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Volumn 111, Issue 5, 2014, Pages 1825-1830

Functional map of arrestin-1 at single amino acid resolution

Author keywords

Cell signaling; Membrane receptor; Protein engineering; Scanning mutagenesis; Visual system

Indexed keywords

AMINO ACID; ARGININE; ASPARTIC ACID; BETA ARRESTIN 1; G PROTEIN COUPLED RECEPTOR; GLUTAMINE; GLYCINE; LYSINE; METHIONINE; MUTANT PROTEIN; PHENYLALANINE; PHOSPHATE; PHOSPHOPEPTIDE; PROTEIN P44; RHODOPSIN; SERINE; TRYPTOPHAN;

EID: 84893440910     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1319402111     Document Type: Article
Times cited : (55)

References (51)
  • 1
    • 80052082999 scopus 로고    scopus 로고
    • Structural insights into agonist-induced activation of Gprotein-coupled receptors
    • Deupi X, Standfuss J (2011) Structural insights into agonist-induced activation of Gprotein-coupled receptors. Curr Opin Struct Biol 21(4):541-551.
    • (2011) Curr Opin Struct Biol , vol.21 , Issue.4 , pp. 541-551
    • Deupi, X.1    Standfuss, J.2
  • 2
    • 17644402459 scopus 로고    scopus 로고
    • Transduction of receptor signals by beta-arrestins
    • Lefkowitz RJ, Shenoy SK (2005) Transduction of receptor signals by beta-arrestins. Science 308(5721):512-517.
    • (2005) Science , vol.308 , Issue.5721 , pp. 512-517
    • Lefkowitz, R.J.1    Shenoy, S.K.2
  • 3
    • 79953242234 scopus 로고    scopus 로고
    • The structural basis of agonist-induced activation in constitutively active rhodopsin
    • Standfuss J, et al. (2011) The structural basis of agonist-induced activation in constitutively active rhodopsin. Nature 471(7340):656-660.
    • (2011) Nature , vol.471 , Issue.7340 , pp. 656-660
    • Standfuss, J.1
  • 4
    • 84855990615 scopus 로고    scopus 로고
    • Stabilized G protein binding site in the structure of constitutively active metarhodopsin-II
    • Deupi X, et al. (2012) Stabilized G protein binding site in the structure of constitutively active metarhodopsin-II. Proc Natl Acad Sci USA 109(1):119-124.
    • (2012) Proc Natl Acad Sci USA , vol.109 , Issue.1 , pp. 119-124
    • Deupi, X.1
  • 5
    • 79953234218 scopus 로고    scopus 로고
    • Crystal structure of metarhodopsin II
    • Choe H-W, et al. (2011) Crystal structure of metarhodopsin II. Nature 471(7340): 651-655.
    • (2011) Nature , vol.471 , Issue.7340 , pp. 651-655
    • Choe, H.-W.1
  • 6
    • 80051658642 scopus 로고    scopus 로고
    • Crystal structure of the β2 adrenergic receptor-Gs protein complex
    • Rasmussen SG, et al. (2011) Crystal structure of the β2 adrenergic receptor-Gs protein complex. Nature 477(7366):549-555.
    • (2011) Nature , vol.477 , Issue.7366 , pp. 549-555
    • Rasmussen, S.G.1
  • 7
    • 0032568021 scopus 로고    scopus 로고
    • X-ray crystal structure of arrestin from bovine rod outer segments
    • Granzin J, et al. (1998) X-ray crystal structure of arrestin from bovine rod outer segments. Nature 391(6670):918-921.
    • (1998) Nature , vol.391 , Issue.6670 , pp. 918-921
    • Granzin, J.1
  • 8
    • 0033574274 scopus 로고    scopus 로고
    • The 2. 8 A crystal structure of visual arrestin: A model for arrestin's regulation
    • Hirsch JA, Schubert C, Gurevich VV, Sigler PB (1999) The 2.8 A crystal structure of visual arrestin: A model for arrestin's regulation. Cell 97(2):257-269.
    • (1999) Cell , vol.97 , Issue.2 , pp. 257-269
    • Hirsch, J.A.1    Schubert, C.2    Gurevich, V.V.3    Sigler, P.B.4
  • 9
    • 84877581910 scopus 로고    scopus 로고
    • Crystal structure of pre-activated arrestin p44
    • Kim YJ, et al. (2013) Crystal structure of pre-activated arrestin p44. Nature 497(7447): 142-146.
    • (2013) Nature , vol.497 , Issue.7447 , pp. 142-146
    • Kim, Y.J.1
  • 10
    • 84877581626 scopus 로고    scopus 로고
    • Structure of active β-arrestin-1 bound to a G-protein-coupled receptor phosphopeptide
    • Shukla AK, et al. (2013) Structure of active β-arrestin-1 bound to a G-protein-coupled receptor phosphopeptide. Nature 497(7447):137-141.
    • (2013) Nature , vol.497 , Issue.7447 , pp. 137-141
    • Shukla, A.K.1
  • 11
    • 0034528629 scopus 로고    scopus 로고
    • Interactions of metarhodopsin II. Arrestin peptides compete with arrestin and transducin
    • Pulvermüller A, Schroder K, Fischer T, Hofmann KP (2000) Interactions of metarhodopsin II. Arrestin peptides compete with arrestin and transducin. J Biol Chem 275(48):37679-37685.
    • (2000) J Biol Chem , vol.275 , Issue.48 , pp. 37679-37685
    • Pulvermüller, A.1    Schroder, K.2    Fischer, T.3    Hofmann, K.P.4
  • 14
    • 84865436871 scopus 로고    scopus 로고
    • A crystal clear solution for determining G-protein-coupled receptor structures
    • Tate CG (2012) A crystal clear solution for determining G-protein-coupled receptor structures. Trends Biochem Sci 37(9):343-352.
    • (2012) Trends Biochem Sci , vol.37 , Issue.9 , pp. 343-352
    • Tate, C.G.1
  • 15
    • 0024403619 scopus 로고
    • High-resolution epitope mapping of hGH-receptor interactions by alanine-scanning mutagenesis
    • Cunningham BC, Wells JA (1989) High-resolution epitope mapping of hGH-receptor interactions by alanine-scanning mutagenesis. Science 244(4908):1081-1085.
    • (1989) Science , vol.244 , Issue.4908 , pp. 1081-1085
    • Cunningham, B.C.1    Wells, J.A.2
  • 16
    • 84893451465 scopus 로고    scopus 로고
    • AAscan, PCRdesign and MutantChecker: A Suite of Programs for Primer Design and Sequence Analysis for High-Throughput Scanning Mutagenesis
    • Sun D, et al. (2013) AAscan, PCRdesign and MutantChecker: A Suite of Programs for Primer Design and Sequence Analysis for High-Throughput Scanning Mutagenesis. PLoS ONE 8(10):e78878.
    • (2013) PLoS ONE , vol.8 , Issue.10
    • Sun, D.1
  • 17
    • 0027241013 scopus 로고
    • Visual arrestin interaction with rhodopsin. Sequential multisite binding ensures strict selectivity toward light-activated phosphorylated rhodopsin
    • Gurevich VV, Benovic JL (1993) Visual arrestin interaction with rhodopsin. Sequential multisite binding ensures strict selectivity toward light-activated phosphorylated rhodopsin. J Biol Chem 268(16):11628-11638.
    • (1993) J Biol Chem , vol.268 , Issue.16 , pp. 11628-11638
    • Gurevich, V.V.1    Benovic, J.L.2
  • 18
    • 84866102271 scopus 로고    scopus 로고
    • Distinct loops in arrestin differentially regulate ligand binding within the GPCR opsin
    • Sommer ME, Hofmann KP, Heck M (2012) Distinct loops in arrestin differentially regulate ligand binding within the GPCR opsin. Nat Commun 3:995.
    • (2012) Nat Commun , vol.3 , pp. 995
    • Sommer, M.E.1    Hofmann, K.P.2    Heck, M.3
  • 19
    • 78651390998 scopus 로고    scopus 로고
    • Monomeric rhodopsin is sufficient for normal rhodopsin kinase (GRK1) phosphorylation and arrestin-1 binding
    • Bayburt TH, et al. (2011) Monomeric rhodopsin is sufficient for normal rhodopsin kinase (GRK1) phosphorylation and arrestin-1 binding. J Biol Chem 286(2):1420-1428.
    • (2011) J Biol Chem , vol.286 , Issue.2 , pp. 1420-1428
    • Bayburt, T.H.1
  • 20
    • 84872529567 scopus 로고    scopus 로고
    • Involvement of distinct arrestin-1 elements in binding to different functional forms of rhodopsin
    • Zhuang T, et al. (2013) Involvement of distinct arrestin-1 elements in binding to different functional forms of rhodopsin. Proc Natl Acad Sci USA 110(3):942-947.
    • (2013) Proc Natl Acad Sci USA , vol.110 , Issue.3 , pp. 942-947
    • Zhuang, T.1
  • 21
    • 0033597328 scopus 로고    scopus 로고
    • How does arrestin respond to the phosphorylated state of rhodopsin?
    • Vishnivetskiy SA, et al. (1999) How does arrestin respond to the phosphorylated state of rhodopsin? J Biol Chem 274(17):11451-11454.
    • (1999) J Biol Chem , vol.274 , Issue.17 , pp. 11451-11454
    • Vishnivetskiy, S.A.1
  • 22
    • 0032546975 scopus 로고    scopus 로고
    • The selectivity of visual arrestin for light-activated phosphorhodopsin is controlled by multiple nonredundant mechanisms
    • Gurevich VV (1998) The selectivity of visual arrestin for light-activated phosphorhodopsin is controlled by multiple nonredundant mechanisms. J Biol Chem 273(25): 15501-15506.
    • (1998) J Biol Chem , vol.273 , Issue.25 , pp. 15501-15506
    • Gurevich, V.V.1
  • 23
    • 0025777186 scopus 로고
    • Role of the carboxyl-terminal region of arrestin in binding to phosphorylated rhodopsin
    • Palczewski K, Buczyłko J, Imami NR, McDowell JH, Hargrave PA (1991) Role of the carboxyl-terminal region of arrestin in binding to phosphorylated rhodopsin. J Biol Chem 266(23):15334-15339.
    • (1991) J Biol Chem , vol.266 , Issue.23 , pp. 15334-15339
    • Palczewski, K.1    Buczyłko, J.2    Imami, N.R.3    McDowell, J.H.4    Hargrave, P.A.5
  • 24
    • 33645506641 scopus 로고    scopus 로고
    • Differential interaction of spin-labeled arrestin with inactive and active phosphorhodopsin
    • Hanson SM, et al. (2006) Differential interaction of spin-labeled arrestin with inactive and active phosphorhodopsin. Proc Natl Acad Sci USA 103(13):4900-4905.
    • (2006) Proc Natl Acad Sci USA , vol.103 , Issue.13 , pp. 4900-4905
    • Hanson, S.M.1
  • 25
    • 84857585707 scopus 로고    scopus 로고
    • Crystal structure of p44, a constitutively active splice variant of visual arrestin
    • Granzin J, et al. (2012) Crystal structure of p44, a constitutively active splice variant of visual arrestin. J Mol Biol 416(5):611-618.
    • (2012) J Mol Biol , vol.416 , Issue.5 , pp. 611-618
    • Granzin, J.1
  • 26
    • 0037113983 scopus 로고    scopus 로고
    • Transition of arrestin into the active receptor-binding state requires an extended interdomain hinge
    • Vishnivetskiy SA, Hirsch JA, Velez M-G, Gurevich YV, Gurevich VV (2002) Transition of arrestin into the active receptor-binding state requires an extended interdomain hinge. J Biol Chem 277(46):43961-43967.
    • (2002) J Biol Chem , vol.277 , Issue.46 , pp. 43961-43967
    • Vishnivetskiy, S.A.1    Hirsch, J.A.2    Velez, M.-G.3    Gurevich, Y.V.4    Gurevich, V.V.5
  • 28
    • 84868573187 scopus 로고    scopus 로고
    • Conformation of receptor-bound visual arrestin
    • Kim M, et al. (2012) Conformation of receptor-bound visual arrestin. Proc Natl Acad Sci USA 109(45):18407-18412.
    • (2012) Proc Natl Acad Sci USA , vol.109 , Issue.45 , pp. 18407-18412
    • Kim, M.1
  • 29
    • 84876911193 scopus 로고    scopus 로고
    • Critical role of the central 139-loop in stability and binding selectivity of arrestin-1
    • Vishnivetskiy SA, Baameur F, Findley KR, Gurevich VV (2013) Critical role of the central 139-loop in stability and binding selectivity of arrestin-1. J Biol Chem 288(17):11741-11750.
    • (2013) J Biol Chem , vol.288 , Issue.17 , pp. 11741-11750
    • Vishnivetskiy, S.A.1    Baameur, F.2    Findley, K.R.3    Gurevich, V.V.4
  • 30
    • 70449591430 scopus 로고    scopus 로고
    • Helix formation in arrestin accompanies recognition of photoactivated rhodopsin
    • Feuerstein SE, et al. (2009) Helix formation in arrestin accompanies recognition of photoactivated rhodopsin. Biochemistry 48(45):10733-10742.
    • (2009) Biochemistry , vol.48 , Issue.45 , pp. 10733-10742
    • Feuerstein, S.E.1
  • 31
    • 34548490297 scopus 로고    scopus 로고
    • Dynamics of arrestin-rhodopsin interactions: Loop movement is involved in arrestin activation and receptor binding
    • Sommer ME, Farrens DL, McDowell JH, Weber LA, Smith WC (2007) Dynamics of arrestin-rhodopsin interactions: Loop movement is involved in arrestin activation and receptor binding. J Biol Chem 282(35):25560-25568.
    • (2007) J Biol Chem , vol.282 , Issue.35 , pp. 25560-25568
    • Sommer, M.E.1    Farrens, D.L.2    McDowell, J.H.3    Weber, L.A.4    Smith, W.C.5
  • 32
    • 33847607436 scopus 로고    scopus 로고
    • Each rhodopsin molecule binds its own arrestin
    • Hanson SM, et al. (2007) Each rhodopsin molecule binds its own arrestin. Proc Natl Acad Sci USA 104(9):3125-3128.
    • (2007) Proc Natl Acad Sci USA , vol.104 , Issue.9 , pp. 3125-3128
    • Hanson, S.M.1
  • 33
    • 77954760056 scopus 로고    scopus 로고
    • Monomeric rhodopsin is the minimal functional unit required for arrestin binding
    • Tsukamoto H, Sinha A, DeWitt M, Farrens DL (2010) Monomeric rhodopsin is the minimal functional unit required for arrestin binding. J Mol Biol 399(3):501-511.
    • (2010) J Mol Biol , vol.399 , Issue.3 , pp. 501-511
    • Tsukamoto, H.1    Sinha, A.2    Dewitt, M.3    Farrens, D.L.4
  • 34
    • 52949102889 scopus 로고    scopus 로고
    • Crystal structure of opsin in its G-protein-interacting conformation
    • Scheerer P, et al. (2008) Crystal structure of opsin in its G-protein-interacting conformation. Nature 455(7212):497-502.
    • (2008) Nature , vol.455 , Issue.7212 , pp. 497-502
    • Scheerer, P.1
  • 35
    • 34548861782 scopus 로고    scopus 로고
    • Protein-protein docking with backbone flexibility
    • Wang C, Bradley P, Baker D (2007) Protein-protein docking with backbone flexibility. J Mol Biol 373(2):503-519.
    • (2007) J Mol Biol , vol.373 , Issue.2 , pp. 503-519
    • Wang, C.1    Bradley, P.2    Baker, D.3
  • 36
    • 84862776738 scopus 로고    scopus 로고
    • Biased signaling pathways in β2-adrenergic receptor characterized by 19F-NMR
    • Liu JJ, Horst R, Katritch V, Stevens RC, Wüthrich K (2012) Biased signaling pathways in β2-adrenergic receptor characterized by 19F-NMR. Science 335(6072):1106-1110.
    • (2012) Science , vol.335 , Issue.6072 , pp. 1106-1110
    • Liu, J.J.1    Horst, R.2    Katritch, V.3    Stevens, R.C.4    Wüthrich, K.5
  • 37
    • 81755187017 scopus 로고    scopus 로고
    • Conformational dynamics of helix 8 in the GPCR rhodopsin controls arrestin activation in the desensitization process
    • Kirchberg K, et al. (2011) Conformational dynamics of helix 8 in the GPCR rhodopsin controls arrestin activation in the desensitization process. Proc Natl Acad Sci USA 108(46):18690-18695.
    • (2011) Proc Natl Acad Sci USA , vol.108 , Issue.46 , pp. 18690-18695
    • Kirchberg, K.1
  • 38
    • 84878582491 scopus 로고    scopus 로고
    • Insights into congenital stationary night blindness based on the structure of G90D rhodopsin
    • Singhal A, et al. (2013) Insights into congenital stationary night blindness based on the structure of G90D rhodopsin. EMBO Rep 14(6):520-526.
    • (2013) EMBO Rep , vol.14 , Issue.6 , pp. 520-526
    • Singhal, A.1
  • 39
    • 84881111811 scopus 로고    scopus 로고
    • Constitutively active rhodopsin mutants causing night blindness are effectively phosphorylated by GRKs but differ in arrestin-1 binding
    • Vishnivetskiy SA, et al. (2013) Constitutively active rhodopsin mutants causing night blindness are effectively phosphorylated by GRKs but differ in arrestin-1 binding. Cell Signal 25(11):2155-2162.
    • (2013) Cell Signal , vol.25 , Issue.11 , pp. 2155-2162
    • Vishnivetskiy, S.A.1
  • 40
    • 33947577189 scopus 로고    scopus 로고
    • Structure and function of the visual arrestin oligomer
    • Hanson SM, et al. (2007) Structure and function of the visual arrestin oligomer. EMBO J 26(6):1726-1736.
    • (2007) EMBO J , vol.26 , Issue.6 , pp. 1726-1736
    • Hanson, S.M.1
  • 41
    • 44649193852 scopus 로고    scopus 로고
    • A model for the solution structure of the rod arrestin tetramer
    • Hanson SM, et al. (2008) A model for the solution structure of the rod arrestin tetramer. Structure 16(6):924-934.
    • (2008) Structure , vol.16 , Issue.6 , pp. 924-934
    • Hanson, S.M.1
  • 42
    • 79953213342 scopus 로고    scopus 로고
    • Arrestin-rhodopsin binding stoichiometry in isolated rod outer segment membranes depends on the percentage of activated receptors
    • Sommer ME, Hofmann KP, Heck MM (2011) Arrestin-rhodopsin binding stoichiometry in isolated rod outer segment membranes depends on the percentage of activated receptors. J Biol Chem 286(9):7359-7369.
    • (2011) J Biol Chem , vol.286 , Issue.9 , pp. 7359-7369
    • Sommer, M.E.1    Hofmann, K.P.2    Heck, M.M.3
  • 43
    • 33646899690 scopus 로고    scopus 로고
    • Dynamics of arrestin-rhodopsin interactions: Acidic phospholipids enable binding of arrestin to purified rhodopsin in detergent
    • Sommer ME, Smith WC, Farrens DL (2006) Dynamics of arrestin-rhodopsin interactions: Acidic phospholipids enable binding of arrestin to purified rhodopsin in detergent. J Biol Chem 281(14):9407-9417.
    • (2006) J Biol Chem , vol.281 , Issue.14 , pp. 9407-9417
    • Sommer, M.E.1    Smith, W.C.2    Farrens, D.L.3
  • 44
    • 78651411166 scopus 로고    scopus 로고
    • Structure of a nanobody-stabilized active state of the β(2) adrenoceptor
    • Rasmussen SGF, et al. (2011) Structure of a nanobody-stabilized active state of the β(2) adrenoceptor. Nature 469(7329):175-180.
    • (2011) Nature , vol.469 , Issue.7329 , pp. 175-180
    • Rasmussen, S.G.F.1
  • 45
    • 84865527500 scopus 로고    scopus 로고
    • Manipulation of very few receptor discriminator residues greatly enhances receptor specificity of non-visual arrestins
    • Gimenez LE, Vishnivetskiy SA, Baameur F, Gurevich VV (2012) Manipulation of very few receptor discriminator residues greatly enhances receptor specificity of non-visual arrestins. J Biol Chem 287(35):29495-29505.
    • (2012) J Biol Chem , vol.287 , Issue.35 , pp. 29495-29505
    • Gimenez, L.E.1    Vishnivetskiy, S.A.2    Baameur, F.3    Gurevich, V.V.4
  • 46
    • 84873323643 scopus 로고    scopus 로고
    • Engineering visual arrestin-1 with special functional characteristics
    • Vishnivetskiy SA, et al. (2013) Engineering visual arrestin-1 with special functional characteristics. J Biol Chem 288(5):3394-3405.
    • (2013) J Biol Chem , vol.288 , Issue.5 , pp. 3394-3405
    • Vishnivetskiy, S.A.1
  • 47
    • 6344227960 scopus 로고    scopus 로고
    • Crystals of native and modified bovine rhodopsins and their heavy atom derivatives
    • Edwards PC, et al. (2004) Crystals of native and modified bovine rhodopsins and their heavy atom derivatives. J Mol Biol 343(5):1439-1450.
    • (2004) J Mol Biol , vol.343 , Issue.5 , pp. 1439-1450
    • Edwards, P.C.1
  • 48
    • 0034087630 scopus 로고    scopus 로고
    • Isolation of isoelectric species of phosphorylated rhodopsin
    • McDowell JH, Nawrocki JP, Hargrave PA (2000) Isolation of isoelectric species of phosphorylated rhodopsin. Methods Enzymol 315:70-76.
    • (2000) Methods Enzymol , vol.315 , pp. 70-76
    • McDowell, J.H.1    Nawrocki, J.P.2    Hargrave, P.A.3
  • 49
    • 36148992935 scopus 로고    scopus 로고
    • Regulation of arrestin binding by rhodopsin phosphorylation level
    • Vishnivetskiy SA, et al. (2007) Regulation of arrestin binding by rhodopsin phosphorylation level. J Biol Chem 282(44):32075-32083.
    • (2007) J Biol Chem , vol.282 , Issue.44 , pp. 32075-32083
    • Vishnivetskiy, S.A.1


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