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Volumn 9, Issue 4, 2004, Pages 322-333

Development of a BRET2 screening assay using β-arrestin 2 mutants

Author keywords

Arrestin 2; BRET2; GPCRs; Screening

Indexed keywords

2 BENZHYDRYL 3 (2 METHOXYBENZYLAMINO) 1 AZABICYCLO[2.2.2]OCTANE; ADRENERGIC RECEPTOR BLOCKING AGENT; BETA 2 ADRENERGIC RECEPTOR; BETA 2 ADRENERGIC RECEPTOR STIMULATING AGENT; BETA ARRESTIN; CLATHRIN; G PROTEIN COUPLED RECEPTOR; ISOPRENALINE; MUTANT PROTEIN; NEUROKININ 1 RECEPTOR; NEUROKININ 1 RECEPTOR AGONIST; NEUROPEPTIDE Y2 RECEPTOR; PINDOLOL; SUBSTANCE P; TACHYKININ RECEPTOR AGONIST; TACHYKININ RECEPTOR ANTAGONIST; HYBRID PROTEIN; RETINA S ANTIGEN;

EID: 2542437470     PISSN: 10870571     EISSN: None     Source Type: Journal    
DOI: 10.1177/1087057104263212     Document Type: Article
Times cited : (80)

References (44)
  • 1
    • 0037082324 scopus 로고    scopus 로고
    • Target validation of G-protein coupled receptors
    • Wise A, Gearing K, Rees S: Target validation of G-protein coupled receptors. Drug Discov Today 2002;7:235-246.
    • (2002) Drug Discov Today , vol.7 , pp. 235-246
    • Wise, A.1    Gearing, K.2    Rees, S.3
  • 2
    • 0037394124 scopus 로고    scopus 로고
    • Designing screens: How to make your hits a hit
    • Walters WP, Namchuk M: Designing screens: how to make your hits a hit. Nat Rev Drug Discov 2003;2:259-266.
    • (2003) Nat Rev Drug Discov , vol.2 , pp. 259-266
    • Walters, W.P.1    Namchuk, M.2
  • 3
    • 0036209874 scopus 로고    scopus 로고
    • Endocytosis of G protein-coupled receptors: Roles of G protein-coupled receptor kinases and β-arrestin proteins
    • Claing A, Laporte SA, Caron MG, Lefkowitz RJ, Perry SJ: Endocytosis of G protein-coupled receptors: roles of G protein-coupled receptor kinases and β-arrestin proteins. Prog Neurobiol 2002;66:61-79.
    • (2002) Prog Neurobiol , vol.66 , pp. 61-79
    • Claing, A.1    Laporte, S.A.2    Caron, M.G.3    Lefkowitz, R.J.4    Perry, S.J.5
  • 4
    • 0036499130 scopus 로고    scopus 로고
    • Arresting developments in heptahelical receptor signaling and regulation
    • Perry SJ, Lefkowitz RJ: Arresting developments in heptahelical receptor signaling and regulation. Trends Cell Biol 2002;12:130-138.
    • (2002) Trends Cell Biol , vol.12 , pp. 130-138
    • Perry, S.J.1    Lefkowitz, R.J.2
  • 5
    • 0034595860 scopus 로고    scopus 로고
    • Differential affinities of visual arrestin, β arrestin1, and β arrestin2 for G protein-coupled receptors delineate two major classes of receptors
    • Oakley RH, Laporte SA, Holt JA, Caron MG, Barak LS: Differential affinities of visual arrestin, β arrestin1, and β arrestin2 for G protein-coupled receptors delineate two major classes of receptors. J Biol Chem 2000;275:17201-17210.
    • (2000) J Biol Chem , vol.275 , pp. 17201-17210
    • Oakley, R.H.1    Laporte, S.A.2    Holt, J.A.3    Caron, M.G.4    Barak, L.S.5
  • 6
    • 0035374624 scopus 로고    scopus 로고
    • Molecular determinants underlying the formation of stable intracellular G protein-coupled receptor-β-arrestin complexes after receptor endocytosis
    • Oakley RH, Laporte SA, Holt JA, Barak LS, Caron MG, Zhang J, et al: Molecular determinants underlying the formation of stable intracellular G protein-coupled receptor-β-arrestin complexes after receptor endocytosis. J Biol Chem 2001;276:19452-19460.
    • (2001) J Biol Chem , vol.276 , pp. 19452-19460
    • Oakley, R.H.1    Laporte, S.A.2    Holt, J.A.3    Barak, L.S.4    Caron, M.G.5    Zhang, J.6
  • 7
    • 0030967614 scopus 로고    scopus 로고
    • Arrestin/clathrin interaction: Localization of the clathrin binding domain of nonvisual arrestins to the carboxy terminus
    • Krupnick JG, Goodman OB Jr, Keen JH, Benovic JL: Arrestin/clathrin interaction: localization of the clathrin binding domain of nonvisual arrestins to the carboxy terminus. J Biol Chem 1997;272:15011-15016.
    • (1997) J Biol Chem , vol.272 , pp. 15011-15016
    • Krupnick, J.G.1    Goodman Jr., O.B.2    Keen, J.H.3    Benovic, J.L.4
  • 8
    • 12644259509 scopus 로고    scopus 로고
    • Arrestin/clathrin interaction: Localization of the arrestin binding locus to the clathrin terminal domain
    • Goodman OB Jr, Krupnick JG, Gurevich VV, Benovic JL, Keen JH: Arrestin/ clathrin interaction: localization of the arrestin binding locus to the clathrin terminal domain. J Biol Chem 1997;272:15017-15022.
    • (1997) J Biol Chem , vol.272 , pp. 15017-15022
    • Goodman Jr., O.B.1    Krupnick, J.G.2    Gurevich, V.V.3    Benovic, J.L.4    Keen, J.H.5
  • 12
    • 0034083428 scopus 로고    scopus 로고
    • Recent advances in technology for measuring and manipulating cell signals
    • Zacharias DA, Baird GS, Tsien RY: Recent advances in technology for measuring and manipulating cell signals. Curr Opin Neurobiol 2000;10:416-421.
    • (2000) Curr Opin Neurobiol , vol.10 , pp. 416-421
    • Zacharias, D.A.1    Baird, G.S.2    Tsien, R.Y.3
  • 13
    • 0033524455 scopus 로고    scopus 로고
    • A bioluminescence resonance energy transfer (BRET) system: Application to interacting circadian clock proteins
    • Xu Y, Piston DW, Johnson CH: A bioluminescence resonance energy transfer (BRET) system: application to interacting circadian clock proteins. Proc Natl Acad Sci USA 1999;96:151-156.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 151-156
    • Xu, Y.1    Piston, D.W.2    Johnson, C.H.3
  • 15
    • 0034801960 scopus 로고    scopus 로고
    • Monitoring the activation state of the insulin receptor using bioluminescence resonance energy transfer
    • Boute N, Pernet K, Issad T: Monitoring the activation state of the insulin receptor using bioluminescence resonance energy transfer. Mol Pharmacol 2001;60:640-645.
    • (2001) Mol Pharmacol , vol.60 , pp. 640-645
    • Boute, N.1    Pernet, K.2    Issad, T.3
  • 16
    • 0036174608 scopus 로고    scopus 로고
    • Dimerization: An emerging concept for G protein-coupled receptor ontogeny and function
    • Angers S, Salahpour A, Bouvier M: Dimerization: an emerging concept for G protein-coupled receptor ontogeny and function. Annu Rev Pharmacol Toxicol 2002;42:409-435.
    • (2002) Annu Rev Pharmacol Toxicol , vol.42 , pp. 409-435
    • Angers, S.1    Salahpour, A.2    Bouvier, M.3
  • 17
    • 0036973242 scopus 로고    scopus 로고
    • 2/arrestin assay in stable recombinant cells: A platform to screen for compounds that interact with G protein-coupled receptors (GPCRs)
    • 2/arrestin assay in stable recombinant cells: a platform to screen for compounds that interact with G protein-coupled receptors (GPCRs). J Recept Signal Transduct Res 2002;22:533-541.
    • (2002) J Recept Signal Transduct Res , vol.22 , pp. 533-541
    • Bertrand, L.1    Parent, S.2    Caron, M.3    Legault, M.4    Joly, E.5    Angers, S.6
  • 18
    • 0038170289 scopus 로고    scopus 로고
    • Applications of novel resonance energy transfer techniques to study dynamic hormone receptor interactions in living cells
    • Eidne KA, Kroeger KM. Hanyaloglu AC: Applications of novel resonance energy transfer techniques to study dynamic hormone receptor interactions in living cells. Trends Endocrinol Metab 2002;13:415-421.
    • (2002) Trends Endocrinol Metab , vol.13 , pp. 415-421
    • Eidne, K.A.1    Kroeger, K.M.2    Hanyaloglu, A.C.3
  • 19
    • 0036696695 scopus 로고    scopus 로고
    • The use of resonance energy transfer in high-throughput screening: BRET versus FRET
    • Boute N, Jockers R, Issad T: The use of resonance energy transfer in high-throughput screening: BRET versus FRET. Trends Pharmacol Sci 2002;23:351-354.
    • (2002) Trends Pharmacol Sci , vol.23 , pp. 351-354
    • Boute, N.1    Jockers, R.2    Issad, T.3
  • 20
    • 12244268639 scopus 로고    scopus 로고
    • Bioluminescence resonance energy transfer: Monitoring protein-protein interactions in living cells
    • Xu Y, Kanauchi A, von Arnim AG, Piston DW, Johnson CH: Bioluminescence resonance energy transfer: monitoring protein-protein interactions in living cells. Methods Enzymol 2003;360:289-301.
    • (2003) Methods Enzymol , vol.360 , pp. 289-301
    • Xu, Y.1    Kanauchi, A.2    Von Arnim, A.G.3    Piston, D.W.4    Johnson, C.H.5
  • 21
    • 0037101774 scopus 로고    scopus 로고
    • Homo- and heterooligomeric interactions between G-protein-coupled receptors in living cells monitored by two variants of bioluminescence resonance energy transfer (BRET): Hetero-oligomers between receptor subtypes form more efficiently than between less closely related sequences
    • Ramsay D, Kellett E, McVey M, Rees S, Milligan G: Homo- and heterooligomeric interactions between G-protein-coupled receptors in living cells monitored by two variants of bioluminescence resonance energy transfer (BRET): hetero-oligomers between receptor subtypes form more efficiently than between less closely related sequences. Biochem J 2002;365:429-440.
    • (2002) Biochem J , vol.365 , pp. 429-440
    • Ramsay, D.1    Kellett, E.2    McVey, M.3    Rees, S.4    Milligan, G.5
  • 23
    • 0031757743 scopus 로고    scopus 로고
    • Agonist-induced endocytosis and recycling of the gonadotropin-releasing hormone receptor: Effect of β-arrestin on internalization kinetics
    • Vrecl M, Anderson L, Hanyaloglu A, McGregor AM, Groarke AD, Milligan G. et al: Agonist-induced endocytosis and recycling of the gonadotropin-releasing hormone receptor: effect of β-arrestin on internalization kinetics. Mol Endocrinol 1998;12:1818-1829.
    • (1998) Mol Endocrinol , vol.12 , pp. 1818-1829
    • Vrecl, M.1    Anderson, L.2    Hanyaloglu, A.3    McGregor, A.M.4    Groarke, A.D.5    Milligan, G.6
  • 25
    • 0031914895 scopus 로고    scopus 로고
    • Steric hindrance mutagenesis versus alanine scan in mapping of ligand binding sites in the tachykinin NK1 receptor
    • Holst B, Zoffmann S, Elling CE, Hjorth SA, Schwartz TW: Steric hindrance mutagenesis versus alanine scan in mapping of ligand binding sites in the tachykinin NK1 receptor. Mol Pharmacol 1998;53:166-175.
    • (1998) Mol Pharmacol , vol.53 , pp. 166-175
    • Holst, B.1    Zoffmann, S.2    Elling, C.E.3    Hjorth, S.A.4    Schwartz, T.W.5
  • 27
    • 0012132962 scopus 로고    scopus 로고
    • The cellular distribution of fluorescently labeled arrestins provides a robust, sensitive, and universal assay for screening G protein-coupled receptors
    • Oakley RH, Hudson CC, Cruickshank RD, Meyers DM, Payne RE, Rhem SM, et al: The cellular distribution of fluorescently labeled arrestins provides a robust, sensitive, and universal assay for screening G protein-coupled receptors. Assay Drug Dev Techn 2002;1:21-30.
    • (2002) Assay Drug Dev Techn , vol.1 , pp. 21-30
    • Oakley, R.H.1    Hudson, C.C.2    Cruickshank, R.D.3    Meyers, D.M.4    Payne, R.E.5    Rhem, S.M.6
  • 28
    • 0037088679 scopus 로고    scopus 로고
    • Conservation of the phosphate-sensitive elements in the arrestin family of proteins
    • Celver J, Vishnivetskiy SA, Chavkin C, Gurevich VV: Conservation of the phosphate-sensitive elements in the arrestin family of proteins. J Biol Chem 2002;277:9043-9048.
    • (2002) J Biol Chem , vol.277 , pp. 9043-9048
    • Celver, J.1    Vishnivetskiy, S.A.2    Chavkin, C.3    Gurevich, V.V.4
  • 29
    • 0037163045 scopus 로고    scopus 로고
    • Differential roles of arrestin-2 interaction with clathrin and adaptor protein 2 in G protein-coupled receptor trafficking
    • Kim YM, Benovic JL: Differential roles of arrestin-2 interaction with clathrin and adaptor protein 2 in G protein-coupled receptor trafficking. J Biol Chem 2002;277:30760-30768.
    • (2002) J Biol Chem , vol.277 , pp. 30760-30768
    • Kim, Y.M.1    Benovic, J.L.2
  • 30
    • 0037066145 scopus 로고    scopus 로고
    • Scaffolding functions of arrestin-2 revealed by crystal structure and mutagenesis
    • Milano SK, Pace HC, Kim YM, Brenner C, Benovic JL: Scaffolding functions of arrestin-2 revealed by crystal structure and mutagenesis. Biochemistry 2002;41:3321-3328.
    • (2002) Biochemistry , vol.41 , pp. 3321-3328
    • Milano, S.K.1    Pace, H.C.2    Kim, Y.M.3    Brenner, C.4    Benovic, J.L.5
  • 31
    • 0034802172 scopus 로고    scopus 로고
    • Crystal structure of β-arrestin at 1.9 Å: Possible mechanism of receptor binding and membrane translocation
    • Han M, Gurevich VV, Vishnivetskiy SA, Sigler PB, Schubert C: Crystal structure of β-arrestin at 1.9 Å: possible mechanism of receptor binding and membrane translocation. Structure 2001;9:869-880.
    • (2001) Structure , vol.9 , pp. 869-880
    • Han, M.1    Gurevich, V.V.2    Vishnivetskiy, S.A.3    Sigler, P.B.4    Schubert, C.5
  • 32
    • 10544233013 scopus 로고    scopus 로고
    • Desensitization of the neurokinin 1 receptor is mediated by the receptor carboxy-terminal region, but is not caused by receptor internalization
    • Sanders MA, LeVine H III: Desensitization of the neurokinin 1 receptor is mediated by the receptor carboxy-terminal region, but is not caused by receptor internalization. J Neurochem 1996;67:2362-2372.
    • (1996) J Neurochem , vol.67 , pp. 2362-2372
    • Sanders, M.A.1    LeVine III, H.2
  • 33
    • 0037022687 scopus 로고    scopus 로고
    • Heterologous regulation of trafficking and signaling of G protein-coupled receptors: β-arrestin-dependent interactions between neurokinin receptors
    • Schmidlin F, Dery O, Bunnett NW, Grady EF: Heterologous regulation of trafficking and signaling of G protein-coupled receptors: β-arrestin- dependent interactions between neurokinin receptors. Proc Natl Acad Sci USA 2002; 99:3324-3329.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 3324-3329
    • Schmidlin, F.1    Dery, O.2    Bunnett, N.W.3    Grady, E.F.4
  • 34
    • 0037200067 scopus 로고    scopus 로고
    • Identification of a novel human eicosanoid receptor coupled to G(i/o)
    • Hosoi T, Koguchi Y, Sugikawa E, Chikada A, Ogawa K, Tsuda N. et al: Identification of a novel human eicosanoid receptor coupled to G(i/o). J Biol Chem 2002;277:31459-31465.
    • (2002) J Biol Chem , vol.277 , pp. 31459-31465
    • Hosoi, T.1    Koguchi, Y.2    Sugikawa, E.3    Chikada, A.4    Ogawa, K.5    Tsuda, N.6
  • 35
    • 0030609874 scopus 로고    scopus 로고
    • 2-adrenergic receptor sequestration: Intracellular complement of β-adrenergic receptor kinase and β-arrestin determine kinetics of internalization
    • 2-adrenergic receptor sequestration: intracellular complement of β-adrenergic receptor kinase and β-arrestin determine kinetics of internalization. Mol Pharmacol 1997;51:800-808.
    • (1997) Mol Pharmacol , vol.51 , pp. 800-808
    • Menard, L.1    Ferguson, S.S.2    Zhang, J.3    Lin, F.T.4    Lefkowitz, R.J.5    Caron, M.G.6
  • 36
    • 0037107007 scopus 로고    scopus 로고
    • Novel detection strategies for drug discovery
    • Hemmila IA, Hurskainen P: Novel detection strategies for drug discovery. Drug Discov Today 2002;7:5150-5156.
    • (2002) Drug Discov Today , vol.7 , pp. 5150-5156
    • Hemmila, I.A.1    Hurskainen, P.2
  • 37
    • 0033527663 scopus 로고    scopus 로고
    • Association of β-arrestin with G protein-coupled receptors during clathrin-mediated endocytosis dictates the profile of receptor resensitization
    • Oakley RH, Laporte SA, Holt JA, Barak LS, Caron MG: Association of β-arrestin with G protein-coupled receptors during clathrin-mediated endocytosis dictates the profile of receptor resensitization. J Biol Chem 1999;274:32248-32257.
    • (1999) J Biol Chem , vol.274 , pp. 32248-32257
    • Oakley, R.H.1    Laporte, S.A.2    Holt, J.A.3    Barak, L.S.4    Caron, M.G.5
  • 38
    • 0033548433 scopus 로고    scopus 로고
    • Targeted construction of phosphorylation-independent β-arrestin mutants with constitutive activity in cells
    • Kovoor A, Celver J, Abdryashitov RI, Chavkin C, Gurevich VV: Targeted construction of phosphorylation-independent β-arrestin mutants with constitutive activity in cells. J Biol Chem 1999;274:6831-6834.
    • (1999) J Biol Chem , vol.274 , pp. 6831-6834
    • Kovoor, A.1    Celver, J.2    Abdryashitov, R.I.3    Chavkin, C.4    Gurevich, V.V.5
  • 39
    • 0031015458 scopus 로고    scopus 로고
    • Mechanism of phosphorylation-recognition by visual arrestin and the transition of arrestin into a high affinity binding state
    • Gurevich VV, Benovic JL: Mechanism of phosphorylation-recognition by visual arrestin and the transition of arrestin into a high affinity binding state. Mol Pharmacol 1997;51:161-169.
    • (1997) Mol Pharmacol , vol.51 , pp. 161-169
    • Gurevich, V.V.1    Benovic, J.L.2
  • 41
    • 0039702902 scopus 로고    scopus 로고
    • Substance P-induced trafficking of β-arrestins: The role of β-arrestins in endocytosis of the neurokinin-1 receptor
    • McConalogue K, Dery O, Lovett M, Wong H, Walsh JH, Grady EF, et al: Substance P-induced trafficking of β-arrestins: the role of β-arrestins in endocytosis of the neurokinin-1 receptor. J Biol Chem 1999;274:16257-16268.
    • (1999) J Biol Chem , vol.274 , pp. 16257-16268
    • McConalogue, K.1    Dery, O.2    Lovett, M.3    Wong, H.4    Walsh, J.H.5    Grady, E.F.6
  • 42
    • 0037838870 scopus 로고    scopus 로고
    • The nature of the arrestin-receptor complex determines the ultimate fate of the internalized receptor
    • Pan L, Gurevich EV, Gurevich VV: The nature of the arrestin-receptor complex determines the ultimate fate of the internalized receptor. J Biol Chem 2003;278:11623-11632.
    • (2003) J Biol Chem , vol.278 , pp. 11623-11632
    • Pan, L.1    Gurevich, E.V.2    Gurevich, V.V.3
  • 44
    • 0035918215 scopus 로고    scopus 로고
    • Constitutive and agonist-dependent homo-oligomerization of the thyrotropin-releasing hormone receptor: Detection in living cells using bioluminescence resonance energy transfer
    • Kroeger KM, Hanyaloglu AC, Seeber RM, Miles LE, Eidne KA: Constitutive and agonist-dependent homo-oligomerization of the thyrotropin-releasing hormone receptor: detection in living cells using bioluminescence resonance energy transfer. J Biol Chem 2001;276:12736-12743.
    • (2001) J Biol Chem , vol.276 , pp. 12736-12743
    • Kroeger, K.M.1    Hanyaloglu, A.C.2    Seeber, R.M.3    Miles, L.E.4    Eidne, K.A.5


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