메뉴 건너뛰기




Volumn 6, Issue , 2015, Pages

Phospho-selective mechanisms of arrestin conformations and functions revealed by unnatural amino acid incorporation and 19 F-NMR

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; BETA ARRESTIN 1; CLATHRIN; FLUORINE; G PROTEIN COUPLED RECEPTOR; PHOSPHATE; PHOSPHOPEPTIDE; SMALL INTERFERING RNA; 3,5-DIFLUOROTYROSINE; ADRBK1 PROTEIN, HUMAN; ARRB1 PROTEIN, HUMAN; BETA ARRESTIN; G PROTEIN COUPLED RECEPTOR KINASE; G PROTEIN COUPLED RECEPTOR KINASE 2; G-PROTEIN-COUPLED RECEPTOR KINASE 6; PHOSPHATE BINDING PROTEIN; PHOSPHOPROTEIN; RETINA S ANTIGEN; TYROSINE;

EID: 84941048021     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms9202     Document Type: Article
Times cited : (159)

References (64)
  • 1
    • 84862776738 scopus 로고    scopus 로고
    • Biased signaling pathways in beta2-adrenergic receptor characterized by 19F-NMR
    • Liu, J. J., Horst, R., Katritch, V., Stevens, R. C. & Wuthrich, K. Biased signaling pathways in beta2-adrenergic receptor characterized by 19F-NMR. Science 335, 1106-1110 (2012).
    • (2012) Science , vol.335 , pp. 1106-1110
    • Liu, J.J.1    Horst, R.2    Katritch, V.3    Stevens, R.C.4    Wuthrich, K.5
  • 2
    • 84906232914 scopus 로고    scopus 로고
    • Visualization of arrestin recruitment by a G-protein-Coupled receptor
    • Shukla, A. K. et al. Visualization of arrestin recruitment by a G-protein-coupled receptor. Nature 512, 218-222 (2014).
    • (2014) Nature , vol.512 , pp. 218-222
    • Shukla, A.K.1
  • 3
    • 84900516697 scopus 로고    scopus 로고
    • Divergent transducer-specific molecular efficacies generate biased agonism at a G protein-coupled receptor (GPCR)
    • Strachan, R. T. et al. Divergent transducer-specific molecular efficacies generate biased agonism at a G protein-coupled receptor (GPCR). J. Biol. Chem. 289, 14211-14224 (2014).
    • (2014) J. Biol. Chem , vol.289 , pp. 14211-14224
    • Strachan, R.T.1
  • 4
    • 17644402459 scopus 로고    scopus 로고
    • Transduction of receptor signals by beta-arrestins
    • Lefkowitz, R. J. & Shenoy, S. K. Transduction of receptor signals by beta-arrestins. Science 308, 512-517 (2005).
    • (2005) Science , vol.308 , pp. 512-517
    • Lefkowitz, R.J.1    Shenoy, S.K.2
  • 5
    • 80051616441 scopus 로고    scopus 로고
    • Distinct phosphorylation sites on the beta(2)-adrenergic receptor establish a barcode that encodes differential functions of beta-arrestin
    • Nobles, K. N. et al. Distinct phosphorylation sites on the beta(2)-adrenergic receptor establish a barcode that encodes differential functions of beta-arrestin. Sci. Signal. 4, ra51 (2011).
    • (2011) Sci. Signal. , vol.4 , pp. 51
    • Nobles, K.N.1
  • 6
    • 80052832196 scopus 로고    scopus 로고
    • A stress response pathway regulates DNA damage through beta2-adrenoreceptors and beta-arrestin-1
    • Hara, M. R. et al. A stress response pathway regulates DNA damage through beta2-adrenoreceptors and beta-arrestin-1. Nature 477, 349-353 (2011).
    • (2011) Nature , vol.477 , pp. 349-353
    • Hara, M.R.1
  • 7
    • 77956998735 scopus 로고    scopus 로고
    • Global phosphorylation analysis of beta-arrestin-mediated signaling downstream of a seven transmembrane receptor (7TMR)
    • Xiao, K. et al. Global phosphorylation analysis of beta-arrestin-mediated signaling downstream of a seven transmembrane receptor (7TMR). Proc. Natl Acad. Sci. USA 107, 15299-15304 (2010).
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 15299-15304
    • Xiao, K.1
  • 8
    • 0029770657 scopus 로고    scopus 로고
    • Beta-arrestin acts as a clathrin adaptor in endocytosis of the beta2-adrenergic receptor
    • Goodman, Jr O. B. et al. Beta-arrestin acts as a clathrin adaptor in endocytosis of the beta2-adrenergic receptor. Nature 383, 447-450 (1996).
    • (1996) Nature , vol.383 , pp. 447-450
    • Goodman, O.B.1
  • 9
    • 0037174646 scopus 로고    scopus 로고
    • Targeting of cyclic AMP degradation to beta 2-adrenergic receptors by beta-arrestins
    • Perry, S. J. et al. Targeting of cyclic AMP degradation to beta 2-adrenergic receptors by beta-arrestins. Science 298, 834-836 (2002).
    • (2002) Science , vol.298 , pp. 834-836
    • Perry, S.J.1
  • 10
    • 22744449073 scopus 로고    scopus 로고
    • An Akt/beta-arrestin 2/PP2A signaling complex mediates dopaminergic neurotransmission and behavior
    • Beaulieu, J. M. et al. An Akt/beta-arrestin 2/PP2A signaling complex mediates dopaminergic neurotransmission and behavior. Cell 122, 261-273 (2005).
    • (2005) Cell , vol.122 , pp. 261-273
    • Beaulieu, J.M.1
  • 11
    • 84877581626 scopus 로고    scopus 로고
    • Structure of active beta-arrestin-1 bound to a G-protein-coupled receptor phosphopeptide
    • Shukla, A. K. et al. Structure of active beta-arrestin-1 bound to a G-protein-coupled receptor phosphopeptide. Nature 497, 137-141 (2013).
    • (2013) Nature , vol.497 , pp. 137-141
    • Shukla, A.K.1
  • 12
    • 34547512353 scopus 로고    scopus 로고
    • Functional specialization of beta-arrestin interactions revealed by proteomic analysis
    • Xiao, K. et al. Functional specialization of beta-arrestin interactions revealed by proteomic analysis. Proc. Natl Acad. Sci. USA 104, 12011-12016 (2007).
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 12011-12016
    • Xiao, K.1
  • 13
    • 84860201432 scopus 로고    scopus 로고
    • Structural insights into biased G protein-coupled receptor signaling revealed by fluorescence spectroscopy
    • Rahmeh, R. et al. Structural insights into biased G protein-coupled receptor signaling revealed by fluorescence spectroscopy. Proc. Natl Acad. Sci. USA 109, 6733-6738 (2012).
    • (2012) Proc. Natl Acad. Sci. USA , vol.109 , pp. 6733-6738
    • Rahmeh, R.1
  • 14
    • 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, J. M. et al. Site-specific phosphorylation of CXCR4 is dynamically regulated by multiple kinases and results in differential modulation of CXCR4 signaling. J. Biol. Chem. 285, 7805-7817 (2010).
    • (2010) J. Biol. Chem , vol.285 , pp. 7805-7817
    • Busillo, J.M.1
  • 15
    • 84903513580 scopus 로고    scopus 로고
    • Concomitant action of structural elements and receptor phosphorylation determines arrestin-3 interaction with the free fatty acid receptor FFA4
    • Butcher, A. J. et al. Concomitant action of structural elements and receptor phosphorylation determines arrestin-3 interaction with the free fatty acid receptor FFA4. J. Biol. Chem. 289, 18451-18465 (2014).
    • (2014) J. Biol. Chem , vol.289 , pp. 18451-18465
    • Butcher, A.J.1
  • 16
    • 79953192547 scopus 로고    scopus 로고
    • Differential G-protein-coupled receptor phosphorylation provides evidence for a signaling bar code
    • Butcher, A. J. et al. Differential G-protein-coupled receptor phosphorylation provides evidence for a signaling bar code. J. Biol. Chem. 286, 11506-11518 (2011).
    • (2011) J. Biol. Chem , vol.286 , pp. 11506-11518
    • Butcher, A.J.1
  • 17
    • 84899489705 scopus 로고    scopus 로고
    • Mutation of putative GRK phosphorylation sites in the cannabinoid receptor 1 (CB1R) confers resistance to cannabinoid tolerance and hypersensitivity to cannabinoids in mice
    • Morgan, D. J. et al. Mutation of putative GRK phosphorylation sites in the cannabinoid receptor 1 (CB1R) confers resistance to cannabinoid tolerance and hypersensitivity to cannabinoids in mice. J. Neurosci. 34, 5152-5163 (2014).
    • (2014) J. Neurosci , vol.34 , pp. 5152-5163
    • Morgan, D.J.1
  • 18
    • 80052678736 scopus 로고    scopus 로고
    • Role of phosphorylation in the control of clathrinmediated internalization of GPCR
    • Delom, F. & Fessart, D. Role of phosphorylation in the control of clathrinmediated internalization of GPCR. Int. J. Cell Biol. 2011, 246954 (2011).
    • (2011) Int. J. Cell Biol , vol.2011 , pp. 246954
    • Delom, F.1    Fessart, D.2
  • 19
    • 84875756632 scopus 로고    scopus 로고
    • A genetically encoded 19F NMR probe for tyrosine phosphorylation
    • Li, F. et al. A genetically encoded 19F NMR probe for tyrosine phosphorylation. Angew. Chem. Int. Ed. Engl. 52, 3958-3962 (2013).
    • (2013) Angew. Chem. Int. Ed. Engl , vol.52 , pp. 3958-3962
    • Li, F.1
  • 20
    • 77953643054 scopus 로고    scopus 로고
    • Adding new chemistries to the genetic code
    • Liu, C. C. & Schultz, P. G. Adding new chemistries to the genetic code. Annu. Rev. Biochem. 79, 413-444 (2010).
    • (2010) Annu. Rev. Biochem , vol.79 , pp. 413-444
    • Liu, C.C.1    Schultz, P.G.2
  • 21
    • 84899694169 scopus 로고    scopus 로고
    • Targeted disruption of beta-arrestin 2-mediated signaling pathways by aptamer chimeras leads to inhibition of leukemic cell growth
    • Kotula, J. W. et al. Targeted disruption of beta-arrestin 2-mediated signaling pathways by aptamer chimeras leads to inhibition of leukemic cell growth. PLoS ONE 9, e93441 (2014).
    • (2014) PLoS ONE , vol.9 , pp. e93441
    • Kotula, J.W.1
  • 22
    • 84878944044 scopus 로고    scopus 로고
    • Readout of epigenetic modifications
    • Patel, D. J. & Wang, Z. Readout of epigenetic modifications. Annu. Rev. Biochem. 82, 81-118 (2013).
    • (2013) Annu. Rev. Biochem , vol.82 , pp. 81-118
    • Patel, D.J.1    Wang, Z.2
  • 23
    • 84877581910 scopus 로고    scopus 로고
    • Crystal structure of pre-activated arrestin p44
    • Kim, Y. J. et al. Crystal structure of pre-activated arrestin p44. Nature 497, 142-146 (2013).
    • (2013) Nature , vol.497 , pp. 142-146
    • Kim, Y.J.1
  • 24
    • 13444270337 scopus 로고    scopus 로고
    • Different G protein-coupled receptor kinases govern G protein and beta-arrestin-mediated signaling of V2 vasopressin receptor
    • Ren, X. R. et al. 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).
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 1448-1453
    • Ren, X.R.1
  • 25
    • 13444291851 scopus 로고    scopus 로고
    • Functional antagonism of different G protein-coupled receptor kinases for beta-arrestin-mediated angiotensin II receptor signaling
    • Kim, J. et al. 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).
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 1442-1447
    • Kim, J.1
  • 26
    • 84867514722 scopus 로고    scopus 로고
    • Beta-Arrestin1-mediated recruitment of c-Src underlies the proliferative action of glucagon-like peptide-1 in pancreatic beta INS832/13 cells
    • Talbot, J., Joly, E., Prentki, M. & Buteau, J. beta-Arrestin1-mediated recruitment of c-Src underlies the proliferative action of glucagon-like peptide-1 in pancreatic beta INS832/13 cells. Mol. Cell. Endocrinol. 364, 65-70 (2012).
    • (2012) Mol. Cell. Endocrinol , vol.364 , pp. 65-70
    • Talbot, J.1    Joly, E.2    Prentki, M.3    Buteau, J.4
  • 27
    • 31944452649 scopus 로고    scopus 로고
    • Role of beta-arrestin 1 in the metastatic progression of colorectal cancer
    • Buchanan, F. G. et al. Role of beta-arrestin 1 in the metastatic progression of colorectal cancer. Proc. Natl Acad. Sci. USA 103, 1492-1497 (2006).
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 1492-1497
    • Buchanan, F.G.1
  • 28
    • 78650476918 scopus 로고    scopus 로고
    • Meningococcus Hijacks a beta2-adrenoceptor/beta-Arrestin pathway to cross brain microvasculature endothelium
    • Coureuil, M. et al. Meningococcus Hijacks a beta2-adrenoceptor/beta-Arrestin pathway to cross brain microvasculature endothelium. Cell 143, 1149-1160 (2010).
    • (2010) Cell , vol.143 , pp. 1149-1160
    • Coureuil, M.1
  • 29
    • 5944221106 scopus 로고    scopus 로고
    • Regulation of tyrosine kinase activation and granule release through beta-arrestin by CXCRI
    • Barlic, J. et al. Regulation of tyrosine kinase activation and granule release through beta-arrestin by CXCRI. Nat. Immunol. 1, 227-233 (2000).
    • (2000) Nat. Immunol , vol.1 , pp. 227-233
    • Barlic, J.1
  • 30
    • 0033613938 scopus 로고    scopus 로고
    • Beta-arrestin-dependent formation of beta2 adrenergic receptor-Src protein kinase complexes
    • Luttrell, L. M. et al. Beta-arrestin-dependent formation of beta2 adrenergic receptor-Src protein kinase complexes. Science 283, 655-661 (1999).
    • (1999) Science , vol.283 , pp. 655-661
    • Luttrell, L.M.1
  • 31
    • 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, K. A. et al. 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).
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 11086-11091
    • De Fea, K.A.1
  • 32
    • 33746012381 scopus 로고    scopus 로고
    • G-protein-coupled receptor kinase specificity for beta-arrestin recruitment to the beta2-adrenergic receptor revealed by fluorescence resonance energy transfer
    • Violin, J. D., Ren, X. R. & Lefkowitz, R. J. G-protein-coupled receptor kinase specificity for beta-arrestin recruitment to the beta2-adrenergic receptor revealed by fluorescence resonance energy transfer. J. Biol. Chem. 281, 20577-20588 (2006).
    • (2006) J. Biol. Chem , vol.281 , pp. 20577-20588
    • Violin, J.D.1    Ren, X.R.2    Lefkowitz, R.J.3
  • 33
    • 0842331059 scopus 로고    scopus 로고
    • The molecular acrobatics of arrestin activation
    • Gurevich, V. V. & Gurevich, E. V. The molecular acrobatics of arrestin activation. Trends Pharmacol. Sci. 25, 105-111 (2004).
    • (2004) Trends Pharmacol. Sci. , vol.25 , pp. 105-111
    • Gurevich, V.V.1    Gurevich, E.V.2
  • 34
    • 70350351401 scopus 로고    scopus 로고
    • Structure of an arrestin2-clathrin complex reveals a novel clathrin binding domain that modulates receptor trafficking
    • Kang, D. S. et al. Structure of an arrestin2-clathrin complex reveals a novel clathrin binding domain that modulates receptor trafficking. J. Biol. Chem. 284, 29860-29872 (2009).
    • (2009) J. Biol. Chem , vol.284 , pp. 29860-29872
    • Kang, D.S.1
  • 35
    • 80052967337 scopus 로고    scopus 로고
    • Multiple ligand-specific conformations of the beta2-adrenergic receptor
    • Kahsai, A. W. et al. Multiple ligand-specific conformations of the beta2-adrenergic receptor. Nat. Chem. Biol. 7, 692-700 (2011).
    • (2011) Nat. Chem. Biol , vol.7 , pp. 692-700
    • Kahsai, A.W.1
  • 36
    • 84873298278 scopus 로고    scopus 로고
    • The dynamic process of beta(2)-adrenergic receptor activation
    • Nygaard, R. et al. The dynamic process of beta(2)-adrenergic receptor activation. Cell 152, 532-542 (2013).
    • (2013) Cell , vol.152 , pp. 532-542
    • Nygaard, R.1
  • 37
    • 73849149844 scopus 로고    scopus 로고
    • Ligand-specific regulation of the extracellular surface of a G-protein-coupled receptor
    • Bokoch, M. P. et al. Ligand-specific regulation of the extracellular surface of a G-protein-coupled receptor. Nature 463, 108-112 (2010).
    • (2010) Nature , vol.463 , pp. 108-112
    • Bokoch, M.P.1
  • 38
    • 84919704267 scopus 로고    scopus 로고
    • Major ligand-induced rearrangement of the heptahelical domain interface in a GPCR dimer
    • Xue, L. et al. Major ligand-induced rearrangement of the heptahelical domain interface in a GPCR dimer. Nat. Chem. Biol. 11, 134-140 (2015).
    • (2015) Nat. Chem. Biol , vol.11 , pp. 134-140
    • Xue, L.1
  • 39
    • 84922309763 scopus 로고    scopus 로고
    • Ghrelin receptor conformational dynamics regulate the transition from a preassembled to an active receptor:Gq complex
    • Damian, M. et al. Ghrelin receptor conformational dynamics regulate the transition from a preassembled to an active receptor:Gq complex. Proc. Natl Acad. Sci. USA 112, 1601-1606 (2015).
    • (2015) Proc. Natl Acad. Sci. USA , vol.112 , pp. 1601-1606
    • Damian, M.1
  • 40
    • 84868573187 scopus 로고    scopus 로고
    • Conformation of receptor-bound visual arrestin
    • Kim, M. et al. Conformation of receptor-bound visual arrestin. Proc. Natl Acad. Sci. USA 109, 18407-18412 (2012).
    • (2012) Proc. Natl Acad. Sci. USA , vol.109 , pp. 18407-18412
    • Kim, M.1
  • 41
    • 84872529567 scopus 로고    scopus 로고
    • Involvement of distinct arrestin-1 elements in binding to different functional forms of rhodopsin
    • Zhuang, T. et al. Involvement of distinct arrestin-1 elements in binding to different functional forms of rhodopsin. Proc. Natl Acad. Sci. USA 110, 942-947 (2013).
    • (2013) Proc. Natl Acad. Sci. USA , vol.110 , pp. 942-947
    • Zhuang, T.1
  • 42
    • 17644391412 scopus 로고    scopus 로고
    • Monitoring agonist-promoted conformational changes of beta-arrestin in living cells by intramolecular BRET
    • Charest, P. G., Terrillon, S. & Bouvier, M. Monitoring agonist-promoted conformational changes of beta-arrestin in living cells by intramolecular BRET. EMBO Rep. 6, 334-340 (2005).
    • (2005) EMBO Rep , vol.6 , pp. 334-340
    • Charest, P.G.1    Terrillon, S.2    Bouvier, M.3
  • 43
    • 84916610476 scopus 로고    scopus 로고
    • Crystal structure of a common GPCR-binding interface for G protein and arrestin
    • Szczepek, M. et al. Crystal structure of a common GPCR-binding interface for G protein and arrestin. Nat. Commun. 5, 4801 (2014).
    • (2014) Nat. Commun , vol.5 , pp. 4801
    • Szczepek, M.1
  • 44
    • 0037066145 scopus 로고    scopus 로고
    • Scaffolding functions of arrestin-2 revealed by crystal structure and mutagenesis
    • Milano, S. K., Pace, H. C., Kim, Y. M., Brenner, C. & Benovic, J. L. Scaffolding functions of arrestin-2 revealed by crystal structure and mutagenesis. Biochemistry 41, 3321-3328 (2002).
    • (2002) Biochemistry , vol.41 , pp. 3321-3328
    • Milano, S.K.1    Pace, H.C.2    Kim, Y.M.3    Brenner, C.4    Benovic, J.L.5
  • 45
    • 0034802172 scopus 로고    scopus 로고
    • Crystal structure of beta-arrestin at 19A: Possible mechanism of receptor binding and membrane Translocation
    • Han, M., Gurevich, V. V., Vishnivetskiy, S. A., Sigler, P. B. & Schubert, C. Crystal structure of beta-arrestin at 1.9A: possible mechanism of receptor binding and membrane Translocation. Structure 9, 869-880 (2001).
    • (2001) Structure , vol.9 , pp. 869-880
    • Han, M.1    Gurevich, V.V.2    Vishnivetskiy, S.A.3    Sigler, P.B.4    Schubert, C.5
  • 46
    • 84925871557 scopus 로고    scopus 로고
    • Dual agonist occupancy of AT1-R-alpha2C-AR heterodimers results in atypical Gs-PKA signaling
    • Bellot, M. et al. Dual agonist occupancy of AT1-R-alpha2C-AR heterodimers results in atypical Gs-PKA signaling. Nat. Chem. Biol. 11, 271-279 (2015).
    • (2015) Nat. Chem. Biol , vol.11 , pp. 271-279
    • Bellot, M.1
  • 47
    • 33845923854 scopus 로고    scopus 로고
    • BRET analysis of GPCR oligomerization: Newer does not mean better
    • author reply 4
    • Bouvier, M., Heveker, N., Jockers, R., Marullo, S. & Milligan, G. BRET analysis of GPCR oligomerization: newer does not mean better. Nat. Methods 4, 3-4 author reply 4 (2007).
    • (2007) Nat. Methods , vol.4 , pp. 3-4
    • Bouvier, M.1    Heveker, N.2    Jockers, R.3    Marullo, S.4    Milligan, G.5
  • 48
    • 0033574274 scopus 로고    scopus 로고
    • The 28A crystal structure of visual arrestin: A model for arrestin's regulation
    • Hirsch, J. A., Schubert, C., Gurevich, V. V. & Sigler, P. B. The 2.8A crystal structure of visual arrestin: a model for arrestin's regulation. Cell 97, 257-269 (1999).
    • (1999) Cell , vol.97 , pp. 257-269
    • Hirsch, J.A.1    Schubert, C.2    Gurevich, V.V.3    Sigler, P.B.4
  • 49
    • 0033597819 scopus 로고    scopus 로고
    • Visual arrestin activity may be regulated by self-association
    • Schubert, C. et al. Visual arrestin activity may be regulated by self-association. J. Biol. Chem. 274, 21186-21190 (1999).
    • (1999) J. Biol. Chem , vol.274 , pp. 21186-21190
    • Schubert, C.1
  • 50
    • 36749103225 scopus 로고    scopus 로고
    • Beta-arrestin 2 oligomerization controls the Mdm2-dependent inhibition of p53
    • Boularan, C. et al. Beta-arrestin 2 oligomerization controls the Mdm2-dependent inhibition of p53. Proc. Natl Acad. Sci. USA 104, 18061-18066 (2007).
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 18061-18066
    • Boularan, C.1
  • 51
    • 80052038573 scopus 로고    scopus 로고
    • Beta-arrestin-mediated receptor trafficking and signal transduction
    • Shenoy, S. K. & Lefkowitz, R. J. Beta-arrestin-mediated receptor trafficking and signal transduction. Trends Pharmacol. Sci. 32, 521-533 (2011).
    • (2011) Trends Pharmacol. Sci , vol.32 , pp. 521-533
    • Shenoy, S.K.1    Lefkowitz, R.J.2
  • 52
    • 77956399106 scopus 로고    scopus 로고
    • GLP-1 inhibits and adrenaline stimulates glucagon release by differential modulation of N-and L-type Ca2\+ channel-dependent exocytosis
    • De Marinis, Y. Z. et al. GLP-1 inhibits and adrenaline stimulates glucagon release by differential modulation of N-and L-type Ca2\+ channel-dependent exocytosis. Cell Metab. 11, 543-553
    • Cell Metab , vol.11 , pp. 543-553
    • De Marinis, Y.Z.1
  • 53
    • 80052359992 scopus 로고    scopus 로고
    • Emerging paradigms of beta-arrestindependent seven transmembrane receptor signaling
    • Shukla, A. K., Xiao, K. & Lefkowitz, R. J. Emerging paradigms of beta-arrestindependent seven transmembrane receptor signaling. Trends Biochem. Sci. 36, 457-469 (2011).
    • (2011) Trends Biochem. Sci. , vol.36 , pp. 457-469
    • Shukla, A.K.1    Xiao, K.2    Lefkowitz, R.J.3
  • 54
    • 84855901533 scopus 로고    scopus 로고
    • Molecular mechanism of beta-arrestin-biased agonism at seven-transmembrane receptors
    • Reiter, E., Ahn, S., Shukla, A. K. & Lefkowitz, R. J. Molecular mechanism of beta-arrestin-biased agonism at seven-transmembrane receptors. Annu. Rev. Pharmacol. Toxicol. 52, 179-197 (2012).
    • (2012) Annu. Rev. Pharmacol. Toxicol , vol.52 , pp. 179-197
    • Reiter, E.1    Ahn, S.2    Shukla, A.K.3    Lefkowitz, R.J.4
  • 55
    • 46349099824 scopus 로고    scopus 로고
    • Structural basis for the recognition of c-Src by its inactivator Csk
    • Levinson, N. M. et al. Structural basis for the recognition of c-Src by its inactivator Csk. Cell 134, 124-134 (2008).
    • (2008) Cell , vol.134 , pp. 124-134
    • Levinson, N.M.1
  • 56
    • 38049160121 scopus 로고    scopus 로고
    • Structure, inhibitor, and regulatory mechanism of Lyp, a lymphoid-specific tyrosine phosphatase implicated in autoimmune diseases
    • Yu, X. et al. Structure, inhibitor, and regulatory mechanism of Lyp, a lymphoid-specific tyrosine phosphatase implicated in autoimmune diseases. Proc. Natl Acad. Sci. USA 104, 19767-19772 (2007).
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 19767-19772
    • Yu, X.1
  • 57
    • 48249126790 scopus 로고    scopus 로고
    • Distinct conformational changes in beta-arrestin report biased agonism at seven-transmembrane receptors
    • Shukla, A. K. et al. Distinct conformational changes in beta-arrestin report biased agonism at seven-transmembrane receptors. Proc. Natl Acad. Sci. USA 105, 9988-9993 (2008).
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , pp. 9988-9993
    • Shukla, A.K.1
  • 58
    • 17644391412 scopus 로고    scopus 로고
    • Monitoring agonist-promoted conformational changes of beta-arrestin in living cells by intramolecular BRET
    • Charest, P. G., Terrillon, S. & Bouvier, M. Monitoring agonist-promoted conformational changes of beta-arrestin in living cells by intramolecular BRET. EMBO Rep. 6, 334-340 (2005).
    • (2005) EMBO Rep , vol.6 , pp. 334-340
    • Charest, P.G.1    Terrillon, S.2    Bouvier, M.3
  • 59
    • 84863331506 scopus 로고    scopus 로고
    • Competing G protein-coupled receptor kinases balance G protein and beta-arrestin signaling
    • Heitzler, D. et al. Competing G protein-coupled receptor kinases balance G protein and beta-arrestin signaling. Mol. Syst. Biol. 8, 590 (2012).
    • (2012) Mol. Syst. Biol , vol.8 , pp. 590
    • Heitzler, D.1
  • 60
    • 11144256194 scopus 로고    scopus 로고
    • Activity-dependent internalization of smoothened mediated by beta-arrestin 2 and GRK2
    • Chen, W. et al. Activity-dependent internalization of smoothened mediated by beta-arrestin 2 and GRK2. Science 306, 2257-2260 (2004).
    • (2004) Science , vol.306 , pp. 2257-2260
    • Chen, W.1
  • 61
    • 84905579934 scopus 로고    scopus 로고
    • A stress response pathway in mice upregulates somatostatin level and transcription in pancreatic delta cells through Gs and beta-arrestin 1
    • Wang, H. M. et al. A stress response pathway in mice upregulates somatostatin level and transcription in pancreatic delta cells through Gs and beta-arrestin 1. Diabetologia 57, 1899-1910 (2014).
    • (2014) Diabetologia , vol.57 , pp. 1899-1910
    • Wang, H.M.1
  • 62
    • 85027920395 scopus 로고    scopus 로고
    • The catalytic region and PEST domain of PTPN18 distinctly regulate the HER2 phosphorylation and ubiquitination barcodes
    • Wang, H. M. et al. The catalytic region and PEST domain of PTPN18 distinctly regulate the HER2 phosphorylation and ubiquitination barcodes. Cell Res. 24, 1067-1090 (2014).
    • (2014) Cell Res , vol.24 , pp. 1067-1090
    • Wang, H.M.1
  • 63
    • 11244311659 scopus 로고    scopus 로고
    • Activation-dependent conformational changes in {beta}-arrestin 2
    • Xiao, K. et al. Activation-dependent conformational changes in {beta}-arrestin 2. J. Biol. Chem. 279, 55744-55753 (2004).
    • (2004) J. Biol. Chem , vol.279 , pp. 55744-55753
    • Xiao, K.1
  • 64
    • 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, K. N. et al. 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).
    • (2007) J. Biol. Chem , vol.282 , pp. 21370-21381
    • Nobles, K.N.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.