: role of the C-terminus in the receptor-dependent and receptor-independent activation. J Recept Res 13:591-608
    • (1993) J Recept Res , vol.13 , pp. 591-608
    • Pantaloni, C.1    Audigier, Y.2
  • 49
    • 47049130668 scopus 로고    scopus 로고
    • Crystal structure of the ligand-free G-protein-coupled receptor opsin
    • Park JH, Scheerer P, Hofmann KP, Choe HW, Ernst OP 2008 Crystal structure of the ligand-free G-protein-coupled receptor opsin. Nature 454:183-187
    • (2008) Nature , vol.454 , pp. 183-187
    • Park, J.H.1    Scheerer, P.2    Hofmann, K.P.3    Choe, H.W.4    Ernst, O.P.5
  • 52
    • 0028172104 scopus 로고
    • A novel Gsa mutant in a patient with Albright hereditary osteodystrophy uncouples cell surface receptors from adenylyl cyclase
    • Schwindinger WF, Miric A, Zimmerman D, Levine MA 1994 A novel Gsa mutant in a patient with Albright hereditary osteodystrophy uncouples cell surface receptors from adenylyl cyclase. J Biol Chem 269:25387-25391
    • (1994) J Biol Chem , vol.269 , pp. 25387-25391
    • Schwindinger, W.F.1    Miric, A.2    Zimmerman, D.3    Levine, M.A.4
  • 54
    • 41549137044 scopus 로고    scopus 로고
    • Mechanisms of inter- and intramolecular communication in GPCR and G proteins
    • Raimondi F, Seeber M, Benedetti PG, Fanelli F 2008 Mechanisms of inter- and intramolecular communication in GPCR and G proteins. J Am Chem Soc 130:4310-4325
    • (2008) J Am Chem Soc , vol.130 , pp. 4310-4325
    • Raimondi, F.1    Seeber, M.2    Benedetti, P.G.3    Fanelli, F.4
  • 56
    • 0023062991 scopus 로고
    • G proteins: Transducers of receptor-generated signals
    • Gilman AG 1987 G proteins: transducers of receptor-generated signals. Annu Rev Biochem 56:615-649
    • (1987) Annu Rev Biochem , vol.56 , pp. 615-649
    • Gilman, A.G.1
  • 57
    • 37549016836 scopus 로고    scopus 로고
    • Heterotrimeric G protein activation by G-protein-coupled receptors
    • Oldham WM, Hamm HE 2008 Heterotrimeric G protein activation by G-protein-coupled receptors. Nat Rev Mol Cell Biol 9:60-71
    • (2008) Nat Rev Mol Cell Biol , vol.9 , pp. 60-71
    • Oldham, W.M.1    Hamm, H.E.2
  • 58
    • 0024556150 scopus 로고
    • Engineering hybrid genes without the use of restriction enzymes: Gene splicing by overlap extension
    • Horton RM, Hunt HD, Ho SN, Pullen JK, Pease LR 1989 Engineering hybrid genes without the use of restriction enzymes: gene splicing by overlap extension. Gene 77:61-68
    • (1989) Gene , vol.77 , pp. 61-68
    • Horton, R.M.1    Hunt, H.D.2    Ho, S.N.3    Pullen, J.K.4    Pease, L.R.5
  • 59
    • 0035722086 scopus 로고    scopus 로고
    • Expression and functional analysis of G protein a subunits in S49 lymphoma cells
    • Berlot CH 2002 Expression and functional analysis of G protein a subunits in S49 lymphoma cells. Methods Enzymol 344:261-277
    • (2002) Methods Enzymol , vol.344 , pp. 261-277
    • Berlot, C.H.1
  • 60
    • 0029856730 scopus 로고    scopus 로고
    • Protein engineering of a novel constitutively active hormone-receptor complex
    • Wu C, Narayan P, Puett D 1996 Protein engineering of a novel constitutively active hormone-receptor complex. J Biol Chem 271: 31638-31642
    • (1996) J Biol Chem , vol.271 , pp. 31638-31642
    • Wu, C.1    Narayan, P.2    Puett, D.3
  • 61
    • 0242322528 scopus 로고    scopus 로고
    • An implicit membrane generalized born theory for the study of structure, stability, and interactions of membrane proteins
    • Im W, Feig M, Brooks 3rd CL 2003 An implicit membrane generalized born theory for the study of structure, stability, and interactions of membrane proteins. Biophys J 85:2900-2918
    • (2003) Biophys J , vol.85 , pp. 2900-2918
    • Im, W.1    Feig, M.2    Brooks, C.L.3
  • 64
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • Sali A, Blundell TL 1993 Comparative protein modelling by satisfaction of spatial restraints. J Mol Biol 234:779-815
    • (1993) J Mol Biol , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2


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