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Volumn 171, Issue 16, 2014, Pages 3827-3844

Effect of a toggle switch mutation in TM6 of the human adenosine A 3 receptor on Gi protein-dependent signalling and Gi-independent receptor internalization

Author keywords

[No Author keywords available]

Indexed keywords

2 (1 HEXYNYL) N METHYLADENOSINE; ADENOSINE 5' (N ETHYLCARBOXAMIDE); ADENOSINE A3 RECEPTOR; ADENOSINE A3 RECEPTOR AGONIST; BETA ARRESTIN 2; CYCLIC AMP; INHIBITORY GUANINE NUCLEOTIDE BINDING PROTEIN; MITOGEN ACTIVATED PROTEIN KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE 3; MUTANT PROTEIN; PHENYLALANINE; TRITIUM; UNCLASSIFIED DRUG; YELLOW FLUORESCENT PROTEIN; 2-HEXYN-1-YL-N(6)-METHYLADENOSINE; ADENOSINE; ADENOSINE RECEPTOR STIMULATING AGENT; BETA ARRESTIN; GUANINE NUCLEOTIDE BINDING PROTEIN; RETINA S ANTIGEN;

EID: 84905028134     PISSN: 00071188     EISSN: 14765381     Source Type: Journal    
DOI: 10.1111/bph.12739     Document Type: Article
Times cited : (29)

References (50)
  • 2
    • 0141593597 scopus 로고    scopus 로고
    • Beta-arrestin-mediated activation of MAPK by inverse agonists reveals distinct active conformations for G protein-coupled receptors
    • Azzi M, Charest PG, Angers S, Rousseau G, Kohout T, Bouvier M, et-al. (2003). Beta-arrestin-mediated activation of MAPK by inverse agonists reveals distinct active conformations for G protein-coupled receptors. Proc Natl Acad Sci 11406-11411.
    • (2003) Proc Natl Acad Sci , pp. 11406-11411
    • Azzi, M.1    Charest, P.G.2    Angers, S.3    Rousseau, G.4    Kohout, T.5    Bouvier, M.6
  • 3
    • 0345735773 scopus 로고    scopus 로고
    • Agonist and inverse agonist actions of beta-blockers at the human beta(2)-adrenoceptor provide evidence for agonist-directed signaling
    • Baker JG, Hall IP, Hill SJ, (2003). Agonist and inverse agonist actions of beta-blockers at the human beta(2)-adrenoceptor provide evidence for agonist-directed signaling. Mol Pharmacol 64: 1357-1369.
    • (2003) Mol Pharmacol , vol.64 , pp. 1357-1369
    • Baker, J.G.1    Hall, I.P.2    Hill, S.J.3
  • 4
    • 0036790646 scopus 로고    scopus 로고
    • Pharmacological characterization of CGP 12177 at the human beta(2)-adrenoceptor
    • Baker JG, Hall IP, Hill SJ, (2002). Pharmacological characterization of CGP 12177 at the human beta(2)-adrenoceptor. Br J Pharmacol 137: 400-408.
    • (2002) Br J Pharmacol , vol.137 , pp. 400-408
    • Baker, J.G.1    Hall, I.P.2    Hill, S.J.3
  • 5
    • 1842480997 scopus 로고    scopus 로고
    • Temporal characteristics of cAMP response element-mediated gene transcription: Requirement for sustained cAMP production
    • Baker JG, Hall IP, Hill SJ, (2004). Temporal characteristics of cAMP response element-mediated gene transcription: requirement for sustained cAMP production. Mol Pharmacol 65: 986-998.
    • (2004) Mol Pharmacol , vol.65 , pp. 986-998
    • Baker, J.G.1    Hall, I.P.2    Hill, S.J.3
  • 6
    • 84864754839 scopus 로고    scopus 로고
    • Persistent signaling by thyrotropin-releasing hormone receptors correlates with G-protein and receptor levels
    • Boutin A, Allen MD, Neumann S, Gershengorn MC, (2012). Persistent signaling by thyrotropin-releasing hormone receptors correlates with G-protein and receptor levels. FASEB J 26: 3473-3482.
    • (2012) FASEB J , vol.26 , pp. 3473-3482
    • Boutin, A.1    Allen, M.D.2    Neumann, S.3    Gershengorn, M.C.4
  • 7
    • 80052082999 scopus 로고    scopus 로고
    • Structural insights into agonist-induced activation of G protein-coupled receptors
    • Deupi X, Standfuss J, (2011). Structural insights into agonist-induced activation of G protein-coupled receptors. Curr Opin Struct Biol 21: 541-551.
    • (2011) Curr Opin Struct Biol , vol.21 , pp. 541-551
    • Deupi, X.1    Standfuss, J.2
  • 8
    • 0023838105 scopus 로고
    • Influence of rolipram on the cyclic 3′,5′-adenosine- monophosphate response to histamine and adenosine in slices of guinea-pig cerebral cortex
    • Donaldson J, Brown AM, Hill SJ, (1988). Influence of rolipram on the cyclic 3′,5′-adenosine-monophosphate response to histamine and adenosine in slices of guinea-pig cerebral cortex. Biochem Pharmacol 37: 715-723.
    • (1988) Biochem Pharmacol , vol.37 , pp. 715-723
    • Donaldson, J.1    Brown, A.M.2    Hill, S.J.3
  • 9
    • 0029907599 scopus 로고    scopus 로고
    • Requirement of rigid-body motion of transmembrane helices for light activation of rhodopsin
    • Farrens DL, Altenbach C, Yang K, Hubbell WL, Khorana HG, (1996). Requirement of rigid-body motion of transmembrane helices for light activation of rhodopsin. Science 274: 768-770.
    • (1996) Science , vol.274 , pp. 768-770
    • Farrens, D.L.1    Altenbach, C.2    Yang, K.3    Hubbell, W.L.4    Khorana, H.G.5
  • 11
    • 0037126682 scopus 로고    scopus 로고
    • Subtype-specific regulation of receptor internalization and recycling by the carboxyl-terminal domains of the human A(1) and rat A(3) adenosine receptors: Consequences for agonist-stimulated translocation of arrestin3
    • Ferguson G, Watterson KR, Palmer TM, (2002). Subtype-specific regulation of receptor internalization and recycling by the carboxyl-terminal domains of the human A(1) and rat A(3) adenosine receptors: consequences for agonist-stimulated translocation of arrestin3. Biochem 41: 14748-14761.
    • (2002) Biochem , vol.41 , pp. 14748-14761
    • Ferguson, G.1    Watterson, K.R.2    Palmer, T.M.3
  • 12
    • 79952033865 scopus 로고    scopus 로고
    • International Union of Basic and Clinical Pharmacology. LXXXI. Nomenclature and classification of adenosine receptors-an update
    • Fredholm BB, IJzerman AP, Jacobson KA, Linden J, Müller CE, (2011). International Union of Basic and Clinical Pharmacology. LXXXI. Nomenclature and classification of adenosine receptors-an update. Pharmacol Rev 63: 1-34.
    • (2011) Pharmacol Rev , vol.63 , pp. 1-34
    • Fredholm, B.B.1    Ijzerman, A.P.2    Jacobson, K.A.3    Linden, J.4    Müller, C.E.5
  • 13
    • 0141811657 scopus 로고    scopus 로고
    • The role of a conserved region of the second intracellular loop in AT1 angiotensin receptor activation and signaling
    • Gaborik Z, Jagadeesh G, Zhang M, Spat A, Catt KJ, Hunyady L, (2003). The role of a conserved region of the second intracellular loop in AT1 angiotensin receptor activation and signaling. Endocrinol 144: 2220-2228.
    • (2003) Endocrinol , vol.144 , pp. 2220-2228
    • Gaborik, Z.1    Jagadeesh, G.2    Zhang, M.3    Spat, A.4    Catt, K.J.5    Hunyady, L.6
  • 14
    • 42749095676 scopus 로고    scopus 로고
    • Translocation of arrestin induced by human A3 adenosine receptor ligands in an engineered cell line: Comparison with G Protein-dependent pathways
    • Gao ZG, Jacobson KA, (2008). Translocation of arrestin induced by human A3 adenosine receptor ligands in an engineered cell line: comparison with G Protein-dependent pathways. Pharmacol Res 57: 303-311.
    • (2008) Pharmacol Res , vol.57 , pp. 303-311
    • Gao, Z.G.1    Jacobson, K.A.2
  • 15
    • 0037166356 scopus 로고    scopus 로고
    • Identification by site-directed mutagenesis of residues involved in ligand recognition and activation of the human A(3) adenosine receptor
    • Gao ZG, Chen A, Barak D, Kim SK, Muller CE, Jacobson KA, (2002). Identification by site-directed mutagenesis of residues involved in ligand recognition and activation of the human A(3) adenosine receptor. J Biol Chem 277: 19056-19063.
    • (2002) J Biol Chem , vol.277 , pp. 19056-19063
    • Gao, Z.G.1    Chen, A.2    Barak, D.3    Kim, S.K.4    Muller, C.E.5    Jacobson, K.A.6
  • 16
    • 33744957160 scopus 로고    scopus 로고
    • Distinct β-arrestin- and G protein-dependent pathways for parathyroid hormone receptor-stimulated eRK1/2 activation
    • Gesty-Palmer D, Chen M, Reiter E, Ahn S, Nelson CD, Wang S, et-al. (2006). Distinct β-arrestin- and G protein-dependent pathways for parathyroid hormone receptor-stimulated eRK1/2 activation. J Biol Chem 281: 10856-10864.
    • (2006) J Biol Chem , vol.281 , pp. 10856-10864
    • Gesty-Palmer, D.1    Chen, M.2    Reiter, E.3    Ahn, S.4    Nelson, C.D.5    Wang, S.6
  • 17
    • 0030859541 scopus 로고    scopus 로고
    • Agonists induce conformational changes in transmembrane domains III and VI of the beta(2) adrenoceptor
    • Gether U, Lin S, Ghanouni P, Ballesteros JA, Weinstein H, Kobilka BK, (1997). Agonists induce conformational changes in transmembrane domains III and VI of the beta(2) adrenoceptor. EMBO J 16: 6737-6747.
    • (1997) EMBO J , vol.16 , pp. 6737-6747
    • Gether, U.1    Lin, S.2    Ghanouni, P.3    Ballesteros, J.A.4    Weinstein, H.5    Kobilka, B.K.6
  • 18
    • 57649213524 scopus 로고    scopus 로고
    • Agonist-selective, receptor-specific interaction of human P2Y receptors with β-arrestin-1 and -2
    • Hoffmann C, Ziegler N, Reiner S, Krasel C, Lohse MJ, (2008). Agonist-selective, receptor-specific interaction of human P2Y receptors with β-arrestin-1 and -2. J Biol Chem 283: 30933-30941.
    • (2008) J Biol Chem , vol.283 , pp. 30933-30941
    • Hoffmann, C.1    Ziegler, N.2    Reiner, S.3    Krasel, C.4    Lohse, M.J.5
  • 19
    • 0242330291 scopus 로고    scopus 로고
    • High constitutive signaling of the ghrelin receptor - Identification of a potent inverse agonist
    • Holst B, Cygankiewicz A, Jensen TH, Ankersen M, Schwartz TW, (2003). High constitutive signaling of the ghrelin receptor-identification of a potent inverse agonist. Mol Endocrinol 17: 2201-2210.
    • (2003) Mol Endocrinol , vol.17 , pp. 2201-2210
    • Holst, B.1    Cygankiewicz, A.2    Jensen, T.H.3    Ankersen, M.4    Schwartz, T.W.5
  • 20
    • 77950505038 scopus 로고    scopus 로고
    • A conserved aromatic lock for the tryptophan rotameric switch in TM-VI of seven-transmembrane receptors
    • Holst B, Nygaard R, Valentin-Hansen L, Bach A, Engelstoft MS, Petersen PS, et-al. (2010). A conserved aromatic lock for the tryptophan rotameric switch in TM-VI of seven-transmembrane receptors. J Biol Chem 285: 3973-3985.
    • (2010) J Biol Chem , vol.285 , pp. 3973-3985
    • Holst, B.1    Nygaard, R.2    Valentin-Hansen, L.3    Bach, A.4    Engelstoft, M.S.5    Petersen, P.S.6
  • 22
    • 84872221774 scopus 로고    scopus 로고
    • Structure-function of the G protein-coupled receptor superfamily
    • Katritch V, Cherezov V, Stevens RC, (2013). Structure-function of the G protein-coupled receptor superfamily. Annu Rev Pharmacol Toxicol 53: 531-556.
    • (2013) Annu Rev Pharmacol Toxicol , vol.53 , pp. 531-556
    • Katritch, V.1    Cherezov, V.2    Stevens, R.C.3
  • 23
    • 84857497773 scopus 로고    scopus 로고
    • Biased signaling and allosteric machines: New vistas and challenges for drug discovery
    • Kenakin TP, (2012). Biased signaling and allosteric machines: new vistas and challenges for drug discovery. Br J Pharmacol 165: 1659-1669.
    • (2012) Br J Pharmacol , vol.165 , pp. 1659-1669
    • Kenakin, T.P.1
  • 24
    • 77952867655 scopus 로고    scopus 로고
    • Quantitative analysis of neuropeptide y receptor association with beta-arrestin2 measured by bimolecular fluorescence complementation
    • Kilpatrick LE, Briddon SJ, Hill SJ, Holliday ND, (2010). Quantitative analysis of neuropeptide Y receptor association with beta-arrestin2 measured by bimolecular fluorescence complementation. Br J Pharmacol 160: 892-906.
    • (2010) Br J Pharmacol , vol.160 , pp. 892-906
    • Kilpatrick, L.E.1    Briddon, S.J.2    Hill, S.J.3    Holliday, N.D.4
  • 25
    • 17644402459 scopus 로고    scopus 로고
    • Transduction of receptor signals by beta-arrestins
    • Lefkowitz RJ, Shenoy SK, (2005). Transduction of receptor signals by beta-arrestins. Science 308: 512-517.
    • (2005) Science , vol.308 , pp. 512-517
    • Lefkowitz, R.J.1    Shenoy, S.K.2
  • 26
    • 0035798651 scopus 로고    scopus 로고
    • Control of conformational equilibria in the human B2 bradykinin receptor: Modeling of nonpeptidic ligand action and comparison to the rhodopsin structure
    • Marie J, Richard E, Pruneau D, Paquet JL, Siatka C, Larguier R, et-al. (2001). Control of conformational equilibria in the human B2 bradykinin receptor: modeling of nonpeptidic ligand action and comparison to the rhodopsin structure. J Biol Chem 276: 41100-41111.
    • (2001) J Biol Chem , vol.276 , pp. 41100-41111
    • Marie, J.1    Richard, E.2    Pruneau, D.3    Paquet, J.L.4    Siatka, C.5    Larguier, R.6
  • 27
    • 34247525991 scopus 로고    scopus 로고
    • Detection of transient protein-protein interactions by bimolecular fluorescence complementation: The Abl-SH3 case
    • Morell M, Espargaro A, Aviles FX, Ventura S, (2007). Detection of transient protein-protein interactions by bimolecular fluorescence complementation: the Abl-SH3 case. Proteomics 7: 1023-1036.
    • (2007) Proteomics , vol.7 , pp. 1023-1036
    • Morell, M.1    Espargaro, A.2    Aviles, F.X.3    Ventura, S.4
  • 29
    • 65949105042 scopus 로고    scopus 로고
    • Persistent signaling induced by FTY720-phosphate is mediated by internalized S1P1 receptors
    • Mullershausen F, Zecri F, Cetin C, Billich A, Guerini D, Seuwen K, (2009). Persistent signaling induced by FTY720-phosphate is mediated by internalized S1P1 receptors. Nat Chem Biol 5: 428-434.
    • (2009) Nat Chem Biol , vol.5 , pp. 428-434
    • Mullershausen, F.1    Zecri, F.2    Cetin, C.3    Billich, A.4    Guerini, D.5    Seuwen, K.6
  • 31
    • 63849323943 scopus 로고    scopus 로고
    • Conformational toggle switches implicated in basal constitutive and agonist-induced activated states of 5-hydroxytryptamine-4 receptors
    • Pellissier LP, Sallander J, Campillo M, Gaven F, Queffeulou E, Pillot M, et-al. (2009). Conformational toggle switches implicated in basal constitutive and agonist-induced activated states of 5-hydroxytryptamine-4 receptors. Mol Pharmacol 75: 982-990.
    • (2009) Mol Pharmacol , vol.75 , pp. 982-990
    • Pellissier, L.P.1    Sallander, J.2    Campillo, M.3    Gaven, F.4    Queffeulou, E.5    Pillot, M.6
  • 32
  • 33
    • 0026660158 scopus 로고
    • Light stable rhodopsin. II. An opsin mutant (TRP-265-PHE) and a retinal analogue with a nonisomerizable II-cis configuration form a photostable chromophore
    • Ridge KD, Bhattacharya S, Nakayama TA, Khorana HG, (1992). Light stable rhodopsin. II. An opsin mutant (TRP-265-PHE) and a retinal analogue with a nonisomerizable II-cis configuration form a photostable chromophore. J Biol Chem 267: 6770-6775.
    • (1992) J Biol Chem , vol.267 , pp. 6770-6775
    • Ridge, K.D.1    Bhattacharya, S.2    Nakayama, T.A.3    Khorana, H.G.4
  • 34
    • 77249173336 scopus 로고    scopus 로고
    • Bimolecular fluorescence complementation: Lighting up seven transmembrane domain receptor signalling networks
    • Rose RH, Briddon SJ, Holliday ND, (2010). Bimolecular fluorescence complementation: lighting up seven transmembrane domain receptor signalling networks. Br J Pharmacol 159: 738-750.
    • (2010) Br J Pharmacol , vol.159 , pp. 738-750
    • Rose, R.H.1    Briddon, S.J.2    Holliday, N.D.3
  • 35
    • 0036841034 scopus 로고    scopus 로고
    • Signaling pathway from the human adenosine A(3) receptor expressed in Chinese hamster ovary cells to the extracellular signal-regulated kinase 1/2
    • Schulte G, Fredholm BB, (2002). Signaling pathway from the human adenosine A(3) receptor expressed in Chinese hamster ovary cells to the extracellular signal-regulated kinase 1/2. Mol Pharmacol 62: 1137-1146.
    • (2002) Mol Pharmacol , vol.62 , pp. 1137-1146
    • Schulte, G.1    Fredholm, B.B.2
  • 39
    • 84866724912 scopus 로고    scopus 로고
    • Fragment screening at adenosine-A(3) receptors in living cells using a fluorescence-based binding assay
    • Stoddart LA, Vernall AJ, Denman JL, Briddon SJ, Kellam B, Hill SJ, (2012). Fragment screening at adenosine-A(3) receptors in living cells using a fluorescence-based binding assay. Chem Biol 19: 1105-1115.
    • (2012) Chem Biol , vol.19 , pp. 1105-1115
    • Stoddart, L.A.1    Vernall, A.J.2    Denman, J.L.3    Briddon, S.J.4    Kellam, B.5    Hill, S.J.6
  • 40
    • 69249146075 scopus 로고    scopus 로고
    • Engineering G protein-coupled receptors to facilitate their structure determination
    • Tate CG, Schertler GFX, (2009). Engineering G protein-coupled receptors to facilitate their structure determination. Curr Opin Struct Biol 19: 386-395.
    • (2009) Curr Opin Struct Biol , vol.19 , pp. 386-395
    • Tate, C.G.1    Schertler, G.F.X.2
  • 41
    • 0036882256 scopus 로고    scopus 로고
    • A(3) adenosine receptors in human astrocytoma cells: Agonist-mediated desensitization, internalization, and down-regulation
    • Trincavelli ML, Tuscano D, Marroni M, Falleni A, Gremigni V, Ceruti S, et-al. (2002). A(3) adenosine receptors in human astrocytoma cells: agonist-mediated desensitization, internalization, and down-regulation. Mol Pharmacol 62: 1373-1384.
    • (2002) Mol Pharmacol , vol.62 , pp. 1373-1384
    • Trincavelli, M.L.1    Tuscano, D.2    Marroni, M.3    Falleni, A.4    Gremigni, V.5    Ceruti, S.6
  • 43
    • 84859949278 scopus 로고    scopus 로고
    • Differential signaling by splice variants of the human free fatty acid receptor GPR120
    • Watson S-J, Brown AJH, Holliday ND, (2012). Differential signaling by splice variants of the human free fatty acid receptor GPR120. Mol Pharmacol 81: 631-642.
    • (2012) Mol Pharmacol , vol.81 , pp. 631-642
    • Watson, S.-J.1    Brown, A.J.H.2    Holliday, N.D.3
  • 44
    • 0141703263 scopus 로고    scopus 로고
    • Independent beta-arrestin 2 and G protein-mediated pathways for angiotensin II activation of extracellular signal-regulated kinases 1 and 2
    • Wei HJ, Ahn S, Shenoy SK, Karnik SS, Hunyady L, Luttrell LM, et-al. (2003). Independent beta-arrestin 2 and G protein-mediated pathways for angiotensin II activation of extracellular signal-regulated kinases 1 and 2. Proc Natl Acad Sci 100: 10782-10787.
    • (2003) Proc Natl Acad Sci , vol.100 , pp. 10782-10787
    • Wei, H.J.1    Ahn, S.2    Shenoy, S.K.3    Karnik, S.S.4    Hunyady, L.5    Luttrell, L.M.6
  • 45
    • 84860914331 scopus 로고    scopus 로고
    • Persistent cAMP signaling by internalized TSH receptors occurs in thyroid but not in HEK293 cells
    • Werthmann RC, Volpe S, Lohse MJ, Calebiro D, (2012). Persistent cAMP signaling by internalized TSH receptors occurs in thyroid but not in HEK293 cells. FASEB J 26: 2043-2048.
    • (2012) FASEB J , vol.26 , pp. 2043-2048
    • Werthmann, R.C.1    Volpe, S.2    Lohse, M.J.3    Calebiro, D.4
  • 46
    • 0027533339 scopus 로고
    • Functional role of proline and tryptophan residues highly conserved amount G protein-coupled receptors studied by mutational analysis of the M3 muscarinic receptor
    • Wess J, Nanavati S, Vogel Z, Maggio R, (1993). Functional role of proline and tryptophan residues highly conserved amount G protein-coupled receptors studied by mutational analysis of the M3 muscarinic receptor. EMBO J 12: 331-338.
    • (1993) EMBO J , vol.12 , pp. 331-338
    • Wess, J.1    Nanavati, S.2    Vogel, Z.3    Maggio, R.4
  • 47
    • 79952488185 scopus 로고    scopus 로고
    • Therapeutic potential of beta-arrestin- and G protein-biased agonists
    • Whalen EJ, Rajagopal S, Lefkowitz RJ, (2011). Therapeutic potential of beta-arrestin- and G protein-biased agonists. Trends Mol Med 17: 126-139.
    • (2011) Trends Mol Med , vol.17 , pp. 126-139
    • Whalen, E.J.1    Rajagopal, S.2    Lefkowitz, R.J.3
  • 48
  • 49
    • 79954782236 scopus 로고    scopus 로고
    • Structure of an agonist-bound human A(2A) adenosine receptor
    • Xu F, Wu HX, Katritch V, Han GW, Jacobson KA, Gao ZG, et-al. (2011). Structure of an agonist-bound human A(2A) adenosine receptor. Science 332: 322-327.
    • (2011) Science , vol.332 , pp. 322-327
    • Xu, F.1    Wu, H.X.2    Katritch, V.3    Han, G.W.4    Jacobson, K.A.5    Gao, Z.G.6
  • 50
    • 33746382921 scopus 로고    scopus 로고
    • Coupling ligand structure to specific conformational switches in the beta(2)-adrenoceptor
    • Yao XJ, Parnot C, Deupi X, Ratnala VRP, Swaminath G, Farrens D, et-al. (2006). Coupling ligand structure to specific conformational switches in the beta(2)-adrenoceptor. Nat Chem Biol 2: 417-422.
    • (2006) Nat Chem Biol , vol.2 , pp. 417-422
    • Yao, X.J.1    Parnot, C.2    Deupi, X.3    Ratnala, V.R.P.4    Swaminath, G.5    Farrens, D.6


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