메뉴 건너뛰기




Volumn 29, Issue 38, 2009, Pages 11867-11879

Arrestin competition influences the kinetics and variability of the single-photon responses of mammalian rod photoreceptors

Author keywords

[No Author keywords available]

Indexed keywords

RETINA S ANTIGEN; RHODOPSIN KINASE; TRANSDUCIN;

EID: 70349320393     PISSN: 02706474     EISSN: 15292401     Source Type: Journal    
DOI: 10.1523/JNEUROSCI.0819-09.2009     Document Type: Article
Times cited : (29)

References (80)
  • 1
    • 33244485265 scopus 로고    scopus 로고
    • The interpretation of morphogen gradients
    • Ashe HL, Briscoe J (2006) The interpretation of morphogen gradients. Development 133:385-394.
    • (2006) Development , vol.133 , pp. 385-394
    • Ashe, H.L.1    Briscoe, J.2
  • 2
    • 0018333003 scopus 로고
    • Responses of retinal rods to single photons
    • Baylor DA, Lamb TD, Yau KW (1979) Responses of retinal rods to single photons. J Physiol 288:613-634.
    • (1979) J Physiol , vol.288 , pp. 613-634
    • Baylor, D.A.1    Lamb, T.D.2    Yau, K.W.3
  • 3
    • 21344463521 scopus 로고    scopus 로고
    • Cell signaling: Elementary response of olfactory receptor neurons to odorants
    • DOI 10.1126/science.1109886
    • Bhandawat V, Reisert J, Yau KW (2005) Elementary response of olfactory receptor neurons to odorants. Science 308:1931-1934. (Pubitemid 40941880)
    • (2005) Science , vol.308 , Issue.5730 , pp. 1931-1934
    • Bhandawat, V.1    Reisert, J.2    Yau, K.-W.3
  • 4
    • 43649090740 scopus 로고    scopus 로고
    • Diffusion of the second messengers in the cytoplasm acts as a variability suppressor of the single photon response in vertebrate phototransduction
    • Bisegna P, Caruso G, Andreucci D, Shen L, Gurevich VV, Hamm HE, DiBenedetto E (2008) Diffusion of the second messengers in the cytoplasm acts as a variability suppressor of the single photon response in vertebrate phototransduction. Biophys J 94:3363-3383.
    • (2008) Biophys J , vol.94 , pp. 3363-3383
    • Bisegna, P.1    Caruso, G.2    Andreucci, D.3    Shen, L.4    Gurevich, V.V.5    Hamm, H.E.6    Dibenedetto, E.7
  • 5
    • 0033596952 scopus 로고    scopus 로고
    • Rhodopsin's carboxyl-terminal threonines are required for wild-type arrestin-mediated quench of transducin activation in vitro
    • Brannock MT, Weng K, Robinson PR (1999) Rhodopsin's carboxyl-terminal threonines are required for wild-type arrestin-mediated quench of transducin activation in vitro. Biochemistry 38:3770-3777. (Pubitemid 129514634)
    • (1999) Biochemistry , vol.38 , Issue.12 , pp. 3770-3777
    • Brannock, M.T.1    Weng, K.2    Robinson, P.R.3
  • 7
    • 0034677632 scopus 로고    scopus 로고
    • The molecular architecture of odor and pheromone sensing in mammals
    • Buck LB (2000) The molecular architecture of odor and pheromone sensing in mammals. Cell 100:611-618.
    • (2000) Cell , vol.100 , pp. 611-618
    • Buck, L.B.1
  • 8
    • 0037179759 scopus 로고    scopus 로고
    • Dynamics of cyclic GMP synthesis in retinal rods
    • Burns ME, Mendez A, Chen J, Baylor DA (2002) Dynamics of cyclic GMP synthesis in retinal rods. Neuron 36:81-91.
    • (2002) Neuron , vol.36 , pp. 81-91
    • Burns, M.E.1    Mendez, A.2    Chen, J.3    Baylor, D.A.4
  • 12
    • 33745607882 scopus 로고    scopus 로고
    • Feedback signaling controls leading-edge formation during chemotaxis
    • Charest PG, Firtel RA (2006) Feedback signaling controls leading-edge formation during chemotaxis. Curr Opin Genet Dev 16:339-347.
    • (2006) Curr Opin Genet Dev , vol.16 , pp. 339-347
    • Charest, P.G.1    Firtel, R.A.2
  • 14
    • 0028955343 scopus 로고
    • Mechanisms of rhodopsin inactivation in vivo as revealed by a COOH-terminal truncation mutant
    • Chen J, Makino CL, Peachey NS, Baylor DA, Simon MI (1995) Mechanisms of rhodopsin inactivation in vivo as revealed by a COOH-terminal truncation mutant. Science 267:374-377.
    • (1995) Science , vol.267 , pp. 374-377
    • Chen, J.1    Makino, C.L.2    Peachey, N.S.3    Baylor, D.A.4    Simon, M.I.5
  • 15
    • 0033637433 scopus 로고    scopus 로고
    • Engineering aspects of enzymatic signal transduction: Photoreceptors in the retina
    • Detwiler PB, Ramanathan S, Sengupta A, Shraiman BI (2000) Engineering aspects of enzymatic signal transduction: photoreceptors in the retina. Biophys J 79:2801-2817.
    • (2000) Biophys J , vol.79 , pp. 2801-2817
    • Detwiler, P.B.1    Ramanathan, S.2    Sengupta, A.3    Shraiman, B.I.4
  • 16
    • 33746659395 scopus 로고    scopus 로고
    • Multiple phosphorylation sites confer reproducibility of the Rod's single-photon responses
    • DOI 10.1126/science.1126612
    • Doan T, Mendez A, Detwiler PB, Chen J, Rieke F (2006) Multiple phosphorylation sites confer reproducibility of the rod's single-photon responses. Science 313:530-533. (Pubitemid 44148459)
    • (2006) Science , vol.313 , Issue.5786 , pp. 530-533
    • Doan, T.1    Mendez, A.2    Detwiler, P.B.3    Chen, J.4    Rieke, F.5
  • 17
    • 34447513030 scopus 로고    scopus 로고
    • Emerging concepts of guanine nucleotide-binding protein-coupled receptor (GPCR) function and implications for high throughput screening
    • DOI 10.1089/adt.2007.062
    • Eglen RM, Bosse R, Reisine T (2007) Emerging concepts of guanine nucleotide-binding protein-coupled receptor (GPCR) function and implications for high throughput screening. Assay Drug Dev Technol 5:425-451. (Pubitemid 47067887)
    • (2007) Assay and Drug Development Technologies , vol.5 , Issue.3 , pp. 425-451
    • Eglen, R.M.1    Bosse, R.2    Reisine, T.3
  • 18
    • 0037104628 scopus 로고    scopus 로고
    • Mechanisms regulating variability of the single photon responses of mammalian rod photoreceptors
    • Field GD, Rieke F (2002a) Mechanisms regulating variability of the single photon responses of mammalian rod photoreceptors. Neuron 35:733-747.
    • (2002) Neuron , vol.35 , pp. 733-747
    • Field, G.D.1    Rieke, F.2
  • 19
    • 0037198718 scopus 로고    scopus 로고
    • Nonlinear signal transfer from mouse rods to bipolar cells and implications for visual sensitivity
    • Field GD, Rieke F (2002b) Nonlinear signal transfer from mouse rods to bipolar cells and implications for visual sensitivity. Neuron 34:773-785.
    • (2002) Neuron , vol.34 , pp. 773-785
    • Field, G.D.1    Rieke, F.2
  • 20
    • 12144276559 scopus 로고    scopus 로고
    • Retinal processing near absolute threshold: From behavior to mechanism
    • Field GD, Sampath AP, Rieke F (2005) Retinal processing near absolute threshold: from behavior to mechanism. Annu Rev Physiol 67:491-514.
    • (2005) Annu Rev Physiol , vol.67 , pp. 491-514
    • Field, G.D.1    Sampath, A.P.2    Rieke, F.3
  • 21
    • 0034673947 scopus 로고    scopus 로고
    • Phosphorylation modulates the affinity of light-activated rhodopsin for G protein and arrestin
    • Gibson SK, Parkes JH, Liebman PA (2000) Phosphorylation modulates the affinity of light-activated rhodopsin for G protein and arrestin. Biochemistry 39:5738-5749.
    • (2000) Biochemistry , vol.39 , pp. 5738-5749
    • Gibson, S.K.1    Parkes, J.H.2    Liebman, P.A.3
  • 22
    • 0033166002 scopus 로고    scopus 로고
    • A dissection of the electroretinogram from the isolated rat retina with microelectrodes and drugs
    • DOI 10.1017/S0952523899164125
    • Green DG, Kapousta-Bruneau NV (1999) A dissection of the electroretinogram from the isolated rat retina with microelectrodes and drugs. Vis Neurosci 16:727-741. (Pubitemid 29347765)
    • (1999) Visual Neuroscience , vol.16 , Issue.4 , pp. 727-741
    • Green, D.G.1    Kapousta-Bruneau, N.V.2
  • 23
    • 0026785338 scopus 로고
    • Cell-free expression of visual arrestin. Truncation mutagenesis identifies multiple domains involved in rhodopsin interaction
    • Gurevich VV, Benovic JL (1992) Cell-free expression of visual arrestin. Truncation mutagenesis identifies multiple domains involved in rhodopsin interaction. J Biol Chem 267:21919-21923.
    • (1992) J Biol Chem , vol.267 , pp. 21919-21923
    • Gurevich, V.V.1    Benovic, J.L.2
  • 24
    • 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 268:11628-11638. (Pubitemid 23168111)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.16 , pp. 11628-11638
    • Gurevich, V.V.1    Benovic, J.L.2
  • 25
    • 0028924619 scopus 로고
    • Visual arrestin binding to rhodopsin. Diverse functional roles of positively charged residues within the phosphorylation-recognition region of arrestin
    • Gurevich VV, Benovic JL (1995) Visual arrestin binding to rhodopsin. Diverse functional roles of positively charged residues within the phosphorylation-recognition region of arrestin. J Biol Chem 270:6010-6016.
    • (1995) J Biol Chem , vol.270 , pp. 6010-6016
    • Gurevich, V.V.1    Benovic, J.L.2
  • 26
    • 0842331059 scopus 로고    scopus 로고
    • The molecular acrobatics of arrestin activation
    • Gurevich VV, Gurevich EV (2004) The molecular acrobatics of arrestin activation. Trends Pharmacol Sci 25:105-111.
    • (2004) Trends Pharmacol Sci , vol.25 , pp. 105-111
    • Gurevich, V.V.1    Gurevich, E.V.2
  • 27
    • 0141919837 scopus 로고    scopus 로고
    • Multiple steps of phosphorylation of activated rhodopsin can account for the reproducibility of vertebrate rod single-photon responses
    • DOI 10.1085/jgp.200308832
    • Hamer RD, Nicholas SC, Tranchina D, Liebman PA, Lamb TD (2003) Multiple steps of phosphorylation of activated rhodopsin can account for the reproducibility of vertebrate rod single-photon responses. J Gen Physiol 122:419-444. (Pubitemid 37254726)
    • (2003) Journal of General Physiology , vol.122 , Issue.4 , pp. 419-444
    • Hamer, R.D.1    Nicholas, S.C.2    Tranchina, D.3    Liebman, P.A.4    Lamb, T.D.5
  • 28
    • 0022475858 scopus 로고
    • Protein complement of rod outer segments of frog retina
    • Hamm HE, Bownds MD (1986) Protein complement of rod outer segments of frog retina. Biochemistry 25:4512-4523. (Pubitemid 16010186)
    • (1986) Biochemistry , vol.25 , Issue.16 , pp. 4512-4523
    • Hamm, H.E.1    Bownds, M.D.2
  • 29
    • 33745058056 scopus 로고    scopus 로고
    • Role of G-protein-coupled receptor kinase 2 in the heart: Do regulatory mechanisms open novel therapeutic perspectives?
    • Hansen JL, Theilade J, Aplin M, Sheikh SP (2006) Role of G-protein-coupled receptor kinase 2 in the heart: do regulatory mechanisms open novel therapeutic perspectives? Trends Cardiovasc Med 16:169-177.
    • (2006) Trends Cardiovasc Med , vol.16 , pp. 169-177
    • Hansen, J.L.1    Theilade, J.2    Aplin, M.3    Sheikh, S.P.4
  • 32
    • 0033560916 scopus 로고    scopus 로고
    • Sensitivity and kinetics of mouse rod flash responses determined in vivo from paired-flash electroretinograms
    • Hetling JR, Pepperberg DR (1999) Sensitivity and kinetics of mouse rod flash responses determined in vivo from paired-flash electroretinograms. J Physiol 516:593-609.
    • (1999) J Physiol , vol.516 , pp. 593-609
    • Hetling, J.R.1    Pepperberg, D.R.2
  • 33
    • 0041343058 scopus 로고    scopus 로고
    • Concentration-dependent tetramerization of bovine visual arrestin
    • Imamoto Y, Tamura C, Kamikubo H, Kataoka M (2003) Concentration-dependent tetramerization of bovine visual arrestin. Biophys J 85:1186-1195. (Pubitemid 36909679)
    • (2003) Biophysical Journal , vol.85 , Issue.2 , pp. 1186-1195
    • Imamoto, Y.1    Tamura, C.2    Kamikubo, H.3    Kataoka, M.4
  • 35
    • 0025363918 scopus 로고
    • Characterization of rhodopsin kinase purified from bovine rod outer segments
    • Kelleher DJ, Johnson GL (1990) Characterization of rhodopsin kinase purified from bovine rod outer segments. J Biol Chem 265:2632-2639. (Pubitemid 20092371)
    • (1990) Journal of Biological Chemistry , vol.265 , Issue.5 , pp. 2632-2639
    • Kelleher, D.J.1    Johnson, G.L.2
  • 36
    • 0034885334 scopus 로고    scopus 로고
    • Multiple phosphorylation of rhodopsin and the in vivo chemistry underlying rod photoreceptor dark adaptation
    • Kennedy MJ, Lee KA, Niemi GA, Craven KB, Garwin GG, Saari JC, Hurley JB (2001) Multiple phosphorylation of rhodopsin and the in vivo chemistry underlying rod photoreceptor dark adaptation. Neuron 31:87-101.
    • (2001) Neuron , vol.31 , pp. 87-101
    • Kennedy, M.J.1    Lee, K.A.2    Niemi, G.A.3    Craven, K.B.4    Garwin, G.G.5    Saari, J.C.6    Hurley, J.B.7
  • 37
    • 0037336287 scopus 로고    scopus 로고
    • Acceleration of key reactions as a strategy to elucidate the rate-limiting chemistry underlying phototransduction inactivation
    • Kennedy MJ, Sowa ME, Wensel TG, Hurley JB (2003) Acceleration of key reactions as a strategy to elucidate the rate-limiting chemistry underlying phototransduction inactivation. Invest Ophthalmol Vis Sci 44:1016-1022.
    • (2003) Invest Ophthalmol Vis Sci , vol.44 , pp. 1016-1022
    • Kennedy, M.J.1    Sowa, M.E.2    Wensel, T.G.3    Hurley, J.B.4
  • 38
    • 34447633368 scopus 로고    scopus 로고
    • Conformational complexity of G-protein-coupled receptors
    • Kobilka BK, Deupi X (2007) Conformational complexity of G-protein-coupled receptors. Trends Pharmacol Sci 28:397-406.
    • (2007) Trends Pharmacol Sci , vol.28 , pp. 397-406
    • Kobilka, B.K.1    Deupi, X.2
  • 39
    • 0023891895 scopus 로고
    • Highly cooperative feedback control of retinal rod guanylate cyclase by calcium ions
    • Koch KW, Stryer L (1988) Highly cooperative feedback control of retinal rod guanylate cyclase by calcium ions. Nature 334:64-66.
    • (1988) Nature , vol.334 , pp. 64-66
    • Koch, K.W.1    Stryer, L.2
  • 41
    • 3042798261 scopus 로고    scopus 로고
    • Molecular mechanisms of ligand binding, signaling, and regulation within the superfamily of g-protein-coupled receptors: Molecular modeling and mutagenesis approaches to receptor structure and function
    • Kristiansen K (2004) Molecular mechanisms of ligand binding, signaling, and regulation within the superfamily of g-protein-coupled receptors: molecular modeling and mutagenesis approaches to receptor structure and function. Pharmacol Ther 103:21-80.
    • (2004) Pharmacol Ther , vol.103 , pp. 21-80
    • Kristiansen, K.1
  • 43
    • 0030793446 scopus 로고    scopus 로고
    • Mechanism of quenching of phototransduction. binding competition between arrestin and transducin for phosphorhodopsin
    • Krupnick JG, Gurevich VV, Benovic JL (1997) Mechanism of quenching of phototransduction. binding competition between arrestin and transducin for phosphorhodopsin. J Biol Chem 272:18125-18131.
    • (1997) J Biol Chem , vol.272 , pp. 18125-18131
    • Krupnick, J.G.1    Gurevich, V.V.2    Benovic, J.L.3
  • 44
    • 0021748638 scopus 로고
    • Light-induced binding of 48-kDa protein to photoreceptor membranes is highly enhanced by phosphorylation of rhodopsin
    • DOI 10.1016/0014-5793(84)81221-1
    • Kühn H, Hall SW, Wilden U (1984) Light-induced binding of 48-kDa protein to photoreceptor membranes is highly enhanced by phosphorylation of rhodopsin. FEBS Lett 176:473-478. (Pubitemid 15208287)
    • (1984) FEBS Letters , vol.176 , Issue.2 , pp. 473-478
    • Kuhn, H.1    Hall, S.W.2    Wilden, U.3
  • 46
    • 1942487322 scopus 로고    scopus 로고
    • Experimental and Computational Studies of the Desensitization Process in the Bovine Rhodopsin-Arrestin Complex
    • Ling Y, Ascano M, Robinson P, Gregurick SK (2004) Experimental and computational studies of the desensitization process in the bovine rhodopsin-arrestin complex. Biophys J 86:2445-2454. (Pubitemid 38524432)
    • (2004) Biophysical Journal , vol.86 , Issue.4 , pp. 2445-2454
    • Ling, Y.1    Ascano, M.2    Robinson, P.3    Gregurick, S.K.4
  • 48
    • 33847728682 scopus 로고    scopus 로고
    • Adrenal GRK2 upregulation mediates sympathetic overdrive in heart failure
    • DOI 10.1038/nm1553, PII NM1553
    • Lymperopoulos A, Rengo G, Funakoshi H, Eckhart AD, Koch WJ (2007) Adrenal GRK2 upregulation mediates sympathetic overdrive in heart failure. Nat Med 13:315-323. (Pubitemid 46376685)
    • (2007) Nature Medicine , vol.13 , Issue.3 , pp. 315-323
    • Lymperopoulos, A.1    Rengo, G.2    Funakoshi, H.3    Eckhart, A.D.4    Koch, W.J.5
  • 49
    • 0030050756 scopus 로고    scopus 로고
    • Recovery phase of the murine rod photoresponse reconstructed from electroretinographic recordings
    • Lyubarsky AL, Pugh EN Jr (1996) Recovery phase of the murine rod photoresponse reconstructed from electroretinographic recordings. J Neurosci 16:563-571.
    • (1996) J Neurosci , vol.16 , pp. 563-571
    • Lyubarsky, A.L.1    Pugh Jr., E.N.2
  • 51
    • 0042379627 scopus 로고    scopus 로고
    • Piecing together the timetable for visual transduction with transgenic animals
    • Makino CL, Wen XH, Lem J (2003) Piecing together the timetable for visual transduction with transgenic animals. Curr Opin Neurobiol 13:404-412.
    • (2003) Curr Opin Neurobiol , vol.13 , pp. 404-412
    • Makino, C.L.1    Wen, X.H.2    Lem, J.3
  • 53
    • 0033638108 scopus 로고    scopus 로고
    • Rapid and reproducible deactivation of rhodopsin requires multiple phosphorylation sites
    • Mendez A, Burns ME, Roca A, Lem J, Wu LW, Simon MI, Baylor DA, Chen J (2000) Rapid and reproducible deactivation of rhodopsin requires multiple phosphorylation sites. Neuron 28:153-164.
    • (2000) Neuron , vol.28 , pp. 153-164
    • Mendez, A.1    Burns, M.E.2    Roca, A.3    Lem, J.4    Wu, L.W.5    Simon, M.I.6    Baylor, D.A.7    Chen, J.8
  • 54
    • 33646845296 scopus 로고    scopus 로고
    • GRK et arrestines: La piste therapeutique?
    • Métayé T, Perdrisot R, Kraimps JL (2006) GRKs and arrestins: the therapeutic pathway (in French)? Med Sci (Paris) 22:537-543. (Pubitemid 43774270)
    • (2006) Medecine/Sciences , vol.22 , Issue.5 , pp. 537-543
    • Metaye, T.1    Perdrisot, R.2    Kraimps, J.-L.3
  • 55
    • 25844514195 scopus 로고    scopus 로고
    • Light responses and light adaptation in rat retinal rods at different temperatures
    • DOI 10.1113/jphysiol.2005.090662
    • Nymark S, Heikkinen H, Haldin C, Donner K, Koskelainen A (2005) Light responses and light adaptation in rat retinal rods at different temperatures. J Physiol 567:923-938. (Pubitemid 41387834)
    • (2005) Journal of Physiology , vol.567 , Issue.3 , pp. 923-938
    • Nymark, S.1    Heikkinen, H.2    Haldin, C.3    Donner, K.4    Koskelainen, A.5
  • 58
    • 0033617576 scopus 로고    scopus 로고
    • A cell's sense of direction
    • Parent CA, Devreotes PN (1999) A cell's sense of direction. Science 284:765-770.
    • (1999) Science , vol.284 , pp. 765-770
    • Parent, C.A.1    Devreotes, P.N.2
  • 61
    • 33645235107 scopus 로고    scopus 로고
    • Glc7/protein phosphatase 1 regulatory subunits can oppose the Ipl1/aurora protein kinase by redistributing glc7
    • Pinsky BA, Kotwaliwale CV, Tatsutani SY, Breed CA, Biggins S (2006) Glc7/protein phosphatase 1 regulatory subunits can oppose the Ipl1/aurora protein kinase by redistributing glc7. Mol Cell Biol 26:2648-2660.
    • (2006) Mol Cell Biol , vol.26 , pp. 2648-2660
    • Pinsky, B.A.1    Kotwaliwale, C.V.2    Tatsutani, S.Y.3    Breed, C.A.4    Biggins, S.5
  • 62
    • 33947375174 scopus 로고    scopus 로고
    • Physiological roles of g protein-coupled receptor kinases and arrestins
    • Premont RT, Gainetdinov RR (2007) Physiological roles of g protein-coupled receptor kinases and arrestins. Annu Rev Physiol 69:511-534.
    • (2007) Annu Rev Physiol , vol.69 , pp. 511-534
    • Premont, R.T.1    Gainetdinov, R.R.2
  • 63
    • 0033586719 scopus 로고    scopus 로고
    • Binding of arrestin to cytoplasmic loop mutants of bovine rhodopsin
    • Raman D, Osawa S, Weiss ER (1999) Binding of arrestin to cytoplasmic loop mutants of bovine rhodopsin. Biochemistry 38:5117-5123. (Pubitemid 129514784)
    • (1999) Biochemistry , vol.38 , Issue.16 , pp. 5117-5123
    • Raman, D.1    Osawa, S.2    Weiss, E.R.3
  • 64
    • 0037340792 scopus 로고    scopus 로고
    • The interaction with the cytoplasmic loops of rhodopsin plays a crucial role in arrestin activation and binding
    • DOI 10.1046/j.1471-4159.2003.01598.x
    • Raman D, Osawa S, Gurevich VV, Weiss ER (2003) The interaction with the cytoplasmic loops of rhodopsin plays a crucial role in arrestin activation and binding. J Neurochem 84:1040-1050. (Pubitemid 36330657)
    • (2003) Journal of Neurochemistry , vol.84 , Issue.5 , pp. 1040-1050
    • Raman, D.1    Osawa, S.2    Gurevich, V.V.3    Weiss, E.R.4
  • 65
    • 0031666785 scopus 로고    scopus 로고
    • Origin of reproducibility in the responses of retinal rods to single photons
    • Rieke F, Baylor DA (1998) Origin of reproducibility in the responses of retinal rods to single photons. Biophys J 75:1836-1857. (Pubitemid 28455179)
    • (1998) Biophysical Journal , vol.75 , Issue.4 , pp. 1836-1857
    • Rieke, F.1    Baylor, D.A.2
  • 66
    • 18144408355 scopus 로고    scopus 로고
    • Recoverin improves rod-mediated vision by enhancing signal transmission in the mouse retina
    • DOI 10.1016/j.neuron.2005.04.006, PII S0896627305003193
    • Sampath AP, Strissel KJ, Elias R, Arshavsky VY, McGinnis JF, Chen J, Kawamura S, Rieke F, Hurley JB (2005) Recoverin improves rod-mediated vision by enhancing signal transmission in the mouse retina. Neuron 46:413-420. (Pubitemid 40616885)
    • (2005) Neuron , vol.46 , Issue.3 , pp. 413-420
    • Sampath, A.P.1    Strissel, K.J.2    Elias, R.3    Arshavsky, V.Y.4    McGinnis, J.F.5    Chen, J.6    Kawamura, S.7    Rieke, F.8    Hurley, J.B.9
  • 68
    • 0028900858 scopus 로고
    • Rhodopsin mutants discriminate sites important for the activation of rhodopsin kinase and gt
    • Shi W, Osawa S, Dickerson CD, Weiss ER (1995) Rhodopsin mutants discriminate sites important for the activation of rhodopsin kinase and gt. J Biol Chem 270:2112-2119.
    • (1995) J Biol Chem , vol.270 , pp. 2112-2119
    • Shi, W.1    Osawa, S.2    Dickerson, C.D.3    Weiss, E.R.4
  • 69
    • 0025863686 scopus 로고
    • Calcium feedback and sensitivity regulation in primate rods
    • Tamura T, Nakatani K, Yau KW (1991) Calcium feedback and sensitivity regulation in primate rods. J Gen Physiol 98:95-130.
    • (1991) J Gen Physiol , vol.98 , pp. 95-130
    • Tamura, T.1    Nakatani, K.2    Yau, K.W.3
  • 72
    • 33845412884 scopus 로고    scopus 로고
    • GRKs and arrestins: Regulators of migration and inflammation
    • DOI 10.1189/jlb.0606373
    • Vroon A, Heijnen CJ, Kavelaars A (2006) GRKs and arrestins: regulators of migration and inflammation. J Leukoc Biol 80:1214-1221. (Pubitemid 44904958)
    • (2006) Journal of Leukocyte Biology , vol.80 , Issue.6 , pp. 1214-1221
    • Vroon, A.1    Heijnen, C.J.2    Kavelaars, A.3
  • 73
    • 3042659111 scopus 로고    scopus 로고
    • Spinophilin blocks arrestin actions in vitro and in vivo at G protein-coupled receptors
    • DOI 10.1126/science.1098274
    • Wang Q, Zhao J, Brady AE, Feng J, Allen PB, Lefkowitz RJ, Greengard P, Limbird LE (2004) Spinophilin blocks arrestin actions in vitro and in vivo at G protein-coupled receptors. Science 304:1940-1944. (Pubitemid 38822181)
    • (2004) Science , vol.304 , Issue.5679 , pp. 1940-1944
    • Wang, Q.1    Zhao, J.2    Brady, A.E.3    Feng, J.4    Allon, P.B.5    Lefkowitz, R.J.6    Greengard, P.7    Limbird, L.E.8
  • 74
    • 0033152452 scopus 로고    scopus 로고
    • Variability in the time course of single photon responses from toad rods: Termination of rhodopsin's activity
    • Whitlock GG, Lamb TD (1999) Variability in the time course of single photon responses from toad rods: termination of rhodopsin's activity. Neuron 23:337-351.
    • (1999) Neuron , vol.23 , pp. 337-351
    • Whitlock, G.G.1    Lamb, T.D.2
  • 75
    • 0028921426 scopus 로고
    • Duration and amplitude of the light-induced cGMP hydrolysis in vertebrate photoreceptors are regulated by multiple phosphorylation of rhodopsin and by arrestin binding
    • Wilden U (1995) Duration and amplitude of the light-induced cGMP hydrolysis in vertebrate photoreceptors are regulated by multiple phosphorylation of rhodopsin and by arrestin binding. Biochemistry 34:1446-1454.
    • (1995) Biochemistry , vol.34 , pp. 1446-1454
    • Wilden, U.1
  • 76
    • 0019956634 scopus 로고
    • Light-dependent phosphorylation of rhodopsin: Number of phosphorylation sites
    • Wilden U, Kühn H (1982) Light-dependent phosphorylation of rhodopsin: number of phosphorylation sites. Biochemistry 21:3014-3022.
    • (1982) Biochemistry , vol.21 , pp. 3014-3022
    • Wilden, U.1    Kühn, H.2
  • 77
    • 0000025689 scopus 로고
    • Phosphodiesterase activation by photoexcited rhodopsin is quenched when rhodopsin is phosphorylated and binds the intrinsic 48-kDa protein of rod outer segments
    • Wilden U, Hall SW, Kühn H (1986) Phosphodiesterase activation by photoexcited rhodopsin is quenched when rhodopsin is phosphorylated and binds the intrinsic 48-kDa protein of rod outer segments. Proc Natl Acad Sci U S A 83:1174-1178. (Pubitemid 16016091)
    • (1986) Proceedings of the National Academy of Sciences of the United States of America , vol.83 , Issue.5 , pp. 1174-1178
    • Wilden, U.1    Hall, S.W.2    Kuhn, H.3
  • 78
    • 0030842611 scopus 로고    scopus 로고
    • Prolonged photoresponses in transgenic mouse rods lacking arrestin
    • DOI 10.1038/39068
    • Xu J, Dodd RL, Makino CL, Simon MI, Baylor DA, Chen J (1997) Prolonged photoresponses in transgenic mouse rods lacking arrestin. Nature 389:505-509. (Pubitemid 27435327)
    • (1997) Nature , vol.389 , Issue.6650 , pp. 505-509
    • Xu, J.1    Dodd, R.L.2    Makino, C.L.3    Simon, M.I.4    Baylor, D.A.5    Chen, J.6
  • 80
    • 0030902488 scopus 로고    scopus 로고
    • Rhodopsin phosphorylation sites and their role in arrestin binding
    • DOI 10.1074/jbc.272.23.14762
    • Zhang L, Sports CD, Osawa S, Weiss ER (1997) Rhodopsin phosphorylation sites and their role in arrestin binding. J Biol Chem 272:14762-14768. (Pubitemid 27251743)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.23 , pp. 14762-14768
    • Zhang, L.1    Sports, C.D.2    Osawa, S.3    Weiss, E.R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.