메뉴 건너뛰기




Volumn 88, Issue 3-4, 2011, Pages 174-181

Beta-arrestin2 as a competitor for GRK2 interaction with the GLP-1 receptor upon receptor activation

Author keywords

arrestin; Bioluminescence resonance energy transfer; G protein coupled receptor kinase; G protein coupled receptors; Glucagon like peptide 1

Indexed keywords

BETA ARRESTIN 2; G PROTEIN COUPLED RECEPTOR KINASE 2; GLUCAGON LIKE PEPTIDE 1; GLUCAGON LIKE PEPTIDE 1 RECEPTOR;

EID: 80155136181     PISSN: 00317012     EISSN: 14230313     Source Type: Journal    
DOI: 10.1159/000330742     Document Type: Article
Times cited : (16)

References (30)
  • 1
    • 0344780741 scopus 로고    scopus 로고
    • G-protein coupled receptor kinases as modulators of G-protein signalling
    • DOI 10.1111/j.1469-7793.1999.0005z.x
    • Bunemann M, Hosey MM: G-protein coupled receptor kinases as modulators of Gprotein signalling. J Physiol 1999; 517: 5-23. (Pubitemid 29243467)
    • (1999) Journal of Physiology , vol.517 , Issue.1 , pp. 5-23
    • Bunemann, M.1    Hosey, M.M.2
  • 2
    • 0025352299 scopus 로고
    • Beta-Arrestin: A protein that regulates beta-adrenergic receptor function
    • Lohse MJ, Benovic JL, Codina J, Caron MG, Lefkowitz RJ: beta-Arrestin: a protein that regulates beta-adrenergic receptor function. Science 1990; 248: 1547-1550.
    • (1990) Science , vol.248 , pp. 1547-1550
    • Lohse, M.J.1    Benovic, J.L.2    Codina, J.3    Caron, M.G.4    Lefkowitz, R.J.5
  • 3
    • 17644402459 scopus 로고    scopus 로고
    • Transduction of receptor signals by beta-arrestins
    • Lefkowitz RJ, Shenoy SK: Transduction of receptor signals by beta-arrestins. Science 2005; 308: 512-517.
    • (2005) Science , vol.308 , pp. 512-517
    • Lefkowitz, R.J.1    Shenoy, S.K.2
  • 6
    • 18744376919 scopus 로고    scopus 로고
    • Real-time monitoring of receptor and G-protein interactions in living cells
    • DOI 10.1038/nmeth743
    • Gales C, Rebois RV, Hogue M, Trieu P, Breit A, Hebert TE, Bouvier M: Real-time monitoring of receptor and G-protein interactions in living cells. Nat Methods 2005; 2: 177-184. (Pubitemid 41122124)
    • (2005) Nature Methods , vol.2 , Issue.3 , pp. 177-184
    • Gales, C.1    Rebois, R.V.2    Hogue, M.3    Trieu, P.4    Breit, A.5    Hebert, T.E.6    Bouvier, M.7
  • 10
    • 35748957503 scopus 로고    scopus 로고
    • The physiology of glucagon-like peptide 1
    • DOI 10.1152/physrev.00034.2006
    • Holst JJ: The physiology of glucagon-like peptide 1. Physiol Rev 2007; 87: 1409-1439. (Pubitemid 350041474)
    • (2007) Physiological Reviews , vol.87 , Issue.4 , pp. 1409-1439
    • Holst, J.J.1
  • 11
    • 0029957956 scopus 로고    scopus 로고
    • Connectivity and orientation of the seven helical bundle in the tachykinin NK-1 receptor probed by zinc site engineering
    • Elling CE, Schwartz TW: Connectivity and orientation of the seven helical bundle in the tachykinin NK-1 receptor probed by zinc site engineering. EMBO J 1996; 15: 6213-6219. (Pubitemid 26397894)
    • (1996) EMBO Journal , vol.15 , Issue.22 , pp. 6213-6219
    • Elling, C.E.1    Schwartz, T.W.2
  • 13
    • 2542437470 scopus 로고    scopus 로고
    • Development of a BRET2 screening assay using beta-arrestin 2 mutants
    • Vrecl M, Jorgensen R, Pogacnik A, Heding A: Development of a BRET2 screening assay using beta-arrestin 2 mutants. J Biomol Screen 2004; 9: 322-333.
    • (2004) J Biomol Screen , vol.9 , pp. 322-333
    • Vrecl, M.1    Jorgensen, R.2    Pogacnik, A.3    Heding, A.4
  • 14
    • 14844321939 scopus 로고    scopus 로고
    • Characterization of glucagon-like peptide-1 receptor β-arrestin 2 interaction: A high-affinity receptor phenotype
    • DOI 10.1210/me.2004-0312
    • Jorgensen R, Martini L, Schwartz TW, Elling CE: Characterization of glucagon-like peptide-1. receptor beta-arrestin 2 interaction: a high-affinity receptor phenotype. Mol Endocrinol 2005; 19: 812-823. (Pubitemid 40349451)
    • (2005) Molecular Endocrinology , vol.19 , Issue.3 , pp. 812-823
    • Jorgensen, R.1    Martini, L.2    Schwartz, T.W.3    Elling, C.E.4
  • 15
    • 38549084354 scopus 로고    scopus 로고
    • Characterization of G-protein coupled receptor kinase interaction with the neurokinin-1 receptor using bioluminescence resonance energy transfer
    • DOI 10.1124/mol.107.038877
    • Jorgensen R, Holliday ND, Hansen JL, Vrecl M, Heding A, Schwartz TW, Elling CE: Characterization of g-protein coupled receptor kinase interaction with the neurokinin-1 receptor using bioluminescence resonance energy transfer. Mol Pharmacol 2008; 73: 349-358. (Pubitemid 351159205)
    • (2008) Molecular Pharmacology , vol.73 , Issue.2 , pp. 349-358
    • Jorgensen, R.1    Holliday, N.D.2    Hansen, J.L.3    Vrecl, M.4    Heding, A.5    Schwartz, T.W.6    Elling, C.E.7
  • 16
    • 33746012381 scopus 로고    scopus 로고
    • 2-adrenergic receptor revealed by fluorescence resonance energy transfer
    • DOI 10.1074/jbc.M513605200
    • Violin JD, Ren XR, Lefkowitz RJ: G-proteincoupled receptor kinase specificity for betaarrestin recruitment to the beta2-adrenergic receptor revealed by fluorescence resonance energy transfer. J Biol Chem 2006; 281: 20577-20588. (Pubitemid 44065829)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.29 , pp. 20577-20588
    • Violin, J.D.1    Ren, X.-R.2    Lefkowitz, R.J.3
  • 17
    • 34250159099 scopus 로고    scopus 로고
    • Assembly and signaling of CRLR and RAMP1 complexes assessed by BRET
    • DOI 10.1021/bi0622470
    • Heroux M, Breton B, Hogue M, Bouvier M: Assembly and signaling of CRLR and RAMP1 complexes assessed by BRET. Biochemistry 2007; 46: 7022-7033. (Pubitemid 46906431)
    • (2007) Biochemistry , vol.46 , Issue.23 , pp. 7022-7033
    • Heroux, M.1    Breton, B.2    Hogue, M.3    Bouvier, M.4
  • 18
    • 0037160105 scopus 로고    scopus 로고
    • 2- adrenergic receptor homo- and heterodimerization by bioluminescence resonance energy transfer
    • DOI 10.1074/jbc.M205767200
    • Mercier JF, Salahpour A, Angers S, Breit A, Bouvier M: Quantitative assessment of beta 1-and beta 2-adrenergic receptor homo-and heterodimerization by bioluminescence resonance energy transfer. J Biol Chem 2002; 277: 44925-44931. (Pubitemid 36159089)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.47 , pp. 44925-44931
    • Mercier, J.-F.1    Salahpour, A.2    Angers, S.3    Breit, A.4    Bouvier, M.5
  • 19
    • 0031435817 scopus 로고    scopus 로고
    • Modulation of the arrestin-clathrin interaction in cells: Characterization of β-arrestin dominant-negative mutants
    • DOI 10.1074/jbc.272.51.32507
    • Krupnick JG, Santini F, Gagnon AW, Keen JH, Benovic JL: Modulation of the arrestinclathrin interaction in cells: characterization of beta-arrestin dominant-negative mutants. J Biol Chem 1997; 272: 32507-32512. (Pubitemid 28011936)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.51 , pp. 32507-32512
    • Krupnick, J.G.1    Santini, F.2    Gagnon, A.W.3    Keen, J.H.4    Benovic, J.L.5
  • 20
    • 0035374624 scopus 로고    scopus 로고
    • Molecular determinants underlying the formation of stable intracellular G protein-coupled receptor-beta-arrestin complexes after receptor endocytosis *
    • Oakley RH, Laporte SA, Holt JA, Barak LS, Caron MG: Molecular determinants underlying the formation of stable intracellular G protein-coupled receptor-beta-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
  • 21
    • 0031001096 scopus 로고    scopus 로고
    • Internalization and homologous desensitization of the GLP-1 receptor depend on phosphorylation of the receptor carboxyl tail at the same three sites
    • DOI 10.1210/me.11.8.1094
    • Widmann C, Dolci W, Thorens B: Internalization and homologous desensitization of the GLP-1 receptor depend on phosphorylation of the receptor carboxyl tail at the same three sites. Mol Endocrinol 1997; 11: 1094-1102. (Pubitemid 27278832)
    • (1997) Molecular Endocrinology , vol.11 , Issue.8 , pp. 1094-1102
    • Widmann, C.1    Dolci, W.2    Thorens, B.3
  • 22
    • 0026640659 scopus 로고
    • Receptor-specific desensitization with purified proteins: Kinase dependence and receptor specificity of beta-arrestin and arrestin in the beta 2-adrenergic receptor and rhodopsin systems
    • Lohse MJ, Andexinger S, Pitcher J, Trukawinski S, Codina J, Faure JP, Caron MG, Lefkowitz RJ: Receptor-specific desensitization with purified proteins: kinase dependence and receptor specificity of beta-arrestin and arrestin in the beta 2-adrenergic receptor and rhodopsin systems. J Biol Chem 1992; 267: 8558-8564.
    • (1992) J Biol Chem , vol.267 , pp. 8558-8564
    • Lohse, M.J.1    Andexinger, S.2    Pitcher, J.3    Trukawinski, S.4    Codina, J.5    Faure, J.P.6    Caron, M.G.7    Lefkowitz, R.J.8
  • 23
    • 0029160575 scopus 로고
    • Binding of purified recombinant beta-arrestin to guanine-nucleotide- binding-protein-coupled receptors
    • Sohlemann P, Hekman M, Puzicha M, Buchen C, Lohse MJ: Binding of purified recombinant beta-arrestin to guanine-nucleotide-binding-protein-coupled receptors. Eur J Biochem 1995; 232: 464-472.
    • (1995) Eur J Biochem , vol.232 , pp. 464-472
    • Sohlemann, P.1    Hekman, M.2    Puzicha, M.3    Buchen, C.4    Lohse, M.J.5
  • 24
    • 78650854802 scopus 로고    scopus 로고
    • Beta-arrestins as regulators of signal termination and transduction: How do they determine what to scaffold?
    • DeFea KA: Beta-arrestins as regulators of signal termination and transduction: How do they determine what to scaffold? Cell Signal 2011; 23: 621-629.
    • (2011) Cell Signal , vol.23 , pp. 621-629
    • Defea, K.A.1
  • 25
    • 28844463975 scopus 로고    scopus 로고
    • q-GRK2-Gβγ complex
    • DOI 10.1126/science.1118890
    • Tesmer VM, Kawano T, Shankaranarayanan A, Kozasa T, Tesmer JJG: Snapshot of activated G proteins at the membrane: the Galphaq-GRK2-Gbetagamma complex. Science 2005; 310: 1686-1690. (Pubitemid 41780792)
    • (2005) Science , vol.310 , Issue.5754 , pp. 1686-1690
    • Tesmer, V.M.1    Kawano, T.2    Shankaranarayanan, A.3    Kozasa, T.4    Tesmer, J.J.G.5
  • 26
    • 0034802172 scopus 로고    scopus 로고
    • Crystal structure of β-arrestin at 1.9 Å: Possible mechanism of receptor binding and membrane translocation
    • DOI 10.1016/S0969-2126(01)00644-X, PII S096921260100644X
    • Han M, Gurevich VV, Vishnivetskiy SA, Sigler PB, Schubert C: Crystal structure of betaarrestin at 1.9 A: possible mechanism of receptor binding and membrane translocation. Structure 2001; 9: 869-880. (Pubitemid 32913504)
    • (2001) Structure , vol.9 , Issue.9 , pp. 869-880
    • Han, M.1    Gurevich, V.V.2    Vishnivetskiy, S.A.3    Sigler, P.B.4    Schubert, C.5
  • 29
    • 77952840083 scopus 로고    scopus 로고
    • The complex G protein-coupled receptor kinase 2 (GRK2) interactome unveils new physiopathological targets
    • Penela P, Murga C, Ribas C, Lafarga V, Mayor F: The complex G protein-coupled receptor kinase 2 (GRK2) interactome unveils new physiopathological targets. Br J Pharmacol 2010; 160: 821-832.
    • (2010) Br J Pharmacol , vol.160 , pp. 821-832
    • Penela, P.1    Murga, C.2    Ribas, C.3    Lafarga, V.4    Mayor, F.5
  • 30
    • 78651404851 scopus 로고    scopus 로고
    • Multiple scaffolding functions of beta-arrestins in the degradation of G protein-coupled receptor kinase 2
    • Nogues L, Salcedo A, Mayor F, Penela P: Multiple scaffolding functions of beta-arrestins in the degradation of G protein-coupled receptor kinase 2. J Biol Chem 2011; 286: 1165-1173.
    • (2011) J Biol Chem , vol.286 , pp. 1165-1173
    • Nogues, L.1    Salcedo, A.2    Mayor, F.3    Penela, P.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.