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Volumn 497, Issue 7447, 2013, Pages 137-141

Structure of active β-arrestin-1 bound to a G-protein-coupled receptor phosphopeptide

Author keywords

[No Author keywords available]

Indexed keywords

BETA ARRESTIN 1; G PROTEIN COUPLED RECEPTOR; PHOSPHOPEPTIDE; VASOPRESSIN V2 RECEPTOR;

EID: 84877581626     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature12120     Document Type: Article
Times cited : (364)

References (38)
  • 3
    • 0029719789 scopus 로고    scopus 로고
    • Desensitization of G protein-coupled receptors
    • discussion 352-313
    • Freedman, N. J. & Lefkowitz, R. J. Desensitization of G protein-coupled receptors. Recent Prog. Horm. Res. 51, 319-351; discussion 352-313 (1996).
    • (1996) Recent Prog. Horm. Res , vol.51 , pp. 319-351
    • Freedman, N.J.1    Lefkowitz, R.J.2
  • 4
    • 17644402459 scopus 로고    scopus 로고
    • Transduction of receptor signals by b-arrestins
    • Lefkowitz, R. J. & Shenoy, S. K. Transduction of receptor signals by b-arrestins. Science 308, 512-517 (2005).
    • (2005) Science , vol.308 , pp. 512-517
    • Lefkowitz, R.J.1    Shenoy, S.K.2
  • 5
    • 34547104638 scopus 로고    scopus 로고
    • The active conformation of b-arrestin1: Direct evidence for the phosphate sensor in the N-domain and conformational differences in the active states of b-arrestins1 and-2
    • Nobles, K. N., Guan, Z., Xiao, K., Oas, T. G. & Lefkowitz, R. J. The active conformation of b-arrestin1: direct evidence for the phosphate sensor in the N-domain and conformational differences in the active states of b-arrestins1 and-2. J. Biol. Chem. 282, 21370-21381 (2007).
    • (2007) J. Biol. Chem , vol.282 , pp. 21370-21381
    • Nobles, K.N.1    Guan, Z.2    Xiao, K.3    Oas, T.G.4    Lefkowitz, R.J.5
  • 6
    • 33646414189 scopus 로고    scopus 로고
    • The structural basis of arrestin-mediated regulationofG-protein-coupled receptors
    • Gurevich, V. V. & Gurevich, E. V. The structural basis of arrestin-mediated regulationofG-protein-coupled receptors. Pharmacol. Ther.110,465-502(2006).
    • (2006) Pharmacol. Ther , vol.110 , pp. 465-502
    • Gurevich, V.V.1    Gurevich, E.V.2
  • 7
    • 11244311659 scopus 로고    scopus 로고
    • Activation-dependent conformational changes in b-arrestin 2
    • Xiao, K., Shenoy, S. K., Nobles, K. & Lefkowitz, R. J. Activation-dependent conformational changes in b-arrestin 2. J. Biol. Chem. 279, 55744-55753 (2004).
    • (2004) J. Biol. Chem , vol.279 , pp. 55744-55753
    • Xiao, K.1    Shenoy, S.K.2    Nobles, K.3    Lefkowitz, R.J.4
  • 8
    • 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
  • 9
    • 36248970132 scopus 로고    scopus 로고
    • Crystal structure of the human b2 adrenergic G-proteincoupled receptor
    • Rasmussen, S. G. F. et al. Crystal structure of the human b2 adrenergic G-proteincoupled receptor. Nature 450, 383-387 (2007).
    • (2007) Nature , vol.450 , pp. 383-387
    • Rasmussen, S.G.F.1
  • 10
    • 78651411166 scopus 로고    scopus 로고
    • Structure of a nanobody-stabilized active state of the b2 adrenoceptor
    • Rasmussen, S. G. F. et al. Structure of a nanobody-stabilized active state of the b2 adrenoceptor. Nature 469, 175-180 (2011).
    • (2011) Nature , vol.469 , pp. 175-180
    • Rasmussen, S.G.F.1
  • 11
    • 34848848421 scopus 로고    scopus 로고
    • High-throughput generation of synthetic antibodies fromhighly functionalminimalist phage-displayed libraries
    • Fellouse, F. A. et al. High-throughput generation of synthetic antibodies fromhighly functionalminimalist phage-displayed libraries. J. Mol. Biol. 373,924-940(2007).
    • (2007) J. Mol. Biol , vol.373 , pp. 924-940
    • Fellouse, F.A.1
  • 12
    • 0033527663 scopus 로고    scopus 로고
    • Association of b-arrestin withG protein-coupled receptors during clathrin-mediated endocytosis dictates the profile of receptor resensitization
    • Oakley, R. H., Laporte, S. A., Holt, J. A., Barak, L. S. & Caron, M. G. Association of b-arrestin withG protein-coupled receptors during clathrin-mediated endocytosis dictates the profile of receptor resensitization. J. Biol. Chem. 274, 32248-32257 (1999).
    • (1999) J. Biol. Chem , vol.274 , pp. 32248-32257
    • Oakley, R.H.1    Laporte, S.A.2    Holt, J.A.3    Barak, L.S.4    Caron, M.G.5
  • 13
    • 0019137579 scopus 로고
    • A ternary complex model explains the agonist-specific binding properties of the adenylate cyclase-coupled b-adrenergic receptor
    • De Lean, A., Stadel, J. M. & Lefkowitz, R. J. A ternary complex model explains the agonist-specific binding properties of the adenylate cyclase-coupled b-adrenergic receptor. J. Biol. Chem. 255, 7108-7117 (1980).
    • (1980) J. Biol. Chem , vol.255 , pp. 7108-7117
    • De Lean, A.1    Stadel, J.M.2    Lefkowitz, R.J.3
  • 14
    • 0030664060 scopus 로고    scopus 로고
    • Agonist-receptor-arrestin, an alternative ternary complex with high agonist affinity
    • Gurevich, V. V., Pals-Rylaarsdam, R., Benovic, J. L., Hosey, M. M. & Onorato, J. J. Agonist-receptor-arrestin, an alternative ternary complex with high agonist affinity. J. Biol. Chem. 272, 28849-28852 (1997).
    • (1997) J. Biol. Chem , vol.272 , pp. 28849-28852
    • Gurevich, V.V.1    Pals-Rylaarsdam, R.2    Benovic, J.L.3    Hosey, M.M.4    Onorato, J.J.5
  • 15
    • 0034802172 scopus 로고    scopus 로고
    • Crystal structure of b-arrestin at 1.9A? : possible mechanism of receptor binding and membrane translocation
    • Han, M., Gurevich, V. V., Vishnivetskiy, S. A., Sigler, P. B. & Schubert, C. Crystal structure of b-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
  • 16
    • 33645506641 scopus 로고    scopus 로고
    • Differential interaction of spin-labeled arrestin with inactive and active phosphorhodopsin
    • Hanson, S. M. et al. Differential interaction of spin-labeled arrestin with inactive and active phosphorhodopsin. Proc. Natl Acad. Sci. USA 103, 4900-4905 (2006).
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 4900-4905
    • Hanson, S.M.1
  • 17
    • 0034731304 scopus 로고    scopus 로고
    • An additional phosphate-binding element in arrestin molecule. Implications for themechanismof arrestin activation
    • Vishnivetskiy, S. A. et al. An additional phosphate-binding element in arrestin molecule. Implications for themechanismof arrestin activation. J. Biol. Chem. 275, 41049-41057 (2000).
    • (2000) J. Biol. Chem , vol.275 , pp. 41049-41057
    • Vishnivetskiy, S.A.1
  • 18
    • 0033597328 scopus 로고    scopus 로고
    • How does arrestin respond to the phosphorylated state of rhodopsin?
    • Vishnivetskiy, S. A. et al. How does arrestin respond to the phosphorylated state of rhodopsin? J. Biol. Chem. 274, 11451-11454 (1999).
    • (1999) J. Biol. Chem , vol.274 , pp. 11451-11454
    • Vishnivetskiy, S.A.1
  • 19
    • 0025777186 scopus 로고
    • Role of the carboxyl-terminal region of arrestin in binding to phosphorylated rhodopsin
    • Palczewski, K., Buczylko, J., Imami, N. R., McDowell, J. H. & Hargrave, P. A. Role of the carboxyl-terminal region of arrestin in binding to phosphorylated rhodopsin. J. Biol. Chem. 266, 15334-15339 (1991).
    • (1991) J. Biol. Chem , vol.266 , pp. 15334-15339
    • Palczewski, K.1    Buczylko, J.2    Imami, N.R.3    McDowell, J.H.4    Hargrave, P.A.5
  • 20
    • 0029770657 scopus 로고    scopus 로고
    • B-arrestin acts as a clathrin adaptor in endocytosis of the b2-adrenergic receptor
    • Goodman, O. B. Jr et al. b-arrestin acts as a clathrin adaptor in endocytosis of the b2-adrenergic receptor. Nature 383, 447-450 (1996).
    • (1996) Nature , vol.383 , pp. 447-450
    • Goodman Jr., O.B.1
  • 21
    • 0033548433 scopus 로고    scopus 로고
    • Targeted construction of phosphorylation-independent beta-arrestin mutants with constitutive activity in cells
    • Kovoor, A., Celver, J., Abdryashitov, R. I., Chavkin, C. & Gurevich, V. V. Targeted construction of phosphorylation-independent beta-arrestin mutants with constitutive activity in cells. J. Biol. Chem. 274, 6831-6834 (1999).
    • (1999) J. Biol. Chem , vol.274 , pp. 6831-6834
    • Kovoor, A.1    Celver, J.2    Abdryashitov, R.I.3    Chavkin, C.4    Gurevich, V.V.5
  • 22
    • 0037113983 scopus 로고    scopus 로고
    • Transition of arrestin into the active receptor-binding state requires an extended interdomain hinge
    • Vishnivetskiy, S. A., Hirsch, J. A., Velez, M. G., Gurevich, Y. V. & Gurevich, V. V. Transition of arrestin into the active receptor-binding state requires an extended interdomain hinge. J. Biol. Chem. 277, 43961-43967 (2002).
    • (2002) J. Biol. Chem , vol.277 , pp. 43961-43967
    • Vishnivetskiy, S.A.1    Hirsch, J.A.2    Velez, M.G.3    Gurevich, Y.V.4    Gurevich, V.V.5
  • 23
    • 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
  • 24
    • 34547512353 scopus 로고    scopus 로고
    • Functional specialization of b-arrestin interactions revealed by proteomic analysis
    • Xiao, K. et al. Functional specialization of b-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
  • 25
    • 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
  • 26
    • 84866102271 scopus 로고    scopus 로고
    • Distinct loops in arrestin differentially regulate ligand binding within the GPCR opsin
    • Sommer, M. E., Hofmann, K. P. & Heck, M. Distinct loops in arrestin differentially regulate ligand binding within the GPCR opsin. Nature Commun. 3, 995 (2012).
    • (2012) Nature Commun , vol.3 , pp. 995
    • Sommer, M.E.1    Hofmann, K.P.2    Heck, M.3
  • 27
    • 79953779607 scopus 로고    scopus 로고
    • Allosteric control of ligand-binding affinity using engineered conformation-specific effector proteins
    • Rizk, S. S. et al. Allosteric control of ligand-binding affinity using engineered conformation-specific effector proteins. Nature Struct. Mol. Biol. 18, 437-442 (2011).
    • (2011) Nature Struct. Mol. Biol , vol.18 , pp. 437-442
    • Rizk, S.S.1
  • 28
    • 0028809411 scopus 로고
    • Amino and carboxyl terminal modifications to facilitate the production and purification of a G protein-coupled receptor
    • Kobilka, B. K. Amino and carboxyl terminal modifications to facilitate the production and purification of a G protein-coupled receptor. Anal. Biochem. 231, 269-271 (1995).
    • (1995) Anal. Biochem , vol.231 , pp. 269-271
    • Kobilka, B.K.1
  • 29
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z. & Minor, W. Processing of X-ray diffraction data collected in oscillation mode. Macromol. Crystallogr. A 276, 307-326 (1997).
    • (1997) Macromol. Crystallogr. A , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 30
    • 34447508216 scopus 로고    scopus 로고
    • Phaser crystallographic software
    • McCoy, A. J. et al.Phaser crystallographic software. J.Appl. Crystallogr.40, 658-674 (2007).
    • (2007) J.Appl. Crystallogr , vol.40 , pp. 658-674
    • McCoy, A.J.1
  • 31
    • 66149127336 scopus 로고    scopus 로고
    • Crystal structure of full-length KcsA in its closed conformation
    • Uysal, S. et al. Crystal structure of full-length KcsA in its closed conformation. Proc. Natl Acad. Sci. USA 106, 6644-6649 (2009).
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 6644-6649
    • Uysal, S.1
  • 32
    • 0037066145 scopus 로고    scopus 로고
    • Scaffoldingfunctions of arrestin-2 revealed by crystal structure and mutagenesis
    • Milano, S. K., Pace, H. C., Kim,Y. M., Brenner, C.&Benovic, J. L.Scaffoldingfunctions 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
  • 33
    • 13244281317 scopus 로고    scopus 로고
    • Coot: Model-building tools for molecular graphics
    • Emsley, P. & Cowtan, K. Coot: model-building tools for molecular graphics. Acta Crystallogr. D 60, 2126-2132 (2004).
    • (2004) Acta Crystallogr. D , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 34
    • 24644451703 scopus 로고    scopus 로고
    • A robust bulk-solvent correction and anisotropic scaling procedure
    • Afonine, P. V., Grosse-Kunstleve, R. W. & Adams, P. D. A robust bulk-solvent correction and anisotropic scaling procedure. Acta Crystallogr. D 61, 850-855 (2005).
    • (2005) Acta Crystallogr. D , vol.61 , pp. 850-855
    • Afonine, P.V.1    Grosse-Kunstleve, R.W.2    Adams, P.D.3
  • 35
    • 74549178560 scopus 로고    scopus 로고
    • MolProbity: All-atom structure validation for macromolecular crystallography
    • Chen, V. B. et al. MolProbity: all-atom structure validation for macromolecular crystallography. Acta Crystallogr. D 66, 12-21 (2010).
    • (2010) Acta Crystallogr. D , vol.66 , pp. 12-21
    • Chen, V.B.1
  • 37
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch, W. & Sander, C. Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 22, 2577-2637 (1983).
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 38
    • 0030888546 scopus 로고    scopus 로고
    • Model-free methods of analyzing domain motions in proteins from simulation: A comparison of normal mode analysis and molecular dynamics simulation of lysozyme
    • CrossRef
    • Hayward, S., Kitao, A. & Berendsen, H. J. Model-free methods of analyzing domain motions in proteins from simulation: a comparison of normal mode analysis and molecular dynamics simulation of lysozyme. Proteins 27, 425-437 (1997) CrossRef.
    • (1997) Proteins , vol.27 , pp. 425-437
    • Hayward, S.1    Kitao, A.2    Berendsen, H.J.3


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