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Volumn , Issue , 2007, Pages 33-54

Photoactivation of rhodopsin and signal transfer to transducin

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EID: 79958062942     PISSN: None     EISSN: None     Source Type: Book    
DOI: None     Document Type: Chapter
Times cited : (3)

References (86)
  • 1
    • 34248215318 scopus 로고    scopus 로고
    • Visual rhodopsin sees the light: Structure and mechanism of G protein signaling
    • Ridge, K.D. and Palczewski, K. Visual rhodopsin sees the light: Structure and mechanism of G protein signaling. J Biol Chem 282, 9297-301 (2007).
    • (2007) J Biol Chem , vol.282 , pp. 9297-9301
    • Ridge, K.D.1    Palczewski, K.2
  • 2
    • 25144518096 scopus 로고    scopus 로고
    • Focus on molecules: Rhodopsin
    • Kisselev, O.G. Focus on molecules: Rhodopsin. Exp Eye Res 81, 366-7 (2005).
    • (2005) Exp Eye Res , vol.81 , pp. 366-367
    • Kisselev, O.G.1
  • 4
    • 0037285444 scopus 로고    scopus 로고
    • Rhodopsin structure, dynamics, and activation: A perspective from crystallography, site-directed spin labeling, sulfhydryl reactivity, and disulfide cross-linking
    • Hubbell, W.L., Altenbach, C., Hubbell, C.M., and Khorana, H.G. Rhodopsin structure, dynamics, and activation: A perspective from crystallography, site-directed spin labeling, sulfhydryl reactivity, and disulfide cross-linking. Adv Protein Chem 63, 243-90 (2003).
    • (2003) Adv Protein Chem , vol.63 , pp. 243-290
    • Hubbell, W.L.1    Altenbach, C.2    Hubbell, C.M.3    Khorana, H.G.4
  • 6
    • 0035942220 scopus 로고    scopus 로고
    • How activated receptors couple to G proteins
    • Hamm, H.E. How activated receptors couple to G proteins. Proc Natl Acad Sci USA 98, 4819-21 (2001).
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 4819-4821
    • Hamm, H.E.1
  • 8
    • 0037452545 scopus 로고    scopus 로고
    • A conformational trigger for activation of a G protein by a G protein-coupled receptor
    • Yeagle, P.L. and Albert, A.D. A conformational trigger for activation of a G protein by a G protein-coupled receptor. Biochemistry 42, 1365-8 (2003).
    • (2003) Biochemistry , vol.42 , pp. 1365-1368
    • Yeagle, P.L.1    Albert, A.D.2
  • 9
    • 0041656354 scopus 로고    scopus 로고
    • Building a stage for interhelical play in rhodopsin
    • Abdulaev, N.G. Building a stage for interhelical play in rhodopsin. Trends Biochem Sci 28, 399-402 (2003).
    • (2003) Trends Biochem Sci , vol.28 , pp. 399-402
    • Abdulaev, N.G.1
  • 10
    • 0029993990 scopus 로고    scopus 로고
    • Activating mutations of rhodopsin and other G proteincoupled receptors
    • Rao, V.R. and Oprian, D.D. Activating mutations of rhodopsin and other G proteincoupled receptors. Annu. Rev. Biophys. Biomol. Struct. 25, 287-314 (1996).
    • (1996) Annu. Rev. Biophys. Biomol. Struct. , vol.25 , pp. 287-314
    • Rao, V.R.1    Oprian, D.D.2
  • 11
    • 23044486642 scopus 로고    scopus 로고
    • Structure of rhodopsin and the metarhodopsin I photointermediate
    • Schertler, G.F. Structure of rhodopsin and the metarhodopsin I photointermediate.Curr Opin Struct Biol 15, 408-15 (2005).
    • (2005) Curr Opin Struct Biol , vol.15 , pp. 408-415
    • Schertler, G.F.1
  • 12
    • 0035336676 scopus 로고    scopus 로고
    • Activation of rhodopsin: New insights from structural and biochemical studies
    • Okada, T., Ernst, O.P., Palczewski, K., and Hofmann, K.P. Activation of rhodopsin: New insights from structural and biochemical studies. Trends Biochem Sci 26, 318-24 (2001).
    • (2001) Trends Biochem Sci , vol.26 , pp. 318-324
    • Okada, T.1    Ernst, O.P.2    Palczewski, K.3    Hofmann, K.P.4
  • 13
    • 0033252860 scopus 로고    scopus 로고
    • Signalling states of photoactivated rhodopsin
    • discussion 175-80
    • Hofmann, K.P. Signalling states of photoactivated rhodopsin. Novartis Found Symp 224, 158-75; discussion 175-80 (1999).
    • (1999) Novartis Found Symp , vol.224 , pp. 158-175
    • Hofmann, K.P.1
  • 14
    • 0024427734 scopus 로고
    • The transitory complex between photoexcited rhodopsin and transducin. Reciprocal interaction between the retinal site in rhodopsin and the nucleotide site in transducin
    • Bornancin, F., Pfister, C., and Chabre, M. The transitory complex between photoexcited rhodopsin and transducin. Reciprocal interaction between the retinal site in rhodopsin and the nucleotide site in transducin. Eur J Biochem 184, 687-98 (1989).
    • (1989) Eur J Biochem , vol.184 , pp. 687-698
    • Bornancin, F.1    Pfister, C.2    Chabre, M.3
  • 15
    • 0000519923 scopus 로고
    • Flow of information in the light-triggered cyclic nucleotide cascade of vision
    • Fung, B.K., Hurley, J.B., and Stryer, L. Flow of information in the light-triggered cyclic nucleotide cascade of vision. Proc Natl Acad Sci USA 78, 152-6 (1981).
    • (1981) Proc Natl Acad Sci USA , vol.78 , pp. 152-156
    • Fung, B.K.1    Hurley, J.B.2    Stryer, L.3
  • 17
    • 0036498379 scopus 로고    scopus 로고
    • Rhodopsin phosphorylation: From terminating single photon responses to photoreceptor dark adaptation
    • Arshavsky, V.Y. Rhodopsin phosphorylation: From terminating single photon responses to photoreceptor dark adaptation. Trends Neurosci 25, 124-6 (2002).
    • (2002) Trends Neurosci , vol.25 , pp. 124-126
    • Arshavsky, V.Y.1
  • 18
    • 0842331059 scopus 로고    scopus 로고
    • The molecular acrobatics of arrestin activation
    • Gurevich, V.V. and Gurevich, E.V. The molecular acrobatics of arrestin activation.Trends Pharmacol Sci 25, 105-11 (2004).
    • (2004) Trends Pharmacol Sci , vol.25 , pp. 105-111
    • Gurevich, V.V.1    Gurevich, E.V.2
  • 19
    • 1842570287 scopus 로고    scopus 로고
    • Phototransduction in transgenic mice after targeted deletion of the rod transducin alpha-subunit
    • Calvert, P.D. et al. Phototransduction in transgenic mice after targeted deletion of the rod transducin alpha-subunit. Proc Natl Acad Sci USA 97, 13913-8 (2000).
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 13913-13918
    • Calvert, P.D.1
  • 21
    • 85055552550 scopus 로고
    • ed. Hargrave, P.A. Academic Press, Inc
    • Photoreceptor Cells. ed. Hargrave, P.A. Academic Press, Inc., 1993.
    • (1993) Photoreceptor Cells.
  • 22
    • 13344294239 scopus 로고
    • eds. Hargrave, P.A., Hofmann, K.P., and Kaupp, U.B. Springer-Verlag Berlin and Heidelberg GmbH, and Co. K
    • Signal Transduction in Photoreceptor Cells. eds. Hargrave, P.A., Hofmann, K.P., and Kaupp, U.B. Springer-Verlag Berlin and Heidelberg GmbH, and Co. K, 1992.
    • (1992) Signal Transduction in Photoreceptor Cells.
  • 23
    • 0016253492 scopus 로고
    • Rhodopsin content in the outer segment membranes of bovine and frog retinal rods
    • Papermaster, D.S. and Dreyer, W.J. Rhodopsin content in the outer segment membranes of bovine and frog retinal rods. Biochemistry 13, 2438-44 (1974).
    • (1974) Biochemistry , vol.13 , pp. 2438-2444
    • Papermaster, D.S.1    Dreyer, W.J.2
  • 24
    • 0007349708 scopus 로고
    • Reciprocal effects of an inhibitory factor on catalytic activity and noncatalytic cGMP binding sites of rod phosphodiesterase
    • Yamazaki, A., Bartucca, F., Ting, A., and Bitensky, M.W. Reciprocal effects of an inhibitory factor on catalytic activity and noncatalytic cGMP binding sites of rod phosphodiesterase.Proc Natl Acad Sci USA 79, 3702-6 (1982).
    • (1982) Proc Natl Acad Sci USA , vol.79 , pp. 3702-3706
    • Yamazaki, A.1    Bartucca, F.2    Ting, A.3    Bitensky, M.W.4
  • 25
    • 0027483048 scopus 로고
    • Cooperative binding of the retinal rod G-protein, transducin, to light-activated rhodopsin
    • Willardson, B.M., Pou, B., Yoshida, T., and Bitensky, M.W. Cooperative binding of the retinal rod G-protein, transducin, to light-activated rhodopsin. J Biol Chem 268, 6371-82 (1993).
    • (1993) J Biol Chem , vol.268 , pp. 6371-6382
    • Willardson, B.M.1    Pou, B.2    Yoshida, T.3    Bitensky, M.W.4
  • 27
    • 0015396799 scopus 로고
    • Preparation and properties of phospholipid bilayers containing rhodopsin
    • Hong, K. and Hubbell, W.L. Preparation and properties of phospholipid bilayers containing rhodopsin. Proc Natl Acad Sci USA 69, 2617-21 (1972).
    • (1972) Proc Natl Acad Sci USA , vol.69 , pp. 2617-2621
    • Hong, K.1    Hubbell, W.L.2
  • 28
    • 0028093624 scopus 로고
    • A farnesylated domain in the G protein gamma subunit is a specific determinant of receptor coupling
    • Kisselev, O.G., Ermolaeva, M.V., and Gautam, N. A farnesylated domain in the G protein gamma subunit is a specific determinant of receptor coupling. J Biol Chem 269, 21399-402 (1994).
    • (1994) J Biol Chem , vol.269 , pp. 21399-21402
    • Kisselev, O.G.1    Ermolaeva, M.V.2    Gautam, N.3
  • 29
    • 0033609101 scopus 로고    scopus 로고
    • Signal transfer from rhodopsin to the G-protein: Evidence for a two-site sequential fit mechanism
    • Kisselev, O.G., Meyer, C.K., Heck, M., Ernst, O.P., and Hofmann, K.P. Signal transfer from rhodopsin to the G-protein: Evidence for a two-site sequential fit mechanism.Proc Natl Acad Sci USA 96, 4898-4903 (1999).
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 4898-4903
    • Kisselev, O.G.1    Meyer, C.K.2    Heck, M.3    Ernst, O.P.4    Hofmann, K.P.5
  • 30
    • 0018827570 scopus 로고
    • Additional component required for activity and reconstitution of light-activated vertebrate photoreceptor GTPase
    • Shinozawa, T. et al. Additional component required for activity and reconstitution of light-activated vertebrate photoreceptor GTPase. Proc Natl Acad Sci USA 77, 1408-11 (1980).
    • (1980) Proc Natl Acad Sci USA , vol.77 , pp. 1408-1411
    • Shinozawa, T.1
  • 31
    • 0018901497 scopus 로고
    • Light- and GTP-regulated interaction of GTPase and other proteins with bovine photoreceptor membranes
    • Kühn, H. Light- and GTP-regulated interaction of GTPase and other proteins with bovine photoreceptor membranes. Nature 283, 587-9 (1980).
    • (1980) Nature , vol.283 , pp. 587-589
    • Kühn, H.1
  • 32
    • 0023036231 scopus 로고
    • Reciprocal control of retinal rod cyclic GMP phosphodiesterase by its gamma subunit and transducin
    • Wensel, T.G. and Stryer, L. Reciprocal control of retinal rod cyclic GMP phosphodiesterase by its gamma subunit and transducin. Proteins 1, 90-9 (1986).
    • (1986) Proteins , vol.1 , pp. 90-99
    • Wensel, T.G.1    Stryer, L.2
  • 33
    • 0024439305 scopus 로고
    • Activation of cGMP phosphodiesterase in retinal rods:Mechanism of interaction with the GTP-binding protein (transducin)
    • Bennett, N. and Clerc, A. Activation of cGMP phosphodiesterase in retinal rods:Mechanism of interaction with the GTP-binding protein (transducin). Biochemistry 28, 7418-24 (1989).
    • (1989) Biochemistry , vol.28 , pp. 7418-7424
    • Bennett, N.1    Clerc, A.2
  • 34
    • 0026489531 scopus 로고
    • Noncatalytic cGMP-binding sites of amphibian rod cGMP phosphodiesterase control interaction with its inhibitory gammasubunits. A putative regulatory mechanism of the rod photoresponse
    • Arshavsky, V.Y., Dumke, C.L., and Bownds, M.D. Noncatalytic cGMP-binding sites of amphibian rod cGMP phosphodiesterase control interaction with its inhibitory gammasubunits. A putative regulatory mechanism of the rod photoresponse. J Biol Chem 267, 24501-7 (1992).
    • (1992) J Biol Chem , vol.267 , pp. 24501-24507
    • Arshavsky, V.Y.1    Dumke, C.L.2    Bownds, M.D.3
  • 35
    • 0026681641 scopus 로고
    • A site on rod G protein alpha subunit that mediates effector activation
    • Rarick, H.M., Artemyev, N.O., and Hamm, H.E. A site on rod G protein alpha subunit that mediates effector activation. Science 256, 1031-3 (1992).
    • (1992) Science , vol.256 , pp. 1031-1033
    • Rarick, H.M.1    Artemyev, N.O.2    Hamm, H.E.3
  • 36
    • 0344874686 scopus 로고    scopus 로고
    • A point mutation uncouples transducin-alpha from the photoreceptor RGS and effector proteins
    • Natochin, M. and Artemyev, N.O. A point mutation uncouples transducin-alpha from the photoreceptor RGS and effector proteins. J Neurochem 87, 1262-71 (2003).
    • (2003) J Neurochem , vol.87 , pp. 1262-1271
    • Natochin, M.1    Artemyev, N.O.2
  • 37
    • 0022084697 scopus 로고
    • Inhibition of hormonally regulated adenylate cyclase by the beta gamma subunit of transducin
    • Bockaert, J., Deterre, P., Pfister, C., Guillon, G., and Chabre, M. Inhibition of hormonally regulated adenylate cyclase by the beta gamma subunit of transducin. EMBO J 4, 1413-7 (1985).
    • (1985) EMBO J , vol.4 , pp. 1413-1417
    • Bockaert, J.1    Deterre, P.2    Pfister, C.3    Guillon, G.4    Chabre, M.5
  • 38
    • 0033002698 scopus 로고    scopus 로고
    • A molecular mechanism for the phosphorylation-dependent regulation of heterotrimeric G proteins by phosducin
    • Gaudet, R., Savage, J.R., McLaughlin, J.N., Willardson, B.M., and Sigler, P.B. A molecular mechanism for the phosphorylation-dependent regulation of heterotrimeric G proteins by phosducin. Mol Cell 3, 649-60 (1999).
    • (1999) Mol Cell , vol.3 , pp. 649-660
    • Gaudet, R.1    Savage, J.R.2    McLaughlin, J.N.3    Willardson, B.M.4    Sigler, P.B.5
  • 39
    • 0035968163 scopus 로고    scopus 로고
    • Modulation of the G protein regulator phosducin by Ca2+/calmodulin- dependent protein kinase II phosphorylation and 14-3-3 protein binding
    • Thulin, C.D. et al. Modulation of the G protein regulator phosducin by Ca2+/calmodulin- dependent protein kinase II phosphorylation and 14-3-3 protein binding. J Biol Chem 276, 23805-15 (2001).
    • (2001) J Biol Chem , vol.276 , pp. 23805-23815
    • Thulin, C.D.1
  • 40
    • 0035722373 scopus 로고    scopus 로고
    • Phosducin down-regulation of G-protein coupling:Reconstitution of phosducin and transducin of cGMP cascade in bovine rod photoreceptor cells
    • Ho, Y.K., Ting, T.D., and Lee, R.H. Phosducin down-regulation of G-protein coupling:Reconstitution of phosducin and transducin of cGMP cascade in bovine rod photoreceptor cells. Methods Enzymol 344, 126-39 (2002).
    • (2002) Methods Enzymol , vol.344 , pp. 126-139
    • Ho, Y.K.1    Ting, T.D.2    Lee, R.H.3
  • 41
  • 42
    • 0028138403 scopus 로고
    • Roles of lipid modifications of transducin subunits in their GDP-dependent association and membrane binding
    • Bigay, J., Faurobert, E., Franco, M., and Chabre, M. Roles of lipid modifications of transducin subunits in their GDP-dependent association and membrane binding. Biochemistry 33, 14081-90 (1994).
    • (1994) Biochemistry , vol.33 , pp. 14081-14090
    • Bigay, J.1    Faurobert, E.2    Franco, M.3    Chabre, M.4
  • 43
    • 4043147871 scopus 로고    scopus 로고
    • How a G protein binds a membrane
    • Zhang, Z. et al. How a G protein binds a membrane. J Biol Chem 279, 33937-45 (2004).
    • (2004) J Biol Chem , vol.279 , pp. 33937-33945
    • Zhang, Z.1
  • 44
    • 0034603180 scopus 로고    scopus 로고
    • Enhancement of phototransduction protein interactions by lipid surfaces
    • Melia, T.J., Malinski, J.A., He, F., and Wensel, T.G. Enhancement of phototransduction protein interactions by lipid surfaces. J Biol Chem 275, 3535-42 (2000).
    • (2000) J Biol Chem , vol.275 , pp. 3535-3542
    • Melia, T.J.1    Malinski, J.A.2    He, F.3    Wensel, T.G.4
  • 45
    • 0027996145 scopus 로고
    • Characterization of interactions between transducin alpha/beta gamma- subunits and lipid membranes
    • Matsuda, T. et al. Characterization of interactions between transducin alpha/beta gamma- subunits and lipid membranes. J Biol Chem 269, 30358-63 (1994).
    • (1994) J Biol Chem , vol.269 , pp. 30358-30363
    • Matsuda, T.1
  • 46
    • 23744480236 scopus 로고    scopus 로고
    • Farnesylation of retinal transducin underlies its translocation during light adaptation
    • Kassai, H. et al. Farnesylation of retinal transducin underlies its translocation during light adaptation. Neuron 47, 529-39 (2005).
    • (2005) Neuron , vol.47 , pp. 529-539
    • Kassai, H.1
  • 47
    • 0027983602 scopus 로고
    • Effects of carboxyl methylation of photoreceptor G protein gammasubunit in visual transduction
    • Fukada, Y. et al. Effects of carboxyl methylation of photoreceptor G protein gammasubunit in visual transduction. J Biol Chem 269, 5163-70 (1994).
    • (1994) J Biol Chem , vol.269 , pp. 5163-5170
    • Fukada, Y.1
  • 48
    • 0029026880 scopus 로고
    • Receptor-G protein coupling is established by a potential conformational switch in the beta-gamma complex
    • Kisselev, O., Pronin, A., Ermolaeva, M., and Gautam, N. Receptor-G protein coupling is established by a potential conformational switch in the beta-gamma complex. Proc Natl Acad Sci USA 92, 9102-6 (1995).
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 9102-9106
    • Kisselev, O.1    Pronin, A.2    Ermolaeva, M.3    Gautam, N.4
  • 49
    • 33750622785 scopus 로고    scopus 로고
    • G-protein alpha and beta-gamma subunits interact with conformationally distinct signaling states of rhodopsin
    • Downs, M.A., Arimoto, R., Marshall, G.R., and Kisselev, O.G. G-protein alpha and beta-gamma subunits interact with conformationally distinct signaling states of rhodopsin.Vision Res 46, 4442-8 (2006).
    • (2006) Vision Res , vol.46 , pp. 4442-4448
    • Downs, M.A.1    Arimoto, R.2    Marshall, G.R.3    Kisselev, O.G.4
  • 50
    • 0042165824 scopus 로고    scopus 로고
    • Three-dimensional model for meta-II rhodopsin, an activated G-protein-coupled receptor
    • Nikiforovich, G.V. and Marshall, G.R. Three-dimensional model for meta-II rhodopsin, an activated G-protein-coupled receptor. Biochemistry 42, 9110-20 (2003).
    • (2003) Biochemistry , vol.42 , pp. 9110-9120
    • Nikiforovich, G.V.1    Marshall, G.R.2
  • 51
    • 28444450565 scopus 로고    scopus 로고
    • Modeling flexible loops in the dark-adapted and activated states of rhodopsin, a prototypical G-protein-coupled receptor
    • Nikiforovich, G.V. and Marshall, G.R. Modeling flexible loops in the dark-adapted and activated states of rhodopsin, a prototypical G-protein-coupled receptor. Biophys J 89, 3780-9 (2005).
    • (2005) Biophys J , vol.89 , pp. 3780-3789
    • Nikiforovich, G.V.1    Marshall, G.R.2
  • 52
    • 10844255797 scopus 로고    scopus 로고
    • Oligomerization of G proteincoupled receptors: Past, present, and future
    • Park, P.S., Filipek, S., Wells, J.W., and Palczewski, K. Oligomerization of G proteincoupled receptors: Past, present, and future. Biochemistry 43, 15643-56 (2004).
    • (2004) Biochemistry , vol.43 , pp. 15643-15656
    • Park, P.S.1    Filipek, S.2    Wells, J.W.3    Palczewski, K.4
  • 53
    • 0032474767 scopus 로고    scopus 로고
    • G-protein diseases furnish a model for the turn-on switch
    • Iiri, T., Farfel, Z., and Bourne, H.R. G-protein diseases furnish a model for the turn-on switch. Nature 394, 35-8 (1998).
    • (1998) Nature , vol.394 , pp. 35-38
    • Iiri, T.1    Farfel, Z.2    Bourne, H.R.3
  • 54
    • 2642588172 scopus 로고    scopus 로고
    • Sequence of interactions in receptor-G protein coupling
    • Herrmann, R. et al. Sequence of interactions in receptor-G protein coupling. J Biol Chem 279, 24283-90 (2004).
    • (2004) J Biol Chem , vol.279 , pp. 24283-24290
    • Herrmann, R.1
  • 55
    • 0037221946 scopus 로고    scopus 로고
    • Activation of G-protein Galpha subunits by receptors through Galpha-Gbeta and Galpha-Ggamma interactions
    • Cherfils, J. and Chabre, M. Activation of G-protein Galpha subunits by receptors through Galpha-Gbeta and Galpha-Ggamma interactions. Trends Biochem Sci 28, 13-7 (2003).
    • (2003) Trends Biochem Sci , vol.28 , pp. 13-17
    • Cherfils, J.1    Chabre, M.2
  • 56
    • 0030764672 scopus 로고    scopus 로고
    • Crystal structure of the EF-Tu.EF-Ts complex from Thermus thermophilus
    • Wang, Y., Jiang, Y., Meyering-Voss, M., Sprinzl, M., and Sigler, P.B. Crystal structure of the EF-Tu.EF-Ts complex from Thermus thermophilus. Nat Struct Biol 4, 650-6 (1997).
    • (1997) Nat Struct Biol , vol.4 , pp. 650-656
    • Wang, Y.1    Jiang, Y.2    Meyering-Voss, M.3    Sprinzl, M.4    Sigler, P.B.5
  • 57
    • 0037426865 scopus 로고    scopus 로고
    • Atomic-force microscopy: Rhodopsin dimers in native disc membranes
    • Fotiadis, D. et al. Atomic-force microscopy: Rhodopsin dimers in native disc membranes.Nature 421, 127-8 (2003).
    • (2003) Nature , vol.421 , pp. 127-128
    • Fotiadis, D.1
  • 58
    • 21844441860 scopus 로고    scopus 로고
    • Monomeric G-protein-coupled receptor as a functional unit
    • Chabre, M. and le Maire, M. Monomeric G-protein-coupled receptor as a functional unit. Biochemistry 44, 9395-403 (2005).
    • (2005) Biochemistry , vol.44 , pp. 9395-9403
    • Chabre, M.1    le Maire, M.2
  • 59
    • 33645958615 scopus 로고    scopus 로고
    • Structure of the rhodopsin dimer: A working model for G-proteincoupled receptors
    • Fotiadis, D. et al. Structure of the rhodopsin dimer: A working model for G-proteincoupled receptors. Curr Opin Struct Biol 16, 252-9 (2006).
    • (2006) Curr Opin Struct Biol , vol.16 , pp. 252-259
    • Fotiadis, D.1
  • 60
    • 33744965474 scopus 로고    scopus 로고
    • Functional and structural characterization of rhodopsin oligomers
    • Jastrzebska, B. et al. Functional and structural characterization of rhodopsin oligomers.J Biol Chem 281, 11917-22 (2006).
    • (2006) J Biol Chem , vol.281 , pp. 11917-11922
    • Jastrzebska, B.1
  • 61
    • 34247550299 scopus 로고    scopus 로고
    • Modeling of the complex between transducin and photoactivated rhodopsin, a prototypical g-protein-coupled receptor
    • Nikiforovich, G.V., Taylor, C.M., and Marshall, G.R. Modeling of the complex between transducin and photoactivated rhodopsin, a prototypical g-protein-coupled receptor.Biochemistry (2007).
    • (2007) Biochemistry
    • Nikiforovich, G.V.1    Taylor, C.M.2    Marshall, G.R.3
  • 62
    • 33847098734 scopus 로고    scopus 로고
    • Monomeric dark rhodopsin holds the molecular determinants for transducin recognition: Insights from computational analysis
    • Dell’Orco, D., Seeber, M., and Fanelli, F. Monomeric dark rhodopsin holds the molecular determinants for transducin recognition: Insights from computational analysis.FEBS Lett 581, 944-8 (2007).
    • (2007) FEBS Lett , vol.581 , pp. 944-948
    • Dell’Orco, D.1    Seeber, M.2    Fanelli, F.3
  • 63
    • 34447509986 scopus 로고    scopus 로고
    • Transducin activation by nanoscale lipid bilayers containing one and two rhodopsins
    • Bayburt, T.H., Leitz, A.J., Xie, G., Oprian, D.D., and Sligar, S.G. Transducin activation by nanoscale lipid bilayers containing one and two rhodopsins. J Biol Chem (2007).
    • (2007) J Biol Chem
    • Bayburt, T.H.1    Leitz, A.J.2    Xie, G.3    Oprian, D.D.4    Sligar, S.G.5
  • 64
    • 0040678011 scopus 로고    scopus 로고
    • Functional differences in the interaction of arrestin and its splice variant, p44, with rhodopsin
    • Pulvermuller, A. et al. Functional differences in the interaction of arrestin and its splice variant, p44, with rhodopsin. Biochemistry 36, 9253-60 (1997).
    • (1997) Biochemistry , vol.36 , pp. 9253-9260
    • Pulvermuller, A.1
  • 65
    • 0027495918 scopus 로고
    • Tryptophan W207 in transducin T alpha is the fluorescence sensor of the G protein activation switch and is involved in the effector binding
    • Faurobert, E., Otto-Bruc, A., Chardin, P., and Chabre, M. Tryptophan W207 in transducin T alpha is the fluorescence sensor of the G protein activation switch and is involved in the effector binding. EMBO J 12, 4191-8 (1993).
    • (1993) EMBO J , vol.12 , pp. 4191-4198
    • Faurobert, E.1    Otto-Bruc, A.2    Chardin, P.3    Chabre, M.4
  • 66
    • 0009304878 scopus 로고    scopus 로고
    • 1st ed. eds. Stavenga, D.G., De Grip, W.J., and Pugh, E.N., Jr. North Holland
    • Molecular Mechanisms in Visual Transduction 1st ed. eds. Stavenga, D.G., De Grip, W.J., and Pugh, E.N., Jr. North Holland, 2000.
    • (2000) Molecular Mechanisms in Visual Transduction
  • 67
    • 0003423122 scopus 로고    scopus 로고
    • eds. Abelson, J.N., Simon, M., and Palczewski, K. Academic Press
    • Vertebrate Phototransduction and the Visual Cycle. eds. Abelson, J.N., Simon, M., and Palczewski, K. Academic Press, 2000.
    • (2000) Vertebrate Phototransduction and the Visual Cycle.
  • 68
    • 1542650914 scopus 로고    scopus 로고
    • Purification of G protein subunits from Sf9 insect cells using hexahistidinetagged alpha and beta gamma subunits
    • Kozasa, T. Purification of G protein subunits from Sf9 insect cells using hexahistidinetagged alpha and beta gamma subunits. Methods Mol Biol 237, 21-38 (2004).
    • (2004) Methods Mol Biol , vol.237 , pp. 21-38
    • Kozasa, T.1
  • 69
    • 0028961594 scopus 로고
    • Purification of recombinant G proteins from Sf9 cells by hexahistidine tagging of associated subunits. Characterization of alpha 12 and inhibition of adenylyl cyclase by alpha z
    • Kozasa, T. and Gilman, A.G. Purification of recombinant G proteins from Sf9 cells by hexahistidine tagging of associated subunits. Characterization of alpha 12 and inhibition of adenylyl cyclase by alpha z. J Biol Chem 270, 1734-41 (1995).
    • (1995) J Biol Chem , vol.270 , pp. 1734-1741
    • Kozasa, T.1    Gilman, A.G.2
  • 70
    • 0019882018 scopus 로고
    • Silver staining of proteins in polyacrylamide gels
    • Wray, W., Boulikas, T., Wray, V.P., and Hancock, R. Silver staining of proteins in polyacrylamide gels. Anal Biochem 118, 197-203 (1981).
    • (1981) Anal Biochem , vol.118 , pp. 197-203
    • Wray, W.1    Boulikas, T.2    Wray, V.P.3    Hancock, R.4
  • 71
    • 0024584321 scopus 로고
    • Beta gamma-subunit of bovine transducin composed of two components with distinctive gamma-subunits
    • Fukada, Y., Ohguro, H., Saito, T., Yoshizawa, T., and Akino, T. Beta gamma-subunit of bovine transducin composed of two components with distinctive gamma-subunits. J Biol Chem 264, 5937-43 (1989).
    • (1989) J Biol Chem , vol.264 , pp. 5937-5943
    • Fukada, Y.1    Ohguro, H.2    Saito, T.3    Yoshizawa, T.4    Akino, T.5
  • 72
    • 0023114097 scopus 로고
    • Diurnal expression of transducin mRNA and translocation of transducin in rods of rat retina
    • Brann, M.R. and Cohen, L.V. Diurnal expression of transducin mRNA and translocation of transducin in rods of rat retina. Science 235, 585-7 (1987).
    • (1987) Science , vol.235 , pp. 585-587
    • Brann, M.R.1    Cohen, L.V.2
  • 73
    • 0023650261 scopus 로고
    • Light-stimulated protein movement in rod photoreceptor cells of the rat retina
    • Philp, N.J., Chang, W., and Long, K. Light-stimulated protein movement in rod photoreceptor cells of the rat retina. FEBS Lett 225, 127-32 (1987).
    • (1987) FEBS Lett , vol.225 , pp. 127-132
    • Philp, N.J.1    Chang, W.2    Long, K.3
  • 74
    • 0023697234 scopus 로고
    • Light-dependent subcellular movement of photoreceptor proteins
    • Whelan, J.P. and McGinnis, J.F. Light-dependent subcellular movement of photoreceptor proteins. J Neurosci Res 20, 263-70 (1988).
    • (1988) J Neurosci Res , vol.20 , pp. 263-270
    • Whelan, J.P.1    McGinnis, J.F.2
  • 75
    • 0026354572 scopus 로고
    • Adaptive changes in visual cell transduction protein levels:Effect of light
    • Organisciak, D.T. et al. Adaptive changes in visual cell transduction protein levels:Effect of light. Exp Eye Res 53, 773-9 (1991).
    • (1991) Exp Eye Res , vol.53 , pp. 773-779
    • Organisciak, D.T.1
  • 76
    • 0037187644 scopus 로고    scopus 로고
    • Massive light-driven translocation of transducin between the two major compartments of rod cells: A novel mechanism of light adaptation
    • Sokolov, M. et al. Massive light-driven translocation of transducin between the two major compartments of rod cells: A novel mechanism of light adaptation. Neuron 34, 95-106 (2002).
    • (2002) Neuron , vol.34 , pp. 95-106
    • Sokolov, M.1
  • 77
    • 0142166437 scopus 로고    scopus 로고
    • Protein translocation in photoreceptor light adaptation: A common theme in vertebrate and invertebrate vision
    • PE43 (2003)
    • Arshavsky, V.Y. Protein translocation in photoreceptor light adaptation: A common theme in vertebrate and invertebrate vision. Sci STKE 2003, PE43 (2003).
    • (2003) Sci STKE
    • Arshavsky, V.Y.1
  • 78
    • 20444383209 scopus 로고    scopus 로고
    • Light-dependent redistribution of arrestin in vertebrate rods is an energy- independent process governed by protein-protein interactions
    • Nair, K.S. et al. Light-dependent redistribution of arrestin in vertebrate rods is an energy- independent process governed by protein-protein interactions. Neuron 46, 555-67 (2005).
    • (2005) Neuron , vol.46 , pp. 555-567
    • Nair, K.S.1
  • 79
    • 0038071520 scopus 로고    scopus 로고
    • Light-dependent redistribution of visual arrestins and transducin subunits in mice with defective phototransduction
    • Zhang, H. et al. Light-dependent redistribution of visual arrestins and transducin subunits in mice with defective phototransduction. Mol Vis 9, 231-7 (2003).
    • (2003) Mol Vis , vol.9 , pp. 231-237
    • Zhang, H.1
  • 80
    • 3242706927 scopus 로고    scopus 로고
    • Myosin III illuminates the mechanism of arrestin translocation
    • Strissel, K.J. and Arshavsky, V.Y. Myosin III illuminates the mechanism of arrestin translocation. Neuron 43, 2-4 (2004).
    • (2004) Neuron , vol.43 , pp. 2-4
    • Strissel, K.J.1    Arshavsky, V.Y.2
  • 81
    • 3242730441 scopus 로고    scopus 로고
    • Light-dependent translocation of visual arrestin regulated by the NINAC myosin III
    • Lee, S.J. and Montell, C. Light-dependent translocation of visual arrestin regulated by the NINAC myosin III. Neuron 43, 95-103 (2004).
    • (2004) Neuron , vol.43 , pp. 95-103
    • Lee, S.J.1    Montell, C.2
  • 82
    • 23844444496 scopus 로고    scopus 로고
    • Recoverin undergoes light-dependent intracellular translocation in rod photoreceptors
    • Strissel, K.J. et al. Recoverin undergoes light-dependent intracellular translocation in rod photoreceptors. J Biol Chem 280, 29250-5 (2005).
    • (2005) J Biol Chem , vol.280 , pp. 29250-29255
    • Strissel, K.J.1
  • 84
    • 52249116687 scopus 로고    scopus 로고
    • 1st ed. eds. Hollyfield, J.G., Anderson, R.E., and LaVail, M.M. Springer
    • Retinal Degenerative Diseases 1st ed. eds. Hollyfield, J.G., Anderson, R.E., and LaVail, M.M. Springer, 2006.
    • (2006) Retinal Degenerative Diseases
  • 85
    • 0037387322 scopus 로고    scopus 로고
    • Rhodopsin controls a conformational switch on the transducin gamma subunit
    • Kisselev, O.G. and Downs, M.A. Rhodopsin controls a conformational switch on the transducin gamma subunit. Structure (Camb) 11, 367-73 (2003).
    • (2003) Structure (Camb) , vol.11 , pp. 367-373
    • Kisselev, O.G.1    Downs, M.A.2
  • 86
    • 0032516098 scopus 로고    scopus 로고
    • Light-activated rhodopsin induces structural binding motif in G protein alpha subunit
    • Kisselev, O.G. et al. Light-activated rhodopsin induces structural binding motif in G protein alpha subunit. Proc Natl Acad Sci USA 95, 4270-5 (1998).
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 4270-4275
    • Kisselev, O.G.1


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