메뉴 건너뛰기




Volumn 105, Issue 29, 2008, Pages 9988-9993

Distinct conformational changes in β-arrestin report biased agonism at seven-transmembrane receptors

Author keywords

7TMRS; BRET; Phosphorylation

Indexed keywords

BETA ARRESTIN; BETA ARRESTIN 2; G PROTEIN COUPLED RECEPTOR; GUANINE NUCLEOTIDE BINDING PROTEIN; LIGAND; MEMBRANE RECEPTOR;

EID: 48249126790     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0804246105     Document Type: Article
Times cited : (209)

References (26)
  • 2
    • 17644402459 scopus 로고    scopus 로고
    • Transduction of receptor signals by β-arrestins
    • Lefkowitz RJ, Shenoy SK (2005) Transduction of receptor signals by β-arrestins. Science 308:512-517.
    • (2005) Science , vol.308 , pp. 512-517
    • Lefkowitz, R.J.1    Shenoy, S.K.2
  • 4
    • 0035083109 scopus 로고    scopus 로고
    • Inverse, protean, and ligand-selective agonism: Matters of receptor conformation
    • Kenakin T (2001) Inverse, protean, and ligand-selective agonism: Matters of receptor conformation. FASEB J 15:598-611.
    • (2001) FASEB J , vol.15 , pp. 598-611
    • Kenakin, T.1
  • 5
    • 0043235844 scopus 로고    scopus 로고
    • Ligand-selective receptor conformations revisited: The promise and the problem
    • Kenakin T (2003) Ligand-selective receptor conformations revisited: The promise and the problem. Trends Pharmacol Sci 24:346-354.
    • (2003) Trends Pharmacol Sci , vol.24 , pp. 346-354
    • Kenakin, T.1
  • 6
    • 34447649922 scopus 로고    scopus 로고
    • β-arrestin-biased ligands at seven-transmembrane receptors
    • Violin JD, Lefkowitz RJ (2007) β-arrestin-biased ligands at seven-transmembrane receptors. Trends Pharmacol Sci 28:416-422.
    • (2007) Trends Pharmacol Sci , vol.28 , pp. 416-422
    • Violin, J.D.1    Lefkowitz, R.J.2
  • 7
    • 20444499405 scopus 로고    scopus 로고
    • Probing the β2 adrenoceptor binding site with catechol reveals differences in binding and activation by agonists and partial agonists
    • Swaminath G, et al. (2005) Probing the β2 adrenoceptor binding site with catechol reveals differences in binding and activation by agonists and partial agonists. J Biol Chem 280:22165-22171.
    • (2005) J Biol Chem , vol.280 , pp. 22165-22171
    • Swaminath, G.1
  • 9
    • 17644391412 scopus 로고    scopus 로고
    • Monitoring agonist-promoted conformational changes of β-arrestin in living cells by intramolecular BRET
    • Charest PG, Terrillon S, Bouvier M (2005) Monitoring agonist-promoted conformational changes of β-arrestin in living cells by intramolecular BRET. EMBO Rep 6:334-340.
    • (2005) EMBO Rep , vol.6 , pp. 334-340
    • Charest, P.G.1    Terrillon, S.2    Bouvier, M.3
  • 10
    • 0036208442 scopus 로고    scopus 로고
    • Side-chain substitutions within angiotensin II reveal different requirements for signaling, internalization, and phosphorylation of type 1A angiotensin receptors
    • Holloway AC, et al. (2002) Side-chain substitutions within angiotensin II reveal different requirements for signaling, internalization, and phosphorylation of type 1A angiotensin receptors. Mol Pharmacol 61:768-777.
    • (2002) Mol Pharmacol , vol.61 , pp. 768-777
    • Holloway, A.C.1
  • 11
    • 0141703263 scopus 로고    scopus 로고
    • Independent β-arrestin 2 and G protein-mediated pathways for angiotensin II activation of extracellular signal-regulated kinases 1 and 2
    • Wei H, et al. (2003) Independent β-arrestin 2 and G protein-mediated pathways for angiotensin II activation of extracellular signal-regulated kinases 1 and 2. Proc Natl Acad Sci USA 100:10782-10787.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 10782-10787
    • Wei, H.1
  • 12
    • 0034595860 scopus 로고    scopus 로고
    • Differential affinities of visual arrestin, β arrestin 1, and β arrestin 2 for G protein-coupled receptors delineate two major classes of receptors
    • Oakley RH, et al. (2000) Differential affinities of visual arrestin, β arrestin 1, and β arrestin 2 for G protein-coupled receptors delineate two major classes of receptors. J Biol Chem 275:17201-17210.
    • (2000) J Biol Chem , vol.275 , pp. 17201-17210
    • Oakley, R.H.1
  • 14
    • 28844444442 scopus 로고    scopus 로고
    • Homo- and hetero-oligomerization of β-arrestins in living cells
    • Storez H, et al. (2005) Homo- and hetero-oligomerization of β-arrestins in living cells. J Biol Chem 280:40210-40215.
    • (2005) J Biol Chem , vol.280 , pp. 40210-40215
    • Storez, H.1
  • 15
    • 0141593597 scopus 로고    scopus 로고
    • β-arrestin-mediated activation of MAPK by inverse agonists reveals distinct active conformations for G protein-coupled receptors
    • Azzi M, et al. (2003) β-arrestin-mediated activation of MAPK by inverse agonists reveals distinct active conformations for G protein-coupled receptors. Proc Natl Acad Sci USA 100:11406-11411.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 11406-11411
    • Azzi, M.1
  • 16
    • 36749094552 scopus 로고    scopus 로고
    • A unique mechanism of β-blocker action: Carvedilol stimulates β-arrestin signaling
    • Wisler J, et al. (2007) A unique mechanism of β-blocker action: Carvedilol stimulates β-arrestin signaling. Proc Natl Acad Sci USA 104:16657-16662.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 16657-16662
    • Wisler, J.1
  • 17
    • 33644857279 scopus 로고    scopus 로고
    • β-arrestin-dependent, G protein-independent ERK1/2 activation by the β2 adrenergic receptor
    • Shenoy SK, et al. (2006) β-arrestin-dependent, G protein-independent ERK1/2 activation by the β2 adrenergic receptor. J Biol Chem 281:1261-1273.
    • (2006) J Biol Chem , vol.281 , pp. 1261-1273
    • Shenoy, S.K.1
  • 18
    • 41949089470 scopus 로고    scopus 로고
    • β-arrestin-biased agonism at the β2-adrenergic receptor
    • Drake M, et al. (2007) β-arrestin-biased agonism at the β2-adrenergic receptor. J Biol Chem 283:5669-5676.
    • (2007) J Biol Chem , vol.283 , pp. 5669-5676
    • Drake, M.1
  • 19
    • 33744957160 scopus 로고    scopus 로고
    • Distinct β-arrestin- and G protein-dependent pathways for parathyroid hormone receptor-stimulated ERK1/2 activation
    • Gesty-Palmer D, 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
  • 20
    • 48249085593 scopus 로고    scopus 로고
    • Arrestins: Ubiquitous regulators of cellular signaling pathways
    • Gurevich VV, Gurevich EV (2004) Arrestins: Ubiquitous regulators of cellular signaling pathways. Trends Pharmacol Sci 25:205-236.
    • (2004) Trends Pharmacol Sci , vol.25 , pp. 205-236
    • Gurevich, V.V.1    Gurevich, E.V.2
  • 21
    • 34547104638 scopus 로고    scopus 로고
    • The active conformation of β-arrestin 1: Direct evidence for the phosphate sensor in the N-domain and conformational differences in the active states of β-arrestins1 and -2
    • Nobles KN, et al. (2007) The active conformation of β-arrestin 1: Direct evidence for the phosphate sensor in the N-domain and conformational differences in the active states of β-arrestins1 and -2. J Biol Chem 282:21370-21381.
    • (2007) J Biol Chem , vol.282 , pp. 21370-21381
    • Nobles, K.N.1
  • 22
    • 11244311659 scopus 로고    scopus 로고
    • Activation-dependent conformational changes in β-arrestin 2
    • Xiao K, Shenoy SK, Nobles K, Lefkowitz RJ (2004) Activation-dependent conformational changes in β-arrestin 2. J Biol Chem 279:55744-55753.
    • (2004) J Biol Chem , vol.279 , pp. 55744-55753
    • Xiao, K.1    Shenoy, S.K.2    Nobles, K.3    Lefkowitz, R.J.4
  • 23
    • 0034723193 scopus 로고    scopus 로고
    • Agonist-induced phosphorylation of the angiotensin II (AT(1A)) receptor requires generation of a conformation that is distinct from the inositol phosphate-signaling state
    • Thomas WG, Qian H, Chang CS, Karnik S (2004) Agonist-induced phosphorylation of the angiotensin II (AT(1A)) receptor requires generation of a conformation that is distinct from the inositol phosphate-signaling state. J Biol Chem 275:2893-2900.
    • (2004) J Biol Chem , vol.275 , pp. 2893-2900
    • Thomas, W.G.1    Qian, H.2    Chang, C.S.3    Karnik, S.4
  • 24
    • 0026756371 scopus 로고
    • Sites in the third intracellular loop of the alpha 2A-adrenergic receptor confer short term agonist-promoted desensitization. Evidence for a receptor kinase-mediated mechanism
    • Liggett SB, et al. (1992) Sites in the third intracellular loop of the alpha 2A-adrenergic receptor confer short term agonist-promoted desensitization. Evidence for a receptor kinase-mediated mechanism. J Biol Chem 267:4740-4746.
    • (1992) J Biol Chem , vol.267 , pp. 4740-4746
    • Liggett, S.B.1
  • 25
    • 33746012381 scopus 로고    scopus 로고
    • G-protein-coupled receptor kinase specificity for β-arrestin recruitment to the β2-adrenergic receptor revealed by fluorescence resonance energy transfer
    • Violin JD, Ren XR, Lefkowitz RJ (2006) G-protein-coupled receptor kinase specificity for β-arrestin recruitment to the β2-adrenergic receptor revealed by fluorescence resonance energy transfer. J Biol Chem 281:20577-20588.
    • (2006) J Biol Chem , vol.281 , pp. 20577-20588
    • Violin, J.D.1    Ren, X.R.2    Lefkowitz, R.J.3
  • 26
    • 33646162635 scopus 로고    scopus 로고
    • GRKs and β-arrestins: Roles in receptor silencing, trafficking and signaling
    • Reiter E, Lefkowitz RJ (2006) GRKs and β-arrestins: Roles in receptor silencing, trafficking and signaling. Trends Endocrinol Metab 17:159-165.
    • (2006) Trends Endocrinol Metab , vol.17 , pp. 159-165
    • Reiter, E.1    Lefkowitz, R.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.