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Volumn 112, Issue 37, 2015, Pages E5160-E5168

Receptor sequestration in response to β-arrestin-2 phosphorylation by ERK1/2 governs steady-state levels of GPCR cell-surface expression

Author keywords

Cell signaling; G protein coupled receptor; Internalization; MAPK; arrestin

Indexed keywords

ANGIOTENSIN 1 RECEPTOR; BETA ARRESTIN 2; CHEMOKINE RECEPTOR CXCR4; G PROTEIN COUPLED RECEPTOR; MITOGEN ACTIVATED PROTEIN KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE 3; PROSTAGLANDIN F RECEPTOR; PROSTAGLANDIN RECEPTOR; SERINE; THREONINE; UNCLASSIFIED DRUG; VASOPRESSIN; VASOPRESSIN TYPE 2; ARRB2 PROTEIN, HUMAN; ARRB2 PROTEIN, MOUSE; BETA ARRESTIN; LIGAND; MAPK1 PROTEIN, HUMAN; PEPTIDE; PROSTAGLANDIN F2ALPHA RECEPTOR; PROTEIN BINDING; RETINA S ANTIGEN;

EID: 84941712466     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1508836112     Document Type: Article
Times cited : (39)

References (61)
  • 1
    • 0029011218 scopus 로고
    • The MAPK signaling cascade
    • Seger R, Krebs EG (1995) The MAPK signaling cascade. FASEB J 9(9): 726-735.
    • (1995) FASEB J , vol.9 , Issue.9 , pp. 726-735
    • Seger, R.1    Krebs, E.G.2
  • 2
    • 84862294189 scopus 로고    scopus 로고
    • ERK1/2 MAP kinases: Structure, function, and regulation
    • Roskoski R, Jr (2012) ERK1/2 MAP kinases: Structure, function, and regulation. Pharmacol Res 66(2): 105-143.
    • (2012) Pharmacol Res , vol.66 , Issue.2 , pp. 105-143
    • Roskoski, R.1
  • 3
    • 0037145061 scopus 로고    scopus 로고
    • Ligand-induced, receptor-mediated dimerization and activation of EGF receptor
    • Schlessinger J (2002) Ligand-induced, receptor-mediated dimerization and activation of EGF receptor. Cell 110(6): 669-672.
    • (2002) Cell , vol.110 , Issue.6 , pp. 669-672
    • Schlessinger, J.1
  • 4
    • 34248575149 scopus 로고    scopus 로고
    • Integrating signals from RTKs to ERK/MAPK
    • McKay MM, Morrison DK (2007) Integrating signals from RTKs to ERK/MAPK. Oncogene 26(22): 3113-3121.
    • (2007) Oncogene , vol.26 , Issue.22 , pp. 3113-3121
    • McKay, M.M.1    Morrison, D.K.2
  • 5
    • 0035398487 scopus 로고    scopus 로고
    • G-protein-coupled receptors and signaling networks: Emerging paradigms
    • Marinissen MJ, Gutkind JS (2001) G-protein-coupled receptors and signaling networks: Emerging paradigms. Trends Pharmacol Sci 22(7): 368-376.
    • (2001) Trends Pharmacol Sci , vol.22 , Issue.7 , pp. 368-376
    • Marinissen, M.J.1    Gutkind, J.S.2
  • 6
    • 36448956774 scopus 로고    scopus 로고
    • GPCR-jacking: From a new route in RTK signalling to a new concept in GPCR activation
    • Delcourt N, Bockaert J, Marin P (2007) GPCR-jacking: From a new route in RTK signalling to a new concept in GPCR activation. Trends Pharmacol Sci 28(12): 602-607.
    • (2007) Trends Pharmacol Sci , vol.28 , Issue.12 , pp. 602-607
    • Delcourt, N.1    Bockaert, J.2    Marin, P.3
  • 7
    • 0027326410 scopus 로고
    • Protein kinase C alpha activates RAF-1 by direct phosphorylation
    • Kolch W, et al. (1993) Protein kinase C alpha activates RAF-1 by direct phosphorylation. Nature 364(6434): 249-252.
    • (1993) Nature , vol.364 , Issue.6434 , pp. 249-252
    • Kolch, W.1
  • 8
    • 0028670476 scopus 로고
    • Direct evidence that Gi-coupled receptor stimulation of mitogen-activated protein kinase is mediated by G beta gamma activation of p21ras
    • Koch WJ, Hawes BE, Allen LF, Lefkowitz RJ (1994) Direct evidence that Gi-coupled receptor stimulation of mitogen-activated protein kinase is mediated by G beta gamma activation of p21ras. Proc Natl Acad Sci USA 91(26): 12706-12710.
    • (1994) Proc Natl Acad Sci USA , vol.91 , Issue.26 , pp. 12706-12710
    • Koch, W.J.1    Hawes, B.E.2    Allen, L.F.3    Lefkowitz, R.J.4
  • 9
    • 0028240869 scopus 로고
    • Ras-dependent activation of MAP kinase pathway mediated by G-protein beta gamma subunits
    • Crespo P, Xu N, Simonds WF, Gutkind JS (1994) Ras-dependent activation of MAP kinase pathway mediated by G-protein beta gamma subunits. Nature 369(6479): 418-420.
    • (1994) Nature , vol.369 , Issue.6479 , pp. 418-420
    • Crespo, P.1    Xu, N.2    Simonds, W.F.3    Gutkind, J.S.4
  • 10
    • 0029154733 scopus 로고
    • Protein tyrosine kinase PYK2 involved in Ca(2+)-induced regulation of ion channel and MAP kinase functions
    • Lev S, et al. (1995) Protein tyrosine kinase PYK2 involved in Ca(2+)-induced regulation of ion channel and MAP kinase functions. Nature 376(6543): 737-745.
    • (1995) Nature , vol.376 , Issue.6543 , pp. 737-745
    • Lev, S.1
  • 11
    • 0031037296 scopus 로고    scopus 로고
    • Linkage of G protein-coupled receptors to the MAPK signaling pathway through PI 3-kinase gamma
    • Lopez-Ilasaca M, Crespo P, Pellici PG, Gutkind JS, Wetzker R (1997) Linkage of G protein-coupled receptors to the MAPK signaling pathway through PI 3-kinase gamma. Science 275(5298): 394-397.
    • (1997) Science , vol.275 , Issue.5298 , pp. 394-397
    • Lopez-Ilasaca, M.1    Crespo, P.2    Pellici, P.G.3    Gutkind, J.S.4    Wetzker, R.5
  • 12
    • 0033613938 scopus 로고    scopus 로고
    • Beta-arrestin-dependent formation of beta2 adrenergic receptor-Src protein kinase complexes
    • Luttrell LM, et al. (1999) Beta-arrestin-dependent formation of beta2 adrenergic receptor-Src protein kinase complexes. Science 283(5402): 655-661.
    • (1999) Science , vol.283 , Issue.5402 , pp. 655-661
    • Luttrell, L.M.1
  • 13
    • 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, et al. (2000) beta-arrestin-dependent endocytosis of proteinase-activated receptor 2 is required for intracellular targeting of activated ERK1/2. J Cell Biol 148(6): 1267-1281.
    • (2000) J Cell Biol , vol.148 , Issue.6 , pp. 1267-1281
    • De Fea, K.A.1
  • 14
    • 77952415656 scopus 로고    scopus 로고
    • Beyond desensitization: Physiological relevance of arrestin-dependent signaling
    • Luttrell LM, Gesty-Palmer D (2010) Beyond desensitization: Physiological relevance of arrestin-dependent signaling. Pharmacol Rev 62(2): 305-330.
    • (2010) Pharmacol Rev , vol.62 , Issue.2 , pp. 305-330
    • Luttrell, L.M.1    Gesty-Palmer, D.2
  • 15
    • 0030044360 scopus 로고    scopus 로고
    • Role of transactivation of the EGF receptor in signalling by G-protein-coupled receptors
    • Daub H, Weiss FU, Wallasch C, Ullrich A (1996) Role of transactivation of the EGF receptor in signalling by G-protein-coupled receptors. Nature 379(6565): 557-560.
    • (1996) Nature , vol.379 , Issue.6565 , pp. 557-560
    • Daub, H.1    Weiss, F.U.2    Wallasch, C.3    Ullrich, A.4
  • 16
    • 34848820302 scopus 로고    scopus 로고
    • Beta-arrestin-mediated beta1-adrenergic receptor transactivation of the EGFR confers cardioprotection
    • Noma T, et al. (2007) Beta-arrestin-mediated beta1-adrenergic receptor transactivation of the EGFR confers cardioprotection. J Clin Invest 117(9): 2445-2458.
    • (2007) J Clin Invest , vol.117 , Issue.9 , pp. 2445-2458
    • Noma, T.1
  • 17
    • 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(10): 1822-1829.
    • (2008) Cell Signal , vol.20 , Issue.10 , pp. 1822-1829
    • Galet, C.1    Ascoli, M.2
  • 18
    • 33947354585 scopus 로고    scopus 로고
    • Regulation of receptor tyrosine kinase signaling by GRKs and beta-arrestins
    • Hupfeld CJ, Olefsky JM (2007) Regulation of receptor tyrosine kinase signaling by GRKs and beta-arrestins. Annu Rev Physiol 69: 561-577.
    • (2007) Annu Rev Physiol , vol.69 , pp. 561-577
    • Hupfeld, C.J.1    Olefsky, J.M.2
  • 19
    • 0033610892 scopus 로고    scopus 로고
    • Beta-arrestins regulate mitogenic signaling and clathrin-mediated endocytosis of the insulin-like growth factor I receptor
    • Lin FT, Daaka Y, Lefkowitz RJ (1998) beta-arrestins regulate mitogenic signaling and clathrin-mediated endocytosis of the insulin-like growth factor I receptor. J Biol Chem 273(48): 31640-31643.
    • (1998) J Biol Chem , vol.273 , Issue.48 , pp. 31640-31643
    • Lin, F.T.1    Daaka, Y.2    Lefkowitz, R.J.3
  • 20
    • 84860159281 scopus 로고    scopus 로고
    • Engagement of β-arrestin by transactivated insulinlike growth factor receptor is needed for V2 vasopressin receptor-stimulated ERK1/2 activation
    • Oligny-Longpr? G, et al. (2012) Engagement of β-arrestin by transactivated insulinlike growth factor receptor is needed for V2 vasopressin receptor-stimulated ERK1/2 activation. Proc Natl Acad Sci USA 109(17): E1028-E1037.
    • (2012) Proc Natl Acad Sci USA , vol.109 , Issue.17 , pp. E1028-E1037
    • Oligny-Longpré, G.1
  • 21
    • 0035844282 scopus 로고    scopus 로고
    • Insulin and insulinlike growth factor I receptors utilize different G protein signaling components
    • Dalle S, Ricketts W, Imamura T, Vollenweider P, Olefsky JM (2001) Insulin and insulinlike growth factor I receptors utilize different G protein signaling components. J Biol Chem 276(19): 15688-15695.
    • (2001) J Biol Chem , vol.276 , Issue.19 , pp. 15688-15695
    • Dalle, S.1    Ricketts, W.2    Imamura, T.3    Vollenweider, P.4    Olefsky, J.M.5
  • 22
    • 0141564582 scopus 로고    scopus 로고
    • Melanocortin-4 receptor gene: Case-control study and transmission disequilibrium test confirm that functionally relevant mutations are compatible with a major gene effect for extreme obesity
    • Hinney A, et al. (2003) Melanocortin-4 receptor gene: Case-control study and transmission disequilibrium test confirm that functionally relevant mutations are compatible with a major gene effect for extreme obesity. J Clin Endocrinol Metab 88(9): 4258-4267.
    • (2003) J Clin Endocrinol Metab , vol.88 , Issue.9 , pp. 4258-4267
    • Hinney, A.1
  • 23
    • 0037452949 scopus 로고    scopus 로고
    • Regulation of epidermal growth factor receptor internalization by G protein-coupled receptors
    • Kim J, Ahn S, Guo R, Daaka Y (2003) Regulation of epidermal growth factor receptor internalization by G protein-coupled receptors. Biochemistry 42(10): 2887-2894.
    • (2003) Biochemistry , vol.42 , Issue.10 , pp. 2887-2894
    • Kim, J.1    Ahn, S.2    Guo, R.3    Daaka, Y.4
  • 24
    • 17144462277 scopus 로고
    • Tyrosine kinase-mediated signal transduction pathways and the actions of polypeptide growth factors and G-protein-coupled agonists in smooth muscle
    • Hollenberg MD (1995) Tyrosine kinase-mediated signal transduction pathways and the actions of polypeptide growth factors and G-protein-coupled agonists in smooth muscle. Mol Cell Biochem 149-150: 77-85.
    • (1995) Mol Cell Biochem , vol.149-150 , pp. 77-85
    • Hollenberg, M.D.1
  • 25
    • 0344812247 scopus 로고
    • Beta-adrenergic receptor kinase: Identification of a novel protein kinase that phosphorylates the agonist-occupied form of the receptor
    • Benovic JL, Strasser RH, Caron MG, Lefkowitz RJ (1986) Beta-adrenergic receptor kinase: Identification of a novel protein kinase that phosphorylates the agonist-occupied form of the receptor. Proc Natl Acad Sci USA 83(9): 2797-2801.
    • (1986) Proc Natl Acad Sci USA , vol.83 , Issue.9 , pp. 2797-2801
    • Benovic, J.L.1    Strasser, R.H.2    Caron, M.G.3    Lefkowitz, R.J.4
  • 27
    • 0023897940 scopus 로고
    • Removal of phosphorylation sites from the beta 2-adrenergic receptor delays onset of agonist-promoted desensitization
    • Bouvier M, et al. (1988) Removal of phosphorylation sites from the beta 2-adrenergic receptor delays onset of agonist-promoted desensitization. Nature 333(6171): 370-373.
    • (1988) Nature , vol.333 , Issue.6171 , pp. 370-373
    • Bouvier, M.1
  • 28
    • 0022257530 scopus 로고
    • Phosphorylation of the mammalian beta-adrenergic receptor by cyclic AMP-dependent protein kinase. Regulation of the rate of receptor phosphorylation and dephosphorylation by agonist occupancy and effects on coupling of the receptor to the stimulatory guanine nucleotide regulatory protein
    • Benovic JL, et al. (1985) Phosphorylation of the mammalian beta-adrenergic receptor by cyclic AMP-dependent protein kinase. Regulation of the rate of receptor phosphorylation and dephosphorylation by agonist occupancy and effects on coupling of the receptor to the stimulatory guanine nucleotide regulatory protein. J Biol Chem 260(11): 7094-7101.
    • (1985) J Biol Chem , vol.260 , Issue.11 , pp. 7094-7101
    • Benovic, J.L.1
  • 29
    • 0024397065 scopus 로고
    • Phosphorylation sites on two domains of the beta 2-adrenergic receptor are involved in distinct pathways of receptor desensitization
    • Hausdorff WP, et al. (1989) Phosphorylation sites on two domains of the beta 2-adrenergic receptor are involved in distinct pathways of receptor desensitization. J Biol Chem 264(21): 12657-12665.
    • (1989) J Biol Chem , vol.264 , Issue.21 , pp. 12657-12665
    • Hausdorff, W.P.1
  • 30
    • 0033522896 scopus 로고    scopus 로고
    • Feedback regulation of beta-arrestin1 function by extracellular signal-regulated kinases
    • Lin FT, MillerWE, Luttrell LM, Lefkowitz RJ (1999) Feedback regulation of beta-arrestin1 function by extracellular signal-regulated kinases. J Biol Chem 274(23): 15971-15974.
    • (1999) J Biol Chem , vol.274 , Issue.23 , pp. 15971-15974
    • Lin, F.T.1    Miller, W.E.2    Luttrell, L.M.3    Lefkowitz, R.J.4
  • 31
    • 84922020923 scopus 로고    scopus 로고
    • Differential regulation of endosomal GPCR/β-arrestin complexes and trafficking by MAPK
    • Khoury E, Nikolajev L, Simaan M, Namkung Y, Laporte SA (2014) Differential regulation of endosomal GPCR/β-arrestin complexes and trafficking by MAPK. J Biol Chem 289(34): 23302-23317.
    • (2014) J Biol Chem , vol.289 , Issue.34 , pp. 23302-23317
    • Khoury, E.1    Nikolajev, L.2    Simaan, M.3    Namkung, Y.4    Laporte, S.A.5
  • 32
    • 33748355624 scopus 로고    scopus 로고
    • Probing the activation-promoted structural rearrangements in preassembled receptor-G protein complexes
    • Galés C, et al. (2006) Probing the activation-promoted structural rearrangements in preassembled receptor-G protein complexes. Nat Struct Mol Biol 13(9): 778-786.
    • (2006) Nat Struct Mol Biol , vol.13 , Issue.9 , pp. 778-786
    • Galés, C.1
  • 33
    • 51049083138 scopus 로고    scopus 로고
    • Oncogenic MAPK signaling stimulates mTORC1 activity by promoting RSK-mediated raptor phosphorylation
    • Carrière A, et al. (2008) Oncogenic MAPK signaling stimulates mTORC1 activity by promoting RSK-mediated raptor phosphorylation. Curr Biol 18(17): 1269-1277.
    • (2008) Curr Biol , vol.18 , Issue.17 , pp. 1269-1277
    • Carrière, A.1
  • 34
    • 0016645305 scopus 로고
    • Studies on free calcium inside pigeon erythrocyte 'ghosts' by using the calcium-activated luminescent protein, obelin
    • Campbell AK, Dormer RL (1975) Studies on free calcium inside pigeon erythrocyte 'ghosts' by using the calcium-activated luminescent protein, obelin. Biochem Soc Trans 3(5): 709-711.
    • (1975) Biochem Soc Trans , vol.3 , Issue.5 , pp. 709-711
    • Campbell, A.K.1    Dormer, R.L.2
  • 35
    • 0033209897 scopus 로고    scopus 로고
    • The chemokine SDF-1alpha triggers CXCR4 receptor dimerization and activates the JAK/STAT pathway
    • Vila-Coro AJ, et al. (1999) The chemokine SDF-1alpha triggers CXCR4 receptor dimerization and activates the JAK/STAT pathway. FASEB J 13(13): 1699-1710.
    • (1999) FASEB J , vol.13 , Issue.13 , pp. 1699-1710
    • Vila-Coro, A.J.1
  • 36
    • 84891365545 scopus 로고    scopus 로고
    • Pepducin targeting the C-X-C chemokine receptor type 4 acts as a biased agonist favoring activation of the inhibitory G protein
    • Quoyer J, et al. (2013) Pepducin targeting the C-X-C chemokine receptor type 4 acts as a biased agonist favoring activation of the inhibitory G protein. Proc Natl Acad Sci USA 110(52): E5088-E5097.
    • (2013) Proc Natl Acad Sci USA , vol.110 , Issue.52 , pp. E5088-E5097
    • Quoyer, J.1
  • 37
    • 84863205849 scopus 로고    scopus 로고
    • NIH Image to ImageJ: 25 years of image analysis
    • Schneider CA, Rasband WS, Eliceiri KW (2012) NIH Image to ImageJ: 25 years of image analysis. Nat Methods 9(7): 671-675.
    • (2012) Nat Methods , vol.9 , Issue.7 , pp. 671-675
    • Schneider, C.A.1    Rasband, W.S.2    Eliceiri, K.W.3
  • 38
    • 0028568217 scopus 로고
    • Differential activation of ERK and JNK mitogen-activated protein kinases by Raf-1 and MEKK
    • Minden A, et al. (1994) Differential activation of ERK and JNK mitogen-activated protein kinases by Raf-1 and MEKK. Science 266(5191): 1719-1723.
    • (1994) Science , vol.266 , Issue.5191 , pp. 1719-1723
    • Minden, A.1
  • 39
    • 0028222136 scopus 로고
    • A requirement for extracellular signal-regulated kinase (ERK) function in the activation of AP-1 by Ha-Ras, phorbol 12-myristate 13-acetate, and serum
    • Frost JA, Geppert TD, Cobb MH, Feramisco JR (1994) A requirement for extracellular signal-regulated kinase (ERK) function in the activation of AP-1 by Ha-Ras, phorbol 12-myristate 13-acetate, and serum. Proc Natl Acad Sci USA 91(9): 3844-3848.
    • (1994) Proc Natl Acad Sci USA , vol.91 , Issue.9 , pp. 3844-3848
    • Frost, J.A.1    Geppert, T.D.2    Cobb, M.H.3    Feramisco, J.R.4
  • 40
    • 33845316454 scopus 로고    scopus 로고
    • The V2 vasopressin receptor stimulates ERK1/2 activity independently of heterotrimeric G protein signalling
    • Charest PG, Oligny-Longpré G, Bonin H, Azzi M, Bouvier M (2007) The V2 vasopressin receptor stimulates ERK1/2 activity independently of heterotrimeric G protein signalling. Cell Signal 19(1): 32-41.
    • (2007) Cell Signal , vol.19 , Issue.1 , pp. 32-41
    • Charest, P.G.1    Oligny-Longpré, G.2    Bonin, H.3    Azzi, M.4    Bouvier, M.5
  • 41
    • 0036165251 scopus 로고    scopus 로고
    • Pharmacological inhibitors of MAPK pathways
    • English JM, Cobb MH (2002) Pharmacological inhibitors of MAPK pathways. Trends Pharmacol Sci 23(1): 40-45.
    • (2002) Trends Pharmacol Sci , vol.23 , Issue.1 , pp. 40-45
    • English, J.M.1    Cobb, M.H.2
  • 42
    • 84863315292 scopus 로고    scopus 로고
    • Biasing the prostaglandin F2a receptor responses toward EGFRdependent transactivation of MAPK
    • Goupil E, et al. (2012) Biasing the prostaglandin F2a receptor responses toward EGFRdependent transactivation of MAPK. Mol Endocrinol 26(7): 1189-1202.
    • (2012) Mol Endocrinol , vol.26 , Issue.7 , pp. 1189-1202
    • Goupil, E.1
  • 43
    • 0035852697 scopus 로고    scopus 로고
    • Beta-Arrestin 1 and 2 differentially regulate heptahelical receptor signaling and trafficking
    • Kohout TA, Lin FS, Perry SJ, Conner DA, Lefkowitz RJ (2001) beta-Arrestin 1 and 2 differentially regulate heptahelical receptor signaling and trafficking. Proc Natl Acad Sci USA 98(4): 1601-1606.
    • (2001) Proc Natl Acad Sci USA , vol.98 , Issue.4 , pp. 1601-1606
    • Kohout, T.A.1    Lin, F.S.2    Perry, S.J.3    Conner, D.A.4    Lefkowitz, R.J.5
  • 44
    • 4544384577 scopus 로고    scopus 로고
    • Tumor-promoting phorbol esters and activated Ras inactivate the tuberous sclerosis tumor suppressor complex via p90 ribosomal S6 kinase
    • Roux PP, Ballif BA, Anjum R, Gygi SP, Blenis J (2004) Tumor-promoting phorbol esters and activated Ras inactivate the tuberous sclerosis tumor suppressor complex via p90 ribosomal S6 kinase. Proc Natl Acad Sci USA 101(37): 13489-13494.
    • (2004) Proc Natl Acad Sci USA , vol.101 , Issue.37 , pp. 13489-13494
    • Roux, P.P.1    Ballif, B.A.2    Anjum, R.3    Gygi, S.P.4    Blenis, J.5
  • 45
    • 84857047339 scopus 로고    scopus 로고
    • PhosphoSitePlus: A comprehensive resource for investigating the structure and function of experimentally determined post-translational modifications in man and mouse
    • (Database issue
    • Hornbeck PV, et al. (2012) PhosphoSitePlus: A comprehensive resource for investigating the structure and function of experimentally determined post-translational modifications in man and mouse. Nucleic Acids Res 40(Database issue): D261-D270.
    • (2012) Nucleic Acids Res , vol.40 , pp. D261-D270
    • Hornbeck, P.V.1
  • 47
    • 14444272052 scopus 로고    scopus 로고
    • Phorbol esters and SDF-1 induce rapid endocytosis and down modulation of the chemokine receptor CXCR4
    • Signoret N, et al. (1997) Phorbol esters and SDF-1 induce rapid endocytosis and down modulation of the chemokine receptor CXCR4. J Cell Biol 139(3): 651-664.
    • (1997) J Cell Biol , vol.139 , Issue.3 , pp. 651-664
    • Signoret, N.1
  • 48
    • 0022969314 scopus 로고
    • Activation of protein kinase C induces rapid internalization and subsequent degradation of muscarinic acetylcholine receptors in neuroblastoma cells
    • Liles WC, Hunter DD, Meier KE, Nathanson NM (1986) Activation of protein kinase C induces rapid internalization and subsequent degradation of muscarinic acetylcholine receptors in neuroblastoma cells. J Biol Chem 261(12): 5307-5313.
    • (1986) J Biol Chem , vol.261 , Issue.12 , pp. 5307-5313
    • Liles, W.C.1    Hunter, D.D.2    Meier, K.E.3    Nathanson, N.M.4
  • 49
    • 0021232137 scopus 로고
    • Phorbol ester induces desensitization of adenylate cyclase and phosphorylation of the beta-adrenergic receptor in Turkey erythrocytes
    • Kelleher DJ, Pessin JE, Ruoho AE, Johnson GL (1984) Phorbol ester induces desensitization of adenylate cyclase and phosphorylation of the beta-adrenergic receptor in turkey erythrocytes. Proc Natl Acad Sci USA 81(14): 4316-4320.
    • (1984) Proc Natl Acad Sci USA , vol.81 , Issue.14 , pp. 4316-4320
    • Kelleher, D.J.1    Pessin, J.E.2    Ruoho, A.E.3    Johnson, G.L.4
  • 51
    • 84858608294 scopus 로고    scopus 로고
    • Role of receptor-attached phosphates in binding of visual and non-visual arrestins to G protein-coupled receptors
    • Gimenez LE, et al. (2012) Role of receptor-attached phosphates in binding of visual and non-visual arrestins to G protein-coupled receptors. J Biol Chem 287(12): 9028-9040.
    • (2012) J Biol Chem , vol.287 , Issue.12 , pp. 9028-9040
    • Gimenez, L.E.1
  • 52
    • 78650943298 scopus 로고    scopus 로고
    • ERK1/2 phosphorylate Raptor to promote Ras-dependent activation of mTOR complex 1 (mTORC1
    • Carriere A, et al. (2011) ERK1/2 phosphorylate Raptor to promote Ras-dependent activation of mTOR complex 1 (mTORC1). J Biol Chem 286(1): 567-577.
    • (2011) J Biol Chem , vol.286 , Issue.1 , pp. 567-577
    • Carriere, A.1
  • 53
    • 18744376919 scopus 로고    scopus 로고
    • Real-time monitoring of receptor and G-protein interactions in living cells
    • Galés C, et al. (2005) Real-time monitoring of receptor and G-protein interactions in living cells. Nat Methods 2(3): 177-184.
    • (2005) Nat Methods , vol.2 , Issue.3 , pp. 177-184
    • Galés, C.1
  • 54
    • 77951230331 scopus 로고    scopus 로고
    • Site-specific phosphorylation of CXCR4 is dynamically regulated by multiple kinases and results in differential modulation of CXCR4 signaling
    • Busillo JM, et al. (2010) Site-specific phosphorylation of CXCR4 is dynamically regulated by multiple kinases and results in differential modulation of CXCR4 signaling. J Biol Chem 285(10): 7805-7817.
    • (2010) J Biol Chem , vol.285 , Issue.10 , pp. 7805-7817
    • Busillo, J.M.1
  • 55
    • 15444377047 scopus 로고    scopus 로고
    • Bioluminescence resonance energy transfer reveals ligand- induced conformational changes in CXCR4 homo- and heterodimers
    • Percherancier Y, et al. (2005) Bioluminescence resonance energy transfer reveals ligand- induced conformational changes in CXCR4 homo- and heterodimers. J Biol Chem 280(11): 9895-9903.
    • (2005) J Biol Chem , vol.280 , Issue.11 , pp. 9895-9903
    • Percherancier, Y.1
  • 56
    • 84894090269 scopus 로고    scopus 로고
    • Quantification of ligand bias for clinically relevant β2-adrenergic receptor ligands: Implications for drug taxonomy
    • van der Westhuizen ET, Breton B, Christopoulos A, Bouvier M(2014) Quantification of ligand bias for clinically relevant β2-adrenergic receptor ligands: Implications for drug taxonomy. Mol Pharmacol 85(3): 492-509.
    • (2014) Mol Pharmacol , vol.85 , Issue.3 , pp. 492-509
    • Van Der Westhuizen, E.T.1    Breton, B.2    Christopoulos, A.3    Bouvier, M.4
  • 57
    • 84860253205 scopus 로고    scopus 로고
    • Differential β-arrestin-dependent conformational signaling and cellular responses revealed by angiotensin analogs
    • Zimmerman B, et al. (2012) Differential β-arrestin-dependent conformational signaling and cellular responses revealed by angiotensin analogs. Sci Signal 5(221): Ra33.
    • (2012) Sci Signal , vol.5 , Issue.221 , pp. ra33
    • Zimmerman, B.1
  • 58
    • 77955478709 scopus 로고    scopus 로고
    • A novel biased allosteric compound inhibitor of parturition selectively impedes the prostaglandin F2alpha-mediated Rho/ROCK signaling pathway
    • Goupil E, et al. (2010) A novel biased allosteric compound inhibitor of parturition selectively impedes the prostaglandin F2alpha-mediated Rho/ROCK signaling pathway. J Biol Chem 285(33): 25624-25636.
    • (2010) J Biol Chem , vol.285 , Issue.33 , pp. 25624-25636
    • Goupil, E.1
  • 59
    • 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, Caron MG, Barak LS (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(22): 17201-17210.
    • (2000) J Biol Chem , vol.275 , Issue.22 , pp. 17201-17210
    • Oakley, R.H.1    Laporte, S.A.2    Holt, J.A.3    Caron, M.G.4    Barak, L.S.5
  • 60
    • 84883840386 scopus 로고
    • Quantitative studies of the growth of mouse embryo cells in culture and their development into established lines
    • Todaro GJ, Green H (1963) Quantitative studies of the growth of mouse embryo cells in culture and their development into established lines. J Cell Biol 17: 299-313.
    • (1963) J Cell Biol , vol.17 , pp. 299-313
    • Todaro, G.J.1    Green, H.2
  • 61
    • 0037160105 scopus 로고    scopus 로고
    • Quantitative assessment of beta 1- and beta 2-adrenergic receptor homo- and heterodimerization by bioluminescence resonance energy transfer
    • Mercier JF, Salahpour A, Angers S, Breit A, Bouvier M (2002) Quantitative assessment of beta 1- and beta 2-adrenergic receptor homo- and heterodimerization by bioluminescence resonance energy transfer. J Biol Chem 277(47): 44925-44931.
    • (2002) J Biol Chem , vol.277 , Issue.47 , pp. 44925-44931
    • Mercier, J.F.1    Salahpour, A.2    Angers, S.3    Breit, A.4    Bouvier, M.5


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