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Volumn 219, Issue , 2014, Pages 225-257

Arrestin-dependent activation of ERK and Src family kinases

Author keywords

Arrestin; Extracellular signal regulated kinase; G protein coupled receptor; Signal transduction; Src family nonreceptor tyrosine kinase

Indexed keywords

CLATHRIN; G PROTEIN COUPLED RECEPTOR; MITOGEN ACTIVATED PROTEIN KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE 3; MITOGEN ACTIVATED PROTEIN KINASE KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE P38; PROTEIN TYROSINE KINASE; RAF PROTEIN; RETINA S ANTIGEN; STRESS ACTIVATED PROTEIN KINASE; G PROTEIN COUPLED RECEPTOR KINASE; MITOGEN ACTIVATED PROTEIN KINASE; NON RECEPTOR PROTEIN TYROSINE PHOSPHATASE; SCAFFOLD PROTEIN;

EID: 84958526501     PISSN: 01712004     EISSN: 18650325     Source Type: Book Series    
DOI: 10.1007/978-3-642-41199-1_12     Document Type: Article
Times cited : (31)

References (149)
  • 1
    • 0033555946 scopus 로고    scopus 로고
    • Src-mediated tyrosine phosphorylation of dynamin is required for beta2-adrenergic receptor internalization and mitogen-activated protein kinase signaling
    • Ahn S, Maudsley S, Luttrell LM et al (1999) Src-mediated tyrosine phosphorylation of dynamin is required for beta2-adrenergic receptor internalization and mitogen-activated protein kinase signaling. J Biol Chem 274:1185-1188
    • (1999) J Biol Chem , vol.274 , pp. 1185-1188
    • Ahn, S.1    Maudsley, S.2    Luttrell, L.M.3
  • 2
    • 0037135528 scopus 로고    scopus 로고
    • Src-dependent tyrosine phosphorylation regulates dynamin self-assembly and ligand-induced endocytosis of the epidermal growth factor receptor
    • Ahn S, Kim J, Lucaveche CL et al (2002) Src-dependent tyrosine phosphorylation regulates dynamin self-assembly and ligand-induced endocytosis of the epidermal growth factor receptor. J Biol Chem 277:26642-26651
    • (2002) J Biol Chem , vol.277 , pp. 26642-26651
    • Ahn, S.1    Kim, J.2    Lucaveche, C.L.3
  • 3
    • 4143070533 scopus 로고    scopus 로고
    • Differential kinetic and spatial patterns of beta-arrestin and G protein-mediated ERK activation by the angiotensin II receptor
    • Ahn S, Shenoy SK, Wei H et al (2004a) Differential kinetic and spatial patterns of beta-arrestin and G protein-mediated ERK activation by the angiotensin II receptor. J Biol Chem 279:35518-35525
    • (2004) J Biol Chem , vol.279 , pp. 35518-35525
    • Ahn, S.1    Shenoy, S.K.2    Wei, H.3
  • 4
    • 1542350042 scopus 로고    scopus 로고
    • Reciprocal regulation of angiotensin receptor-activated extracellular signal-regulated kinases by beta-arrestins 1 and 2
    • Ahn S, Wei H, Garrison TR et al (2004b) Reciprocal regulation of angiotensin receptor-activated extracellular signal-regulated kinases by beta-arrestins 1 and 2. J Biol Chem 279:7807-7811
    • (2004) J Biol Chem , vol.279 , pp. 7807-7811
    • Ahn, S.1    Wei, H.2    Garrison, T.R.3
  • 5
    • 34247341288 scopus 로고    scopus 로고
    • Differential extracellular signal-regulated kinases 1 and 2 activation by the angiotensin type 1 receptor supports distinct phenotypes of cardiac myocytes
    • Aplin M, Christensen GL, Schneider M et al (2007) Differential extracellular signal-regulated kinases 1 and 2 activation by the angiotensin type 1 receptor supports distinct phenotypes of cardiac myocytes. Basic Clin Pharmacol Toxicol 100:296-301
    • (2007) Basic Clin Pharmacol Toxicol , vol.100 , pp. 296-301
    • Aplin, M.1    Christensen, G.L.2    Schneider, M.3
  • 6
    • 84873326843 scopus 로고    scopus 로고
    • Biasing the parathyroid hormone receptor: Relating in vitro ligand efficacy to in vivo biological activity
    • Appleton KM, Lee MH, Alele C (2013) Biasing the parathyroid hormone receptor: relating in vitro ligand efficacy to in vivo biological activity. Methods Enzymol 522:229-262
    • (2013) Methods Enzymol , vol.522 , pp. 229-262
    • Appleton, K.M.1    Lee, M.H.2    Alele, C.3
  • 7
    • 0032539904 scopus 로고    scopus 로고
    • Monocyte chemoattractant protein-1-induced CCR2B receptor desensitization mediated by the G protein-coupled receptor kinase 2
    • Aragay AM, Mellado M, Frade JM et al (1998) Monocyte chemoattractant protein-1-induced CCR2B receptor desensitization mediated by the G protein-coupled receptor kinase 2. Proc Natl Acad Sci USA 95:2985-2990
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 2985-2990
    • Aragay, A.M.1    Mellado, M.2    Frade, J.M.3
  • 8
    • 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 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 USA 100:11406-11411
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 11406-11411
    • Azzi, M.1    Charest, P.G.2    Angers, S.3
  • 9
    • 5944221106 scopus 로고    scopus 로고
    • Regulation of tyrosine kinase activation and granule release through beta-arrestin by CXCRI
    • Barlic J, Andrews JD, Kelvin AA et al (2000) Regulation of tyrosine kinase activation and granule release through beta-arrestin by CXCRI. Nat Immunol 1:227-233
    • (2000) Nat Immunol , vol.1 , pp. 227-233
    • Barlic, J.1    Andrews, J.D.2    Kelvin, A.A.3
  • 10
    • 14844338481 scopus 로고    scopus 로고
    • Beta-Arrestin 1 and Galphaq/11 coordinately activate RhoA and stress fiber formation following receptor stimulation
    • Barnes WG, Reiter E, Violin JD et al (2005) beta-Arrestin 1 and Galphaq/11 coordinately activate RhoA and stress fiber formation following receptor stimulation. J Biol Chem 280:8041-8050
    • (2005) J Biol Chem , vol.280 , pp. 8041-8050
    • Barnes, W.G.1    Reiter, E.2    Violin, J.D.3
  • 11
    • 37549035071 scopus 로고    scopus 로고
    • Arrestin-2 interacts with the ubiquitin-protein isopeptide ligase atrophin-interacting protein 4 and mediates endosomal sorting of the chemokine receptor CXCR4
    • Bhandari D, Trejo J, Benovic JL et al (2007) Arrestin-2 interacts with the ubiquitin-protein isopeptide ligase atrophin-interacting protein 4 and mediates endosomal sorting of the chemokine receptor CXCR4. J Biol Chem 282:36971-36979
    • (2007) J Biol Chem , vol.282 , pp. 36971-36979
    • Bhandari, D.1    Trejo, J.2    Benovic, J.L.3
  • 12
    • 0038305915 scopus 로고    scopus 로고
    • ERK and RhoA differentially regulate pseudopodia growth and retraction during chemotaxis
    • Brahmbhatt AA, Klemke RL (2003) ERK and RhoA differentially regulate pseudopodia growth and retraction during chemotaxis. J Biol Chem 278:13016-13025
    • (2003) J Biol Chem , vol.278 , pp. 13016-13025
    • Brahmbhatt, A.A.1    Klemke, R.L.2
  • 13
    • 84861740178 scopus 로고    scopus 로고
    • Silent scaffolds: Inhibition of c-Jun N-terminal kinase 3 activity in cell by dominant-negative arrestin-3 mutant
    • Breitman M, Kook S, Gimenez LE et al (2012) Silent scaffolds: inhibition of c-Jun N-terminal kinase 3 activity in cell by dominant-negative arrestin-3 mutant. J Biol Chem 287:19653-19664
    • (2012) J Biol Chem , vol.287 , pp. 19653-19664
    • Breitman, M.1    Kook, S.2    Gimenez, L.E.3
  • 14
    • 0031915950 scopus 로고    scopus 로고
    • Regulation of a calcium-dependent tyrosine kinase in vascular smooth muscle cells by angiotensin II and platelet-derived growth factor. Dependence on calcium and the actin cytoskeleton
    • Brinson RE, Harding T, Diliberto PA et al (1998) Regulation of a calcium-dependent tyrosine kinase in vascular smooth muscle cells by angiotensin II and platelet-derived growth factor. Dependence on calcium and the actin cytoskeleton. J Biol Chem 273:1711-1718
    • (1998) J Biol Chem , vol.273 , pp. 1711-1718
    • Brinson, R.E.1    Harding, T.2    Diliberto, P.A.3
  • 15
    • 0034009390 scopus 로고    scopus 로고
    • Signal transduction: Hanging on a scaffold
    • Burack WR, Shaw AS (2000) Signal transduction: hanging on a scaffold. Curr Opin Cell Biol 12:211-216
    • (2000) Curr Opin Cell Biol , vol.12 , pp. 211-216
    • Burack, W.R.1    Shaw, A.S.2
  • 16
    • 0034681203 scopus 로고    scopus 로고
    • EGF receptor transactivation mediated by the proteolytic production of EGF-like agonists
    • 2000 pe1
    • Carpenter G (2000) EGF receptor transactivation mediated by the proteolytic production of EGF-like agonists. Sci STKE 2000(15):pe1
    • (2000) Sci STKE , pp. 15
    • Carpenter, G.1
  • 17
    • 70349646820 scopus 로고    scopus 로고
    • An arrestin-dependent multi-kinase signaling complex mediates MIP-1beta/CCL4 signaling and chemotaxis of primary human macrophages
    • Cheung R, Malik M, Ravyn V et al (2009) An arrestin-dependent multi-kinase signaling complex mediates MIP-1beta/CCL4 signaling and chemotaxis of primary human macrophages. J Leukoc Biol 86:833-845
    • (2009) J Leukoc Biol , vol.86 , pp. 833-845
    • Cheung, R.1    Malik, M.2    Ravyn, V.3
  • 18
    • 0027983908 scopus 로고
    • Ste5 tethers multiple protein kinases in the MAP kinase cascade required for mating in S. Cerevisiae
    • Choi KY, Satterberg B, Lyons DM et al (1994) Ste5 tethers multiple protein kinases in the MAP kinase cascade required for mating in S. cerevisiae. Cell 78:499-512
    • (1994) Cell , vol.78 , pp. 499-512
    • Choi, K.Y.1    Satterberg, B.2    Lyons, D.M.3
  • 19
    • 0036258990 scopus 로고    scopus 로고
    • G protein-coupled receptor allosterism and complexing
    • Christopoulos A, Kenakin T (2002) G protein-coupled receptor allosterism and complexing. Pharmacol Rev 54:323-374
    • (2002) Pharmacol Rev , vol.54 , pp. 323-374
    • Christopoulos, A.1    Kenakin, T.2
  • 20
    • 70249092519 scopus 로고    scopus 로고
    • The prostaglandin receptor EP2 activates multiple signaling pathways and beta-arrestin1 complex formation during mouse skin papilloma development
    • Chun KS, Lao HC, Trempus CS et al (2009) The prostaglandin receptor EP2 activates multiple signaling pathways and beta-arrestin1 complex formation during mouse skin papilloma development. Carcinogenesis 30:1620-1627
    • (2009) Carcinogenesis , vol.30 , pp. 1620-1627
    • Chun, K.S.1    Lao, H.C.2    Trempus, C.S.3
  • 21
    • 83155164567 scopus 로고    scopus 로고
    • The effect of arrestin conformation on the recruitment of c-Raf1 MEK1, and ERK1/2 activation
    • Coffa S, Breitman M, Hanson SM et al (2011a) The effect of arrestin conformation on the recruitment of c-Raf1, MEK1, and ERK1/2 activation. PloS One 6:e28723
    • (2011) PloS One , vol.6
    • Coffa, S.1    Breitman, M.2    Hanson, S.M.3
  • 22
    • 80051498152 scopus 로고    scopus 로고
    • A single mutation in arrestin-2 prevents ERK1/2 activation by reducing c-Raf1 binding
    • Coffa S, Breitman M, Spiller BW et al (2011b) A single mutation in arrestin-2 prevents ERK1/2 activation by reducing c-Raf1 binding. Biochemistry 50:6951-6958
    • (2011) Biochemistry , vol.50 , pp. 6951-6958
    • Coffa, S.1    Breitman, M.2    Spiller, B.W.3
  • 23
    • 0031975838 scopus 로고    scopus 로고
    • Essential role for G protein-coupled receptor endocytosis in the activation of mitogen-activated protein kinase
    • Daaka Y, Luttrell LM, Ahn S (1998) Essential role for G protein-coupled receptor endocytosis in the activation of mitogen-activated protein kinase. J Biol Chem 273:685-688
    • (1998) J Biol Chem , vol.273 , pp. 685-688
    • Daaka, Y.1    Luttrell, L.M.2    Ahn, S.3
  • 24
    • 33746672599 scopus 로고    scopus 로고
    • Nicotine induces cell proliferation by beta-arrestinmediated activation of Src and Rb-Raf-1 pathways
    • Dasgupta P, Rastogi S, Pillai S et al (2006) Nicotine induces cell proliferation by beta-arrestinmediated activation of Src and Rb-Raf-1 pathways. J Clin Invest 116:2208-2217
    • (2006) J Clin Invest , vol.116 , pp. 2208-2217
    • Dasgupta, P.1    Rastogi, S.2    Pillai, S.3
  • 25
    • 0034689003 scopus 로고    scopus 로고
    • Beta-Arrestin-dependent endocytosis of proteinase-activated receptor 2 is required for intracellular targeting of activated ERK1/2
    • DeFea KA, Zalevsky J, Thoma MS et al (2000a) beta-Arrestin-dependent endocytosis of proteinase-activated receptor 2 is required for intracellular targeting of activated ERK1/2. J Cell Biol 148:1267-1281
    • (2000) J Cell Biol , vol.148 , pp. 1267-1281
    • Defea, K.A.1    Zalevsky, J.2    Thoma, M.S.3
  • 26
    • 0034718604 scopus 로고    scopus 로고
    • The proliferative and antiapoptotic effects of substance P are facilitated by formation of a beta-arrestin-dependent scaffolding complex
    • DeFea KA, Vaughn ZD, O'Bryan EM et al (2000b) The proliferative and antiapoptotic effects of substance P are facilitated by formation of a beta-arrestin-dependent scaffolding complex. Proc Natl Acad Sci USA 97:11086-11091
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 11086-11091
    • Defea, K.A.1    Vaughn, Z.D.2    O'Bryan, E.M.3
  • 27
    • 0033553526 scopus 로고    scopus 로고
    • Pleiotropic coupling of G protein-coupled receptors to the mitogen-activated protein kinase cascade. Role of focal adhesions and receptor tyrosine kinases
    • Della Rocca GJ, Maudsley SR, Daaka Y et al (1999) Pleiotropic coupling of G protein-coupled receptors to the mitogen-activated protein kinase cascade. Role of focal adhesions and receptor tyrosine kinases. J Biol Chem 274:13978-13984
    • (1999) J Biol Chem , vol.274 , pp. 13978-13984
    • Della Rocca, G.J.1    Maudsley, S.R.2    Daaka, Y.3
  • 28
    • 0032480888 scopus 로고    scopus 로고
    • Epac is a Rap1 guanine nucleotide exchange factor directly activated by cAMP
    • DeRooij J, Zwartkruis FL, Verheijen MH et al (1998) Epac is a Rap1 guanine nucleotide exchange factor directly activated by cAMP. Nature 396:474-477
    • (1998) Nature , vol.396 , pp. 474-477
    • Derooij, J.1    Zwartkruis, F.L.2    Verheijen, M.H.3
  • 29
    • 44849117014 scopus 로고    scopus 로고
    • Beta-arrestin-mediated signaling regulates protein synthesis
    • DeWire SM, Kim J, Whalen EJ et al (2008) Beta-arrestin-mediated signaling regulates protein synthesis. J Biol Chem 283:10611-10620
    • (2008) J Biol Chem , vol.283 , pp. 10611-10620
    • Dewire, S.M.1    Kim, J.2    Whalen, E.J.3
  • 30
    • 0029907265 scopus 로고    scopus 로고
    • A role for Pyk2 and Src in linking G-protein-coupled receptors with MAP kinase activation
    • Dikic I, Tokiwa G, Lev S et al (1996) A role for Pyk2 and Src in linking G-protein-coupled receptors with MAP kinase activation. Nature 383:547-550
    • (1996) Nature , vol.383 , pp. 547-550
    • Dikic, I.1    Tokiwa, G.2    Lev, S.3
  • 31
    • 0032486285 scopus 로고    scopus 로고
    • Identification of a new Pyk2 isoform implicated in chemokine and antigen receptor signaling
    • Dikic I, Dikic I, Schlessinger J (1998) Identification of a new Pyk2 isoform implicated in chemokine and antigen receptor signaling. J Biol Chem 273:14301-14308
    • (1998) J Biol Chem , vol.273 , pp. 14301-14308
    • Dikic, I.1    Dikic, I.2    Schlessinger, J.3
  • 32
    • 41949089470 scopus 로고    scopus 로고
    • Beta-Arrestin-biased agonism at the beta2-adrenergic receptor
    • Drake MT, Violin JD, Whalen EJ et al (2008) beta-Arrestin-biased agonism at the beta2-adrenergic receptor. J Biol Chem 283:5669-5676
    • (2008) J Biol Chem , vol.283 , pp. 5669-5676
    • Drake, M.T.1    Violin, J.D.2    Whalen, E.J.3
  • 33
    • 0034111097 scopus 로고    scopus 로고
    • Agonist-dependent modulation of G protein-coupled receptor kinase 2 by mitogen-activated protein kinases
    • Elorza A, Samago S, Mayor F Jr (2000) Agonist-dependent modulation of G protein-coupled receptor kinase 2 by mitogen-activated protein kinases. Mol Pharmacol 57:778-783
    • (2000) Mol Pharmacol , vol.57 , pp. 778-783
    • Elorza, A.1    Samago, S.2    Mayor Jr., F.3
  • 34
    • 0042707658 scopus 로고    scopus 로고
    • MAPK-dependent degradation of G protein-coupled receptor kinase 2
    • Elorza A, Penela P, Sarnago S et al (2003) MAPK-dependent degradation of G protein-coupled receptor kinase 2. J Biol Chem 278:29164-29173
    • (2003) J Biol Chem , vol.278 , pp. 29164-29173
    • Elorza, A.1    Penela, P.2    Sarnago, S.3
  • 35
    • 0028958025 scopus 로고
    • Src family protein tyrosine kinases and cellular signal transduction pathways
    • Erpel T, Courtneidge SA (1995) Src family protein tyrosine kinases and cellular signal transduction pathways. Curr Opin Cell Biol 7:176-182
    • (1995) Curr Opin Cell Biol , vol.7 , pp. 176-182
    • Erpel, T.1    Courtneidge, S.A.2
  • 36
    • 0035918269 scopus 로고    scopus 로고
    • C-Src tyrosine kinase binds the beta2-adrenergic receptor via phospho-Tyr-350, phosphorylates G-protein-linked receptor kinase 2, and mediates agonist-induced receptor desensitization
    • Fan G, Shumay E, Malbon CC et al (2001) c-Src tyrosine kinase binds the beta2-adrenergic receptor via phospho-Tyr-350, phosphorylates G-protein-linked receptor kinase 2, and mediates agonist-induced receptor desensitization. J Biol Chem 276:13240-13247
    • (2001) J Biol Chem , vol.276 , pp. 13240-13247
    • Fan, G.1    Shumay, E.2    Malbon, C.C.3
  • 37
    • 0035101820 scopus 로고    scopus 로고
    • Evolving concepts in G protein-coupled receptor endocytosis: The role in receptor desensitization and signaling
    • Ferguson SS (2001) Evolving concepts in G protein-coupled receptor endocytosis: the role in receptor desensitization and signaling. Pharmacol Rev 53:1-24
    • (2001) Pharmacol Rev , vol.53 , pp. 1-24
    • Ferguson, S.S.1
  • 38
    • 13544264506 scopus 로고    scopus 로고
    • C-Src regulates clathrin adapter protein 2 interaction with beta-arrestin and the angiotensin II type 1 receptor during clathrin-mediated internalization
    • Fessart D, Simaan M, Laporte SA (2005) c-Src regulates clathrin adapter protein 2 interaction with beta-arrestin and the angiotensin II type 1 receptor during clathrin-mediated internalization. Mol Endocrinol 19:491-503
    • (2005) Mol Endocrinol , vol.19 , pp. 491-503
    • Fessart, D.1    Simaan, M.2    Laporte, S.A.3
  • 39
    • 34250654452 scopus 로고    scopus 로고
    • Src-dependent phosphorylation of beta2-adaptin dissociates the beta-arrestin-AP-2 complex
    • Fessart D, Simaan M, Zimmerman B et al (2007) Src-dependent phosphorylation of beta2-adaptin dissociates the beta-arrestin-AP-2 complex. J Cell Sci 120:1723-1732
    • (2007) J Cell Sci , vol.120 , pp. 1723-1732
    • Fessart, D.1    Simaan, M.2    Zimmerman, B.3
  • 40
    • 0037188469 scopus 로고    scopus 로고
    • Defective lymphocyte chemotaxis in betaarrestin2-and GRK6-deficient mice
    • Fong AM, Premont RT, Richardson RM et al (2002) Defective lymphocyte chemotaxis in betaarrestin2-and GRK6-deficient mice. Proc Natl Acad Sci USA 99:7478-7483
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 7478-7483
    • Fong, A.M.1    Premont, R.T.2    Richardson, R.M.3
  • 41
    • 0029719789 scopus 로고    scopus 로고
    • Desensitization of G protein-coupled receptors
    • Freedman NJ, Lefkowitz RJ (1996) Desensitization of G protein-coupled receptors. Recent Prog Horm Res 51:319-351
    • (1996) Recent Prog Horm Res , vol.51 , pp. 319-351
    • Freedman, N.J.1    Lefkowitz, R.J.2
  • 42
    • 33751162165 scopus 로고    scopus 로고
    • Distinct signaling profiles of beta1 and beta2 adrenergic receptor ligands toward adenylyl cyclase and mitogen-activated protein kinase reveals the pluridimensionality of efficacy
    • Galandrin S, Bouvier M (2006) Distinct signaling profiles of beta1 and beta2 adrenergic receptor ligands toward adenylyl cyclase and mitogen-activated protein kinase reveals the pluridimensionality of efficacy. Mol Pharmacol 70:1575-1584
    • (2006) Mol Pharmacol , vol.70 , pp. 1575-1584
    • Galandrin, S.1    Bouvier, M.2
  • 43
    • 49549096431 scopus 로고    scopus 로고
    • Arrestin-3 is essential for the activation of Fyn by the luteinizing hormone receptor (LHR) in MA-10 cells
    • Galet C, Ascoli M (2008) Arrestin-3 is essential for the activation of Fyn by the luteinizing hormone receptor (LHR) in MA-10 cells. Cell Signal 20:1822-2829
    • (2008) Cell Signal , vol.20 , pp. 1822-2829
    • Galet, C.1    Ascoli, M.2
  • 44
    • 0141483377 scopus 로고    scopus 로고
    • A beta-arrestin-dependent scaffold is associated with prolonged MAPK activation in pseudopodia during protease-activated receptor-2-induced chemotaxis
    • Ge L, Ly Y, Hollenberg M et al (2003) A beta-arrestin-dependent scaffold is associated with prolonged MAPK activation in pseudopodia during protease-activated receptor-2-induced chemotaxis. J Biol Chem 278:34418-34426
    • (2003) J Biol Chem , vol.278 , pp. 34418-34426
    • Ge, L.1    Ly, Y.2    Hollenberg, M.3
  • 45
    • 11244255416 scopus 로고    scopus 로고
    • Constitutive protease-activated receptor-2-mediated migration of MDA MB-231 breast cancer cells requires both beta-arrestin-1 and J Biol Chem 279 55419-55424 breast cancer cells requires both beta-arrestin-1 and-2
    • Ge L, Shenoy SK, Lefkowitz RJ et al (2004) Constitutive protease-activated receptor-2-mediated migration of MDA MB-231 breast cancer cells requires both beta-arrestin-1 and-J Biol Chem 279 55419-55424 breast cancer cells requires both beta-arrestin-1 and-2. J Biol Chem 279:55419-55424
    • (2004) J Biol Chem , vol.279 , pp. 55419-55424
    • Ge, L.1    Shenoy, S.K.2    Lefkowitz, R.J.3
  • 46
    • 25444495647 scopus 로고    scopus 로고
    • Beta-Arrestin 2 expression determines the transcriptional response to lysophosphatidic acid stimulation in murine embryo fibroblasts
    • Gesty-Palmer D, El Shewy H, Kohout TA et al (2005) beta-Arrestin 2 expression determines the transcriptional response to lysophosphatidic acid stimulation in murine embryo fibroblasts. J Biol Chem 280:32157-32167
    • (2005) J Biol Chem , vol.280 , pp. 32157-32167
    • Gesty-Palmer, D.1    El Shewy, H.2    Kohout, T.A.3
  • 47
    • 33744957160 scopus 로고    scopus 로고
    • Distinct beta-arrestin-and G protein-dependent pathways for parathyroid hormone receptor-stimulated ERK1/2 activation
    • Gesty-Palmer D, Chen M, Reiter E et al (2006) Distinct beta-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
  • 48
    • 73949084919 scopus 로고    scopus 로고
    • A beta-arrestin biased agonist of the parathyroid hormone receptor (PTH1R) promotes bone formation independent of G protein activation
    • 1ra1
    • Gesty-Palmer D, Flannery P, Yuan L et al (2009) A beta-arrestin biased agonist of the parathyroid hormone receptor (PTH1R) promotes bone formation independent of G protein activation. Sci Transl Med 1:1ra1
    • (2009) Sci Transl Med , pp. 1
    • Gesty-Palmer, D.1    Flannery, P.2    Yuan, L.3
  • 49
    • 84873042671 scopus 로고    scopus 로고
    • Beta-Arrestin pathway-selective G protein-coupled receptor agonists engender unique biological efficacy in vivo
    • Gesty-Palmer D, Liao S, Yuan L et al (2013) beta-Arrestin pathway-selective G protein-coupled receptor agonists engender unique biological efficacy in vivo. Mol Endocrinol 27:296-314
    • (2013) Mol Endocrinol , vol.27 , pp. 296-314
    • Gesty-Palmer, D.1    Liao, S.2    Yuan, L.3
  • 50
    • 0037059804 scopus 로고    scopus 로고
    • Light-dependent association of Src with photoreceptor rod outer segment membrane proteins in vivo
    • Ghalayini AJ, Desai N, Smith KR et al (2002) Light-dependent association of Src with photoreceptor rod outer segment membrane proteins in vivo. J Biol Chem 277:1469-1476
    • (2002) J Biol Chem , vol.277 , pp. 1469-1476
    • Ghalayini, A.J.1    Desai, N.2    Smith, K.R.3
  • 51
    • 33947607229 scopus 로고    scopus 로고
    • Arrestin mobilizes signaling proteins to the cytoskeleton and redirects their activity
    • Hanson SM, Cleghorn WM, Francis DJ et al (2007) Arrestin mobilizes signaling proteins to the cytoskeleton and redirects their activity. J Mol Biol 368:375-387
    • (2007) J Mol Biol , vol.368 , pp. 375-387
    • Hanson, S.M.1    Cleghorn, W.M.2    Francis, D.J.3
  • 52
    • 0035413610 scopus 로고    scopus 로고
    • C-Src tyrosine phosphorylation of epidermal growth factor receptor P190 RhoGAP, and focal adhesion kinase regulates diverse cellular processes
    • Haskell MD, Slack JK, Parsons JT et al (2001) c-Src tyrosine phosphorylation of epidermal growth factor receptor, P190 RhoGAP, and focal adhesion kinase regulates diverse cellular processes. Chem Rev 101:2425-2440
    • (2001) Chem Rev , vol.101 , pp. 2425-2440
    • Haskell, M.D.1    Slack, J.K.2    Parsons, J.T.3
  • 53
    • 0028982948 scopus 로고
    • Distinct pathways of Gi-and Gq-mediated mitogen activated protein kinase activation
    • Hawes BE, van Biesen T, Koch WJ et al (1995) Distinct pathways of Gi-and Gq-mediated mitogen activated protein kinase activation. J Biol Chem 270:17148-17153
    • (1995) J Biol Chem , vol.270 , pp. 17148-17153
    • Hawes, B.E.1    Van Biesen, T.2    Koch, W.J.3
  • 54
    • 84863331506 scopus 로고    scopus 로고
    • Competing G protein-coupled receptor kinases balance G protein and beta-arrestin signaling
    • Heitzler D, Durand G, Gallay N et al (2012) Competing G protein-coupled receptor kinases balance G protein and beta-arrestin signaling. Mol Syst Biol 8:590
    • (2012) Mol Syst Biol , vol.8 , pp. 590
    • Heitzler, D.1    Durand, G.2    Gallay, N.3
  • 55
    • 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, Qian H, Pipolo L 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    Qian, H.2    Pipolo, L.3
  • 56
    • 15744390934 scopus 로고    scopus 로고
    • Beta-arrestin 2-dependent angiotensin II type 1A receptor-mediated pathway of chemotaxis
    • Hunton DL, Barnes WG, Kim J et al (2005) Beta-arrestin 2-dependent angiotensin II type 1A receptor-mediated pathway of chemotaxis. Mol Pharmacol 67:1229-1236
    • (2005) Mol Pharmacol , vol.67 , pp. 1229-1236
    • Hunton, D.L.1    Barnes, W.G.2    Kim, J.3
  • 57
    • 12544254298 scopus 로고    scopus 로고
    • Insulin-induced beta-arrestin1 Ser-412 phosphorylation is a mechanism for desensitization of ERK activation by Galphai-coupled receptors J Biol Chem 280 1016-1023 phosphorylation is a mechanism for desensitization of ERK activation by Galphai-coupled receptors
    • Hupfeld CJ, Resnik JL, Ugi S et al (2005) Insulin-induced beta-arrestin1 Ser-412 phosphorylation is a mechanism for desensitization of ERK activation by Galphai-coupled receptors J Biol Chem 280 1016-1023 phosphorylation is a mechanism for desensitization of ERK activation by Galphai-coupled receptors. J Biol Chem 280:1016-1023
    • (2005) J Biol Chem , vol.280 , pp. 1016-1023
    • Hupfeld, C.J.1    Resnik, J.L.2    Ugi, S.3
  • 58
    • 0032959746 scopus 로고    scopus 로고
    • Requirement of receptor internalization for opioid stimulation of mitogen-activated protein kinase: Biochemical and immunofluorescence confocal microscopic evidence
    • Ignatova EG, Belcheva MM, Bohn LM et al (1999) Requirement of receptor internalization for opioid stimulation of mitogen-activated protein kinase: biochemical and immunofluorescence confocal microscopic evidence. J Neurosci 19:56-63
    • (1999) J Neurosci , vol.19 , pp. 56-63
    • Ignatova, E.G.1    Belcheva, M.M.2    Bohn, L.M.3
  • 59
    • 0035941205 scopus 로고    scopus 로고
    • Beta-Arrestin-mediated recruitment of the Src family kinase Yes mediates endothelin-1-stimulated glucose transport
    • Imamura T, Huang J, Dalle S et al (2001) beta-Arrestin-mediated recruitment of the Src family kinase Yes mediates endothelin-1-stimulated glucose transport. J Biol Chem 276:43663-43667
    • (2001) J Biol Chem , vol.276 , pp. 43663-43667
    • Imamura, T.1    Huang, J.2    Dalle, S.3
  • 60
    • 33745838934 scopus 로고    scopus 로고
    • Constitutive ERK1/2 activation by a chimeric neurokinin 1 receptor-beta-arrestin1 fusion protein. Probing the composition and function of the G protein-coupled receptor signalsome
    • Jafri F, El-Shewy HM, Lee MH et al (2006) Constitutive ERK1/2 activation by a chimeric neurokinin 1 receptor-beta-arrestin1 fusion protein. Probing the composition and function of the G protein-coupled receptor " signalsome". J Biol Chem 281:19346-19357
    • (2006) J Biol Chem , vol.281 , pp. 19346-19357
    • Jafri, F.1    El-Shewy, H.M.2    Lee, M.H.3
  • 61
    • 0029976454 scopus 로고    scopus 로고
    • Receptor conformational induction versus selection: All part of the same energy landscape
    • Kenakin TP (1996) Receptor conformational induction versus selection: All part of the same energy landscape. Trends Pharmacol Sci 17:190-191
    • (1996) Trends Pharmacol Sci , vol.17 , pp. 190-191
    • Kenakin, T.P.1
  • 62
    • 77952354490 scopus 로고    scopus 로고
    • Seven transmembrane receptors as shapeshifting proteins: The impact of allosteric modulation and functional selectivity on new drug discovery
    • Kenakin T, Miller LE (2010) Seven transmembrane receptors as shapeshifting proteins: the impact of allosteric modulation and functional selectivity on new drug discovery. Pharmacol Rev 62:265-304
    • (2010) Pharmacol Rev , vol.62 , pp. 265-304
    • Kenakin, T.1    Miller, L.E.2
  • 63
    • 79957607077 scopus 로고    scopus 로고
    • The beta-arrestin pathway-selective type 1A angiotensin receptor (AT1A) agonist [Sar1, Ile4, Ile8]angiotensin II regulates a robust G protein-independent signaling network
    • Kendall RT, Strungs EG, Rachidi SM et al (2011) The beta-arrestin pathway-selective type 1A angiotensin receptor (AT1A) agonist [Sar1, Ile4, Ile8]angiotensin II regulates a robust G protein-independent signaling network. J Biol Chem 286:19880-19891
    • (2011) J Biol Chem , vol.286 , pp. 19880-19891
    • Kendall, R.T.1    Strungs, E.G.2    Rachidi, S.M.3
  • 64
    • 13444291851 scopus 로고    scopus 로고
    • Functional antagonism of different G protein-coupled receptor kinases for beta-arrestin-mediated angiotensin II receptor signaling
    • Kim J, Ahn S, Ren XR (2005) Functional antagonism of different G protein-coupled receptor kinases for beta-arrestin-mediated angiotensin II receptor signaling. Proc Natl Acad Sci USA 102:1442-1447
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 1442-1447
    • Kim, J.1    Ahn, S.2    Ren, X.R.3
  • 65
    • 48049101191 scopus 로고    scopus 로고
    • Beta-arrestins regulate atherosclerosis and neointimal hyperplasia by controlling smooth muscle cell proliferation and migration
    • Kim J, Zhang L, Peppel K et al (2008) Beta-arrestins regulate atherosclerosis and neointimal hyperplasia by controlling smooth muscle cell proliferation and migration. Circ Res 103:70-79
    • (2008) Circ Res , vol.103 , pp. 70-79
    • Kim, J.1    Zhang, L.2    Peppel, K.3
  • 66
    • 66449134043 scopus 로고    scopus 로고
    • Independent beta-arrestin2 and Gq/protein kinase Czeta pathways for ERK stimulated by angiotensin type 1A receptors in vascular smooth muscle cells converge on transactivation of the epidermal growth factor receptor
    • Kim J, Ahn S, Rajagopal K et al (2009) Independent beta-arrestin2 and Gq/protein kinase Czeta pathways for ERK stimulated by angiotensin type 1A receptors in vascular smooth muscle cells converge on transactivation of the epidermal growth factor receptor. J Biol Chem 284:11953-11962
    • (2009) J Biol Chem , vol.284 , pp. 11953-11962
    • Kim, J.1    Ahn, S.2    Rajagopal, K.3
  • 67
    • 2542423686 scopus 로고    scopus 로고
    • Differential desensitization, receptor phosphorylation, beta-arrestin recruitment, and ERK1/2 activation by the two endogenous ligands for the CC chemokine receptor 7
    • Kohout TA, Nicholas SL, Perry SJ et al (2004) Differential desensitization, receptor phosphorylation, beta-arrestin recruitment, and ERK1/2 activation by the two endogenous ligands for the CC chemokine receptor 7. J Biol Chem 279:23214-23222
    • (2004) J Biol Chem , vol.279 , pp. 23214-23222
    • Kohout, T.A.1    Nicholas, S.L.2    Perry, S.J.3
  • 68
    • 0027326410 scopus 로고
    • Protein kinase C alpha activates Raf-1 by direct phosphorylation
    • Kolch W, Heldecker G, Kochs G et al (1993) Protein kinase C alpha activates Raf-1 by direct phosphorylation. Nature 364:249-255
    • (1993) Nature , vol.364 , pp. 249-255
    • Kolch, W.1    Heldecker, G.2    Kochs, G.3
  • 69
    • 0029744885 scopus 로고    scopus 로고
    • Sounding the alarm: Protein kinase cascades activated by stress and inflammation
    • Kryiakis JM, Avruch J (1996) Sounding the alarm: protein kinase cascades activated by stress and inflammation. J Biol Chem 271:24313-24316
    • (1996) J Biol Chem , vol.271 , pp. 24313-24316
    • Kryiakis, J.M.1    Avruch, J.2
  • 70
    • 33749238356 scopus 로고    scopus 로고
    • Opposing effects of beta-arrestin1 and beta-arrestin2 on activation and degradation of Src induced by protease-activated receptor 1
    • Kuo F-T, Lu T-L, Fu H-W (2006) Opposing effects of beta-arrestin1 and beta-arrestin2 on activation and degradation of Src induced by protease-activated receptor 1. Cell Signal 18:1914-1923
    • (2006) Cell Signal , vol.18 , pp. 1914-1923
    • Kuo, F.-T.1    Lu, T.-L.2    Fu, H.-W.3
  • 71
    • 38349118001 scopus 로고    scopus 로고
    • Role of beta-arrestin-mediated desensitization and signaling in the control of angiotensin AT1a receptor-stimulated transcription
    • Lee M-H, El-Shewy HM, Luttrell DK et al (2008) Role of beta-arrestin-mediated desensitization and signaling in the control of angiotensin AT1a receptor-stimulated transcription. J Biol Chem 283:2088-2097
    • (2008) J Biol Chem , vol.283 , pp. 2088-2097
    • Lee, M.-H.1    El-Shewy, H.M.2    Luttrell, D.K.3
  • 72
    • 84864026147 scopus 로고    scopus 로고
    • Beta-arrestin 2-dependent activation of ERK1/2 is required for ADP-induced paxillin phosphorylation at Ser(83) and microglia chemotaxis
    • Lee SH, Hollingsworth R, Kwon HY et al (2012) beta-arrestin 2-dependent activation of ERK1/2 is required for ADP-induced paxillin phosphorylation at Ser(83) and microglia chemotaxis. Glia 60:1366-1377
    • (2012) Glia , vol.60 , pp. 1366-1377
    • Lee, S.H.1    Hollingsworth, R.2    Kwon, H.Y.3
  • 73
    • 0036839745 scopus 로고    scopus 로고
    • Dancing with different partners: PKA phosphorylation of seven membrane-spanning receptors regulates their G protein coupling specificity
    • Lefkowitz RJ, Pierce KL, Luttrell LM (2002) Dancing with different partners: PKA phosphorylation of seven membrane-spanning receptors regulates their G protein coupling specificity. Mol Pharm 62:971-974
    • (2002) Mol Pharm , vol.62 , pp. 971-974
    • Lefkowitz, R.J.1    Pierce, K.L.2    Luttrell, L.M.3
  • 74
    • 0029154733 scopus 로고
    • Protein tyrosine kinase PYK2 involved in Ca(2+)-induced regulation of ion channel and MAP kinase functions
    • Lev S, Moreno H, Martinez R et al (1995) Protein tyrosine kinase PYK2 involved in Ca(2+)-induced regulation of ion channel and MAP kinase functions. Nature 376:737-745
    • (1995) Nature , vol.376 , pp. 737-745
    • Lev, S.1    Moreno, H.2    Martinez, R.3
  • 75
    • 0032540382 scopus 로고    scopus 로고
    • A calcium-dependent tyrosine kinase splice variant in human monocytes. Activation by a two-stage process involving adherence and a subsequent intracellular signal
    • Li X, Hunter D, Morris J et al (1998) A calcium-dependent tyrosine kinase splice variant in human monocytes. Activation by a two-stage process involving adherence and a subsequent intracellular signal. J Biol Chem 273:9361-9364
    • (1998) J Biol Chem , vol.273 , pp. 9361-9364
    • Li, X.1    Hunter, D.2    Morris, J.3
  • 76
    • 0030680131 scopus 로고    scopus 로고
    • Clathrin-mediated endocytosis of the betaadrenergic receptor is regulated by phosphorylation/dephosphorylation of beta-arrestin1
    • Lin FT, Krueger KM, Kendall HE et al (1997) Clathrin-mediated endocytosis of the betaadrenergic receptor is regulated by phosphorylation/ dephosphorylation of beta-arrestin1. J Biol Chem 272:31051-31057
    • (1997) J Biol Chem , vol.272 , pp. 31051-31057
    • Lin, F.T.1    Krueger, K.M.2    Kendall, H.E.3
  • 77
    • 0033522896 scopus 로고    scopus 로고
    • Feedback regulation of beta-arrestin1 function by extracellular signal-regulated kinases
    • Lin FT, Miller WE, Luttrell LM et al (1999) Feedback regulation of beta-arrestin1 function by extracellular signal-regulated kinases. J Biol Chem 274:15971-15974
    • (1999) J Biol Chem , vol.274 , pp. 15971-15974
    • Lin, F.T.1    Miller, W.E.2    Luttrell, L.M.3
  • 78
    • 0037183495 scopus 로고    scopus 로고
    • Phosphorylation of beta-arrestin2 regulates its function in internalization of beta(2)-adrenergic receptors
    • Lin FT, Chen W, Shenoy S et al (2002) Phosphorylation of beta-arrestin2 regulates its function in internalization of beta(2)-adrenergic receptors. Biochemistry 41:10692-10699
    • (2002) Biochemistry , vol.41 , pp. 10692-10699
    • Lin, F.T.1    Chen, W.2    Shenoy, S.3
  • 79
    • 0027978430 scopus 로고
    • Biochemistry of the Src protein-tyrosine kinase: Regulation by SH2 and SH3 domains
    • Liu X, Pawson T (1994) Biochemistry of the Src protein-tyrosine kinase: regulation by SH2 and SH3 domains. Recent Prog Horm Res 49:149-160
    • (1994) Recent Prog Horm Res , vol.49 , pp. 149-160
    • Liu, X.1    Pawson, T.2
  • 80
    • 0038702295 scopus 로고    scopus 로고
    • Location, Location, Location. Spatial and temporal regulation of MAP kinases by G protein-coupled receptors
    • Luttrell LM (2003) Location, Location, Location. Spatial and temporal regulation of MAP kinases by G protein-coupled receptors. J Mol Endo 30:117-126
    • (2003) J Mol Endo , vol.30 , pp. 117-126
    • Luttrell, L.M.1
  • 81
    • 77952415656 scopus 로고    scopus 로고
    • Beyond desensitization: Physiological relevance of arrestindependent signaling
    • Luttrell LM, Gesty-Palmer D (2010) Beyond desensitization: physiological relevance of arrestindependent signaling. Pharmacol Rev 62:305-330
    • (2010) Pharmacol Rev , vol.62 , pp. 305-330
    • Luttrell, L.M.1    Gesty-Palmer, D.2
  • 82
    • 80054727295 scopus 로고    scopus 로고
    • Refining efficacy: Allosterism and bias in G protein-coupled receptor signaling
    • Luttrell LM, Kenakin TP (2011) Refining efficacy: allosterism and bias in G protein-coupled receptor signaling. Methods Mol Biol 756:3-35
    • (2011) Methods Mol Biol , vol.756 , pp. 3-35
    • Luttrell, L.M.1    Kenakin, T.P.2
  • 83
    • 0036473397 scopus 로고    scopus 로고
    • The role of beta-arrestins in the termination and transduction of G-protein-coupled receptor signals
    • Luttrell LM, Lefkowitz RJ (2002) The role of beta-arrestins in the termination and transduction of G-protein-coupled receptor signals. J Cell Sci 115:455-465
    • (2002) J Cell Sci , vol.115 , pp. 455-465
    • Luttrell, L.M.1    Lefkowitz, R.J.2
  • 84
    • 7944226933 scopus 로고    scopus 로고
    • Not so strange bedfellows: G-protein-coupled receptors and Src family kinases
    • Luttrell DK, Luttrell LM (2004) Not so strange bedfellows: G-protein-coupled receptors and Src family kinases. Oncogene 23:7969-7978
    • (2004) Oncogene , vol.23 , pp. 7969-7978
    • Luttrell, D.K.1    Luttrell, L.M.2
  • 85
    • 0029778177 scopus 로고    scopus 로고
    • Role of c-Src in G protein-coupled receptor-and Gbetagamma subunit-mediated activation of mitogen activated protein kinases
    • Luttrell LM, Hawes BE, van Biesen T et al (1996) Role of c-Src in G protein-coupled receptor-and Gbetagamma subunit-mediated activation of mitogen activated protein kinases. J Biol Chem 271:19443-19450
    • (1996) J Biol Chem , vol.271 , pp. 19443-19450
    • Luttrell, L.M.1    Hawes, B.E.2    Van Biesen, T.3
  • 86
    • 0030614911 scopus 로고    scopus 로고
    • Gbetagamma subunits mediate Src-dependent phosphorylation of the epidermal growth factor receptor
    • Luttrell LM, Della Rocca GJ, Van Biesen T et al (1997) Gbetagamma subunits mediate Src-dependent phosphorylation of the epidermal growth factor receptor. J Biol Chem 272:4637-4644
    • (1997) J Biol Chem , vol.272 , pp. 4637-4644
    • Luttrell, L.M.1    Della Rocca, G.J.2    Van Biesen, T.3
  • 87
    • 0033613938 scopus 로고    scopus 로고
    • Beta-arrestin-dependent formation of beta2 adrenergic receptor-Src protein kinase complexes
    • Luttrell LM, Ferguson SS, Daaka Y et al (1999) Beta-arrestin-dependent formation of beta2 adrenergic receptor-Src protein kinase complexes. Science 283:655-661
    • (1999) Science , vol.283 , pp. 655-661
    • Luttrell, L.M.1    Ferguson, S.S.2    Daaka, Y.3
  • 88
    • 0035956983 scopus 로고    scopus 로고
    • Activation and targeting of extracellular signal-regulated kinases by beta-arrestin scaffolds
    • Luttrell LM, Roudabush FL, Choy EW et al (2001) Activation and targeting of extracellular signal-regulated kinases by beta-arrestin scaffolds. Proc Natl Acad Sci USA 98:2449-2454
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 2449-2454
    • Luttrell, L.M.1    Roudabush, F.L.2    Choy, E.W.3
  • 89
    • 84995271757 scopus 로고    scopus 로고
    • Cell motility: Complex dynamics at the leading edge. Curr Biol 7: R164-R167 Maudsley S, Martin B, Luttrell LM 2005) Perspectives in pharmacology: The origins of diversity and specificity in G protein-coupled receptor signaling
    • Machesky LM (1997) Cell motility: complex dynamics at the leading edge. Curr Biol 7: R164-R167 Maudsley S, Martin B, Luttrell LM (2005) Perspectives in pharmacology: the origins of diversity and specificity in G protein-coupled receptor signaling. J Pharmacol Exp Ther 314:485-494
    • (1997) J Pharmacol Exp Ther , vol.314 , pp. 485-494
    • MacHesky, L.M.1
  • 90
    • 0034711397 scopus 로고    scopus 로고
    • Beta-arrestin 2: A receptor-regulated MAPK scaffold for the activation of JNK3
    • McDonald PH, Chow CW, Miller WE et al (2000) Beta-arrestin 2: a receptor-regulated MAPK scaffold for the activation of JNK3. Science 290:1574-1577
    • (2000) Science , vol.290 , pp. 1574-1577
    • McDonald, P.H.1    Chow, C.W.2    Miller, W.E.3
  • 91
    • 66449088291 scopus 로고    scopus 로고
    • MEK1 binds directly to beta-arrestin1, influencing both its phosphorylation by ERK and the timing of its isoprenaline-stimulated internalization
    • Meng D, Lynch MJ, Huston E et al (2009) MEK1 binds directly to beta-arrestin1, influencing both its phosphorylation by ERK and the timing of its isoprenaline-stimulated internalization. J Biol Chem 284:11425-11435
    • (2009) J Biol Chem , vol.284 , pp. 11425-11435
    • Meng, D.1    Lynch, M.J.2    Huston, E.3
  • 92
    • 0034646687 scopus 로고    scopus 로고
    • Beta-Arrestin1 interacts with the catalytic domain of the tyrosine kinase c-SRC. Role of beta-arrestin1-dependent targeting of c-SRC in receptor endocytosis
    • Miller WE, Maudsley S, Ahn S et al (2000) Beta-Arrestin1 interacts with the catalytic domain of the tyrosine kinase c-SRC. Role of beta-arrestin1- dependent targeting of c-SRC in receptor endocytosis. J Biol Chem 275:11312-11319
    • (2000) J Biol Chem , vol.275 , pp. 11312-11319
    • Miller, W.E.1    Maudsley, S.2    Ahn, S.3
  • 93
    • 0035958940 scopus 로고    scopus 로고
    • Identification of a motif in the carboxyl terminus of beta-arrestin2 responsible for activation of JNK3
    • Miller WE, McDonald PH, Cai SF et al (2001) Identification of a motif in the carboxyl terminus of beta-arrestin2 responsible for activation of JNK3. J Biol Chem 276:27770-27777
    • (2001) J Biol Chem , vol.276 , pp. 27770-27777
    • Miller, W.E.1    McDonald, P.H.2    Cai, S.F.3
  • 94
    • 11044226761 scopus 로고    scopus 로고
    • Activation of extracellular signal-activated kinase by angiotensin II-induced Gq-independent epidermal growth factor receptor transactivation
    • Miura S, Zhang J, Matsuo Y et al (2004) Activation of extracellular signal-activated kinase by angiotensin II-induced Gq-independent epidermal growth factor receptor transactivation. Hypertens Res 27:765-770
    • (2004) Hypertens Res , vol.27 , pp. 765-770
    • Miura, S.1    Zhang, J.2    Matsuo, Y.3
  • 95
    • 49249138363 scopus 로고    scopus 로고
    • Novel role of thromboxane receptors beta isoform in bladder cancer pathogenesis
    • Mossa O, Ashton AW, Fraig M et al (2008) Novel role of thromboxane receptors beta isoform in bladder cancer pathogenesis. Cancer Res 68:4097-4104
    • (2008) Cancer Res , vol.68 , pp. 4097-4104
    • Mossa, O.1    Ashton, A.W.2    Fraig, M.3
  • 96
    • 34547104638 scopus 로고    scopus 로고
    • The active conformation of beta-arrestin1: Direct evidence for the phosphate sensor in the N-domain and conformational differences in the active states of beta-arrestins1 and-2
    • Nobles KN, Guan Z, Xiao K et al (2007) The active conformation of beta-arrestin1: direct evidence for the phosphate sensor in the N-domain and conformational differences in the active states of beta-arrestins1 and-2. J Biol Chem 282:21370-21381
    • (2007) J Biol Chem , vol.282 , pp. 21370-21381
    • Nobles, K.N.1    Guan, Z.2    Xiao, K.3
  • 97
    • 80051616441 scopus 로고    scopus 로고
    • Distinct phosphorylation sites on the ?( 2)-adrenergic receptor establish a barcode that encodes differential functions of ?-arrestin
    • Nobles KN, Xiao K, Ahn S et al (2011) Distinct phosphorylation sites on the ?(2)-adrenergic receptor establish a barcode that encodes differential functions of ?-arrestin. Sci Signal 4:51.
    • (2011) Sci Signal , vol.4 , pp. 51
    • Nobles, K.N.1    Xiao, K.2    Ahn, S.3
  • 98
    • 34848820302 scopus 로고    scopus 로고
    • Beta-arrestin-mediated beta1-adrenergic receptor transactivation of the EGFR confers cardioprotection
    • Noma T, Lemaire A, Naga Prasad SV et al 2007) Beta-arrestin-mediated beta1-adrenergic receptor transactivation of the EGFR confers cardioprotection J Clin Invest 117 2445-2458
    • (2007) J Clin Invest , vol.117 , pp. 2445-2458
    • Noma, T.1    Lemaire, A.2    Naga Prasad, S.V.3
  • 99
    • 0034595860 scopus 로고    scopus 로고
    • Differential affinities of visual arrestin, beta arrestin1, and beta arrestin2 for G protein-coupled receptors delineate two major classes of receptors
    • Oakley RH, Laporte SA, Holt JA et al (2000) Differential affinities of visual arrestin, beta arrestin1, and beta arrestin2 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    Laporte, S.A.2    Holt, J.A.3
  • 100
    • 48349131772 scopus 로고    scopus 로고
    • S-nitrosylation of beta-arrestin regulates betaadrenergic receptor trafficking
    • Ozawa K, Whalen EJ, Nelson CD et al (2008) S-nitrosylation of beta-arrestin regulates betaadrenergic receptor trafficking. Mol Cell 31:395-405
    • (2008) Mol Cell , vol.31 , pp. 395-405
    • Ozawa, K.1    Whalen, E.J.2    Nelson, C.D.3
  • 101
    • 0033605423 scopus 로고    scopus 로고
    • Internalization of the TXA2 receptor alpha and beta isoforms. Role of the differentially spliced COOH terminus in agonist-promoted receptor internalization
    • Parent JL, Labrecque P, Orsini MJ et al (1999) Internalization of the TXA2 receptor alpha and beta isoforms. Role of the differentially spliced COOH terminus in agonist-promoted receptor internalization. J Biol Chem 274:8941-8948
    • (1999) J Biol Chem , vol.274 , pp. 8941-8948
    • Parent, J.L.1    Labrecque, P.2    Orsini, M.J.3
  • 102
    • 0034997845 scopus 로고    scopus 로고
    • Mitogen-activated protein (MAP) kinase pathways: Regulation and physiologic functions
    • Pearson G, Robinson F, Beers G. T et al (2001) Mitogen-activated protein (MAP) kinase pathways: regulation and physiologic functions. Endocr Rev 22:153-183
    • (2001) Endocr Rev , vol.22 , pp. 153-183
    • Pearson, G.1    Robinson, F.2    Beers, G.T.3
  • 103
    • 0035903669 scopus 로고    scopus 로고
    • Beta-arrestin-and c-Src-dependent degradation of G-protein-coupled receptor kinase 2
    • Penela P, Elorza A, Sarnago S et al (2001) Beta-arrestin-and c-Src-dependent degradation of G-protein-coupled receptor kinase 2. EMBO J 20:5129-5138
    • (2001) EMBO J , vol.20 , pp. 5129-5138
    • Penela, P.1    Elorza, A.2    Sarnago, S.3
  • 104
    • 0035952645 scopus 로고    scopus 로고
    • New mechanisms in heptahelical receptor signaling to mitogen activated protein kinase cascades
    • Pierce KL, Luttrell LM, Lefkowitz RJ (2001a) New mechanisms in heptahelical receptor signaling to mitogen activated protein kinase cascades. Oncogene 20:1532-1539
    • (2001) Oncogene , vol.20 , pp. 1532-1539
    • Pierce, K.L.1    Luttrell, L.M.2    Lefkowitz, R.J.3
  • 105
    • 0035933814 scopus 로고    scopus 로고
    • Epidermal growth factor (EGF) receptor-dependent ERK activation by G protein-coupled receptors: A co-culture system for identifying intermediates upstream and downstream of heparin-binding EGF shedding
    • Pierce KL, Tohgo A, Ahn S et al (2001b) Epidermal growth factor (EGF) receptor-dependent ERK activation by G protein-coupled receptors: a co-culture system for identifying intermediates upstream and downstream of heparin-binding EGF shedding. J Biol Chem 276:23155-23160
    • (2001) J Biol Chem , vol.276 , pp. 23155-23160
    • Pierce, K.L.1    Tohgo, A.2    Ahn, S.3
  • 106
    • 0033521109 scopus 로고    scopus 로고
    • Feedback inhibition of G protein-coupled receptor kinase 2 (GRK2) activity by extracellular signal-regulated kinases
    • Pitcher JA, Tesmer JG, Freeman JL et al (1999) Feedback inhibition of G protein-coupled receptor kinase 2 (GRK2) activity by extracellular signal-regulated kinases. J Biol Chem 274:34531-34534
    • (1999) J Biol Chem , vol.274 , pp. 34531-34534
    • Pitcher, J.A.1    Tesmer, J.G.2    Freeman, J.L.3
  • 107
    • 0033599039 scopus 로고    scopus 로고
    • EGF receptor transactivation by G-protein-coupled receptors requires metalloproteinase cleavage of proHB-EGF
    • Prenzel N, Zwick E, Daub H et al (1999) EGF receptor transactivation by G-protein-coupled receptors requires metalloproteinase cleavage of proHB-EGF. Nature 402:884-888
    • (1999) Nature , vol.402 , pp. 884-888
    • Prenzel, N.1    Zwick, E.2    Daub, H.3
  • 108
    • 13444270337 scopus 로고    scopus 로고
    • Different G protein-coupled receptor kinases govern G protein and beta-arrestin-mediated signaling of V2 vasopressin receptor
    • Ren XR, Reiter E, Ahn S et al (2005) Different G protein-coupled receptor kinases govern G protein and beta-arrestin-mediated signaling of V2 vasopressin receptor. Proc Natl Acad Sci USA 102:1448-1453
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 1448-1453
    • Ren, X.R.1    Reiter, E.2    Ahn, S.3
  • 109
    • 0033783132 scopus 로고    scopus 로고
    • GTPase-activating proteins for heterotrimeric G proteins: Regulators of G protein signaling (RGS) and RGS-like proteins
    • Ross EM, Wilkie TM (2000) GTPase-activating proteins for heterotrimeric G proteins: regulators of G protein signaling (RGS) and RGS-like proteins. Annu Rev Biochem 69:795-827
    • (2000) Annu Rev Biochem , vol.69 , pp. 795-827
    • Ross, E.M.1    Wilkie, T.M.2
  • 110
    • 0027513982 scopus 로고
    • A mutation-induced activated state of the beta 2-adrenergic receptor. Extending the ternary complex model
    • Samama P, Cotecchia S, Costa T et al (1993) A mutation-induced activated state of the beta 2-adrenergic receptor. Extending the ternary complex model. J Biol Chem 268:4625-4636
    • (1993) J Biol Chem , vol.268 , pp. 4625-4636
    • Samama, P.1    Cotecchia, S.2    Costa, T.3
  • 111
    • 0033607513 scopus 로고    scopus 로고
    • Agonist-dependent phosphorylation of the G proteincoupled receptor kinase 2 (GRK2) by Src tyrosine kinase
    • Sarnago S, Elorza A, Mayor F Jr (1999) Agonist-dependent phosphorylation of the G proteincoupled receptor kinase 2 (GRK2) by Src tyrosine kinase. J Biol Chem 274:34411-34416
    • (1999) J Biol Chem , vol.274 , pp. 34411-34416
    • Sarnago, S.1    Elorza, A.2    Mayor Jr., F.3
  • 112
    • 0037020264 scopus 로고    scopus 로고
    • Differential nucleocytoplasmic shuttling of betaarrestins. Characterization of a leucine-rich nuclear export signal in beta-arrestin2
    • Scott MG, Le Rouzic E, Perianin A et al (2002) Differential nucleocytoplasmic shuttling of betaarrestins. Characterization of a leucine-rich nuclear export signal in beta-arrestin2. J Biol Chem 277:37693-37701
    • (2002) J Biol Chem , vol.277 , pp. 37693-37701
    • Scott, M.G.1    Le Rouzic, E.2    Perianin, A.3
  • 113
    • 33646263875 scopus 로고    scopus 로고
    • Cooperative regulation of extracellular signalregulated kinase activation and cell shape change by filamin A and beta-arrestins
    • Scott MG, Pierotti V, Storez H et al (2006) Cooperative regulation of extracellular signalregulated kinase activation and cell shape change by filamin A and beta-arrestins. Mol Cell Biol 26:3432-3445
    • (2006) Mol Cell Biol , vol.26 , pp. 3432-3445
    • Scott, M.G.1    Pierotti, V.2    Storez, H.3
  • 114
    • 80051519517 scopus 로고    scopus 로고
    • Identification of arrestin-3-specific residues necessary for JNK3 kinase activation
    • Seo J, Tsakem EL, Breitman M et al (2011) Identification of arrestin-3-specific residues necessary for JNK3 kinase activation. J Biol Chem 286:27894-27901
    • (2011) J Biol Chem , vol.286 , pp. 27894-27901
    • Seo, J.1    Tsakem, E.L.2    Breitman, M.3
  • 115
    • 0037088597 scopus 로고    scopus 로고
    • AT1 receptor mutant lacking heterotrimeric G protein coupling activates the Src-Ras-ERK pathway without nuclear translocation of ERKs
    • Seta K, Nanamori M, Modrall JG et al (2002) AT1 receptor mutant lacking heterotrimeric G protein coupling activates the Src-Ras-ERK pathway without nuclear translocation of ERKs. J Biol Chem 277:9268-9277
    • (2002) J Biol Chem , vol.277 , pp. 9268-9277
    • Seta, K.1    Nanamori, M.2    Modrall, J.G.3
  • 116
    • 34247573976 scopus 로고    scopus 로고
    • Seven-transmembrane receptors and ubiquitination
    • Shenoy SK (2007) Seven-transmembrane receptors and ubiquitination. Circ Res 100:1142-1154
    • (2007) Circ Res , vol.100 , pp. 1142-1154
    • Shenoy, S.K.1
  • 117
    • 0037737763 scopus 로고    scopus 로고
    • Trafficking pattern of beta-arrestin and G protein-coupled receptors determined by the kinetics of beta-arrestin deubiquitination
    • Shenoy SK, Lefkowitz RJ (2003) Trafficking pattern of beta-arrestin and G protein-coupled receptors determined by the kinetics of beta-arrestin deubiquitination. J Biol Chem 278:14498-14506
    • (2003) J Biol Chem , vol.278 , pp. 14498-14506
    • Shenoy, S.K.1    Lefkowitz, R.J.2
  • 118
    • 17144364766 scopus 로고    scopus 로고
    • Receptor-specific ubiquitination of beta-arrestin directs assembly and targeting of seven-transmembrane receptor signalosomes
    • Shenoy SK, Lefkowitz RJ (2005) Receptor-specific ubiquitination of beta-arrestin directs assembly and targeting of seven-transmembrane receptor signalosomes. J Biol Chem 280:15315-15324
    • (2005) J Biol Chem , vol.280 , pp. 15315-15324
    • Shenoy, S.K.1    Lefkowitz, R.J.2
  • 119
    • 0035834428 scopus 로고    scopus 로고
    • Regulation of receptor fate by ubiquitination of activated beta2-adrenergic receptor and beta-arrestin
    • Shenoy SK, McDonald PH, Kohout TA et al (2001) Regulation of receptor fate by ubiquitination of activated beta2-adrenergic receptor and beta-arrestin. Science 294:1307-1313
    • (2001) Science , vol.294 , pp. 1307-1313
    • Shenoy, S.K.1    McDonald, P.H.2    Kohout, T.A.3
  • 120
    • 33644857279 scopus 로고    scopus 로고
    • Beta-Arrestin-dependent, G protein-independent ERK1/2 activation by the beta2 adrenergic receptor
    • Shenoy SK, Drake MT, Nelson CD et al (2006) beta-Arrestin-dependent, G protein-independent ERK1/2 activation by the beta2 adrenergic receptor. J Biol Chem 281:1261-1273
    • (2006) J Biol Chem , vol.281 , pp. 1261-1273
    • Shenoy, S.K.1    Drake, M.T.2    Nelson, C.D.3
  • 121
    • 35748944113 scopus 로고    scopus 로고
    • Ubiquitination of beta-arrestin links seventransmembrane receptor endocytosis and ERK activation
    • Shenoy SK, Barak LS, Xiao K et al (2007) Ubiquitination of beta-arrestin links seventransmembrane receptor endocytosis and ERK activation. J Biol Chem 282:29549-29562
    • (2007) J Biol Chem , vol.282 , pp. 29549-29562
    • Shenoy, S.K.1    Barak, L.S.2    Xiao, K.3
  • 122
    • 52049117442 scopus 로고    scopus 로고
    • Nedd4 mediates agonist-dependent ubiquitination, lysosomal targeting, and degradation of the beta2-adrenergic receptor
    • Shenoy SK, Xiao K, Venkataramanan V et al (2008) Nedd4 mediates agonist-dependent ubiquitination, lysosomal targeting, and degradation of the beta2-adrenergic receptor. J Biol Chem 283:22166-22176
    • (2008) J Biol Chem , vol.283 , pp. 22166-22176
    • Shenoy, S.K.1    Xiao, K.2    Venkataramanan, V.3
  • 123
    • 66149116039 scopus 로고    scopus 로고
    • Beta-arrestin-dependent signaling and trafficking of 7-transmembrane receptors is reciprocally regulated by the deubiquitinase USP33 and the E3 ligase Mdm2
    • Shenoy SK, Modi AS, Shukla AK et al (2009) Beta-arrestin-dependent signaling and trafficking of 7-transmembrane receptors is reciprocally regulated by the deubiquitinase USP33 and the E3 ligase Mdm2. Proc Natl Acad Sci USA 106:6650-6655
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 6650-6655
    • Shenoy, S.K.1    Modi, A.S.2    Shukla, A.K.3
  • 124
    • 48249126790 scopus 로고    scopus 로고
    • Distinct conformational changes in beta-arrestin report biased agonism at seven-transmembrane receptors
    • Shukla AK, Violin JD, Whalen EJ et al (2008) Distinct conformational changes in beta-arrestin report biased agonism at seven-transmembrane receptors. Proc Natl Acad Sci USA 105:9988-9993
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 9988-9993
    • Shukla, A.K.1    Violin, J.D.2    Whalen, E.J.3
  • 125
    • 33746351059 scopus 로고    scopus 로고
    • Visual and both non-visual arrestins in their inactive" conformation bind JNK3 and Mdm2 and relocalize them from the nucleus to the cytoplasm
    • Song X, Raman D, Gurevich EV et al (2006) Visual and both non-visual arrestins in their "inactive" conformation bind JNK3 and Mdm2 and relocalize them from the nucleus to the cytoplasm. J Biol Chem 281:21491-21499
    • (2006) J Biol Chem , vol.281 , pp. 21491-21499
    • Song, X.1    Raman, D.2    Gurevich, E.V.3
  • 126
    • 58649095949 scopus 로고    scopus 로고
    • How does arrestin assemble MAPKs into a signaling complex?
    • Song X, Coffa S, Fu H et al (2009) How does arrestin assemble MAPKs into a signaling complex? J Biol Chem 284:685-695
    • (2009) J Biol Chem , vol.284 , pp. 685-695
    • Song, X.1    Coffa, S.2    Fu, H.3
  • 127
    • 8244240418 scopus 로고    scopus 로고
    • Targeting G protein-coupled receptor kinases to their receptor substrates
    • Stoffel RH III, Pitcher JA, Lefkowitz RJ (1997) Targeting G protein-coupled receptor kinases to their receptor substrates. J Membr Biol 157:1-8
    • (1997) J Membr Biol , vol.157 , pp. 1-8
    • Stoffel III, R.H.1    Pitcher, J.A.2    Lefkowitz, R.J.3
  • 128
    • 0028241533 scopus 로고
    • Activation of Raf as a result of recruitment to the plasma membrane
    • Stokoe D, Macdonald SG, Cadwallader K et al (1994) Activation of Raf as a result of recruitment to the plasma membrane. Science 264:1463-1467
    • (1994) Science , vol.264 , pp. 1463-1467
    • Stokoe, D.1    MacDonald, S.G.2    Cadwallader, K.3
  • 129
    • 1842856885 scopus 로고    scopus 로고
    • ERK signaling: Duration, duration, duration
    • Stork PJ (2002) ERK signaling: duration, duration, duration. Cell Cycle 1:315-317
    • (2002) Cell Cycle , vol.1 , pp. 315-317
    • Stork, P.J.1
  • 130
    • 0033527381 scopus 로고    scopus 로고
    • Pharmacological and signaling analysis of human chemokine receptor CCR-7 stably expressed in HEK-293 cells: High-affinity binding of recombinant ligands MIP-3beta and SLC stimulates multiple signaling cascades Biochem Biophys Res Commun 263 685-690 cells: High-affinity binding of recombinant ligands MIP-3beta and SLC stimulates multiple signaling cascades
    • Sullivan SK, McGrath DA, Grigoriadis D et al (1999) Pharmacological and signaling analysis of human chemokine receptor CCR-7 stably expressed in HEK-293 cells: high-affinity binding of recombinant ligands MIP-3beta and SLC stimulates multiple signaling cascades Biochem Biophys Res Commun 263 685-690 cells: high-affinity binding of recombinant ligands MIP-3beta and SLC stimulates multiple signaling cascades. Biochem Biophys Res Commun 263:685-690
    • (1999) Biochem Biophys Res Commun , vol.263 , pp. 685-690
    • Sullivan, S.K.1    McGrath, D.A.2    Grigoriadis, D.3
  • 131
    • 0029278886 scopus 로고
    • Structure-function relationships in Src family and related protein tyrosine kinases
    • Superti,Furga G Courtneidge SA (1995) Structure-function relationships in Src family and related protein tyrosine kinases. Bioessays 17:321-330
    • (1995) Bioessays , vol.17 , pp. 321-330
    • Superti, F.G.1    Courtneidge, S.A.2
  • 132
    • 84867514722 scopus 로고    scopus 로고
    • Beta-Arrestin1-mediated recruitment of c-Src underlies the proliferative action of glucagon-like peptide-1 in pancreatic ? INS832/13 cells
    • Talbot J, Joly E, Prentki M et al (2012) Beta-Arrestin1-mediated recruitment of c-Src underlies the proliferative action of glucagon-like peptide-1 in pancreatic ? INS832/13 cells. Mol Cell Endocrinol 364:65-70
    • (2012) Mol Cell Endocrinol , vol.364 , pp. 65-70
    • Talbot, J.1    Joly, E.2    Prentki, M.3
  • 133
    • 8144222927 scopus 로고    scopus 로고
    • Receptor activity-independent recruitment of beta-arrestin2 reveals specific signalling modes
    • Terrillon S, Bouvier M (2004) Receptor activity-independent recruitment of beta-arrestin2 reveals specific signalling modes. EMBO J 23:3950-3961
    • (2004) EMBO J , vol.23 , pp. 3950-3961
    • Terrillon, S.1    Bouvier, M.2
  • 134
    • 0037088585 scopus 로고    scopus 로고
    • Beta-Arrestin scaffolding of the ERK cascade enhances cytosolic ERK activity but inhibits ERK mediated transcription following angiotensin AT1a receptor stimulation
    • Tohgo A, Pierce KL, Choy EW et al (2002) beta-Arrestin scaffolding of the ERK cascade enhances cytosolic ERK activity but inhibits ERK mediated transcription following angiotensin AT1a receptor stimulation. J Biol Chem 277:9429-9436
    • (2002) J Biol Chem , vol.277 , pp. 9429-9436
    • Tohgo, A.1    Pierce, K.L.2    Choy, E.W.3
  • 135
    • 0037458614 scopus 로고    scopus 로고
    • The stability of the G protein-coupled receptorbeta-arrestin interaction determines the mechanism and functional consequence of ERK activation
    • Tohgo A, Choy EW, Gesty-Palmer D et al (2003) The stability of the G protein-coupled receptorbeta-arrestin interaction determines the mechanism and functional consequence of ERK activation. J Biol Chem 278:6258-6267
    • (2003) J Biol Chem , vol.278 , pp. 6258-6267
    • Tohgo, A.1    Choy, E.W.2    Gesty-Palmer, D.3
  • 136
    • 0028977847 scopus 로고
    • Receptor tyrosine kinase-and Gbetagammamediated MAP kinase activation by a common signalling pathway
    • Van Biesen T, Hawes BE, Luttrell DK et al (1995) Receptor tyrosine kinase-and Gbetagammamediated MAP kinase activation by a common signalling pathway. Nature 376:781-784
    • (1995) Nature , vol.376 , pp. 781-784
    • Van Biesen, T.1    Hawes, B.E.2    Luttrell, D.K.3
  • 137
    • 0030963439 scopus 로고    scopus 로고
    • CAMP activates MAP kinase and Elk-1 through a B-Raf-and Rap-1-dependent pathway
    • Vossler MR, Yao H, York RD et al (1997) cAMP activates MAP kinase and Elk-1 through a B-Raf-and Rap-1-dependent pathway. Cell 89:73-82
    • (1997) Cell , vol.89 , pp. 73-82
    • Vossler, M.R.1    Yao, H.2    York, R.D.3
  • 138
    • 31344463886 scopus 로고    scopus 로고
    • Association of beta-arrestin and TRAF6 negatively regulates Toll-like receptor-interleukin 1 receptor signaling
    • Wang Y, Tang Y, Teng L et al (2006) Association of beta-arrestin and TRAF6 negatively regulates Toll-like receptor-interleukin 1 receptor signaling. Nat Immunol 7:139-147
    • (2006) Nat Immunol , vol.7 , pp. 139-147
    • Wang, Y.1    Tang, Y.2    Teng, L.3
  • 139
    • 0141703263 scopus 로고    scopus 로고
    • Independent G protein and beta-arrestin2 mediated activation of ERK by angiotensin
    • Wei H, Ahn S, Shenoy SK et al (2003) Independent G protein and beta-arrestin2 mediated activation of ERK by angiotensin. Proc Natl Acad Sci USA 100:10782-10787
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 10782-10787
    • Wei, H.1    Ahn, S.2    Shenoy, S.K.3
  • 140
    • 0034698028 scopus 로고    scopus 로고
    • Essential role of dynamin in internalization of M2 muscarinic acetylcholine and angiotensin AT1A receptors
    • Werbonat Y, Kleutges N, Jakobs KH et al (2000) Essential role of dynamin in internalization of M2 muscarinic acetylcholine and angiotensin AT1A receptors. J Biol Chem 275:21969-21974
    • (2000) J Biol Chem , vol.275 , pp. 21969-21974
    • Werbonat, Y.1    Kleutges, N.2    Jakobs, K.H.3
  • 141
    • 79952488185 scopus 로고    scopus 로고
    • Therapeutic potential of ?-arrestin-and G proteinbiased agonists
    • Whalen EJ, Rajagopal S, Lefkowitz RJ (2011) Therapeutic potential of ?-arrestin-and G proteinbiased 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
  • 142
    • 0032508714 scopus 로고    scopus 로고
    • A mammalian scaffold complex that selectively mediates MAP kinase activation
    • Whitmarsh AJ, Cavanagh J, Tournier C et al (1998) A mammalian scaffold complex that selectively mediates MAP kinase activation. Science 281:1671-1674
    • (1998) Science , vol.281 , pp. 1671-1674
    • Whitmarsh, A.J.1    Cavanagh, J.2    Tournier, C.3
  • 143
    • 36749094552 scopus 로고    scopus 로고
    • A unique mechanism of beta-blocker action: Carvedilol stimulates beta-arrestin signaling
    • Wisler JW, DeWire SM, Whalen EJ et al (2007) A unique mechanism of beta-blocker action: carvedilol stimulates beta-arrestin signaling. Proc Natl Acad Sci USA 104:16657-16662
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 16657-16662
    • Wisler, J.W.1    Dewire, S.M.2    Whalen, E.J.3
  • 144
    • 0027772672 scopus 로고
    • Inhibition of the EGF-activated MAP kinase signaling pathway by adenosine 3',5'-monophosphate
    • Wu J, Dent P, Jelinek T et al (1993) Inhibition of the EGF-activated MAP kinase signaling pathway by adenosine 3',5'-monophosphate. Science 62:1065-1068
    • (1993) Science , vol.62 , pp. 1065-1068
    • Wu, J.1    Dent, P.2    Jelinek, T.3
  • 145
    • 11244311659 scopus 로고    scopus 로고
    • Activation-dependent conformational changes in betaarrestin 2
    • Xiao K, Shenoy SK, Nobles K et al (2004) Activation-dependent conformational changes in betaarrestin 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
  • 146
    • 77956998735 scopus 로고    scopus 로고
    • Global phosphorylation analysis of beta-arrestin-mediated signaling downstream of a seven transmembrane receptor (7TMR)
    • Xiao K, Sun J, Kim J et al (2010) Global phosphorylation analysis of beta-arrestin-mediated signaling downstream of a seven transmembrane receptor (7TMR). Proc Natl Acad Sci USA 107:15299-15304
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 15299-15304
    • Xiao, K.1    Sun, J.2    Kim, J.3
  • 147
    • 67649856866 scopus 로고    scopus 로고
    • Selective engagement of G protein coupled receptor kinases (GRKs) encodes distinct functions of biased ligands
    • Zidar DA, Violin JD, Whalen EJ et al (2009) Selective engagement of G protein coupled receptor kinases (GRKs) encodes distinct functions of biased ligands. Proc Natl Acad Sci USA 106:9649-9654
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 9649-9654
    • Zidar, D.A.1    Violin, J.D.2    Whalen, E.J.3
  • 148
    • 57049140415 scopus 로고    scopus 로고
    • C-Src-mediated phosphorylation of AP-2 reveals a general mechanism for receptors internalizing through the clathrin pathway
    • Zimmerman B, Simaan M, Lee M-H et al (2009) C-Src-mediated phosphorylation of AP-2 reveals a general mechanism for receptors internalizing through the clathrin pathway. Cell Signal 21:103-110
    • (2009) Cell Signal , vol.21 , pp. 103-110
    • Zimmerman, B.1    Simaan, M.2    Lee, M.-H.3
  • 149
    • 34547107639 scopus 로고    scopus 로고
    • Beta-arrestin-dependent regulation of the cofilin pathway downstream of protease-activated receptor-2
    • Zoudilova M, Kumar P, Ge L et al (2007) Beta-arrestin-dependent regulation of the cofilin pathway downstream of protease-activated receptor-2. J Biol Chem 282:20634-20646
    • (2007) J Biol Chem , vol.282 , pp. 20634-20646
    • Zoudilova, M.1    Kumar, P.2    Ge, L.3


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