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Volumn 20, Issue 1, 1998, Pages 95-102

RGS9, a GTPase accelerator for phototransduction

Author keywords

[No Author keywords available]

Indexed keywords

GUANOSINE TRIPHOSPHATASE;

EID: 0031936503     PISSN: 08966273     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0896-6273(00)80437-7     Document Type: Article
Times cited : (314)

References (46)
  • 2
    • 0027430227 scopus 로고
    • A GTPase-accelerating factor for transducin, distinct from its effector cGMP phosphodiesterase, in rod outer segment membranes
    • Angleson, J.K., and Wensel, T.G. (1993). A GTPase-accelerating factor for transducin, distinct from its effector cGMP phosphodiesterase, in rod outer segment membranes. Neuron 11, 939-949.
    • (1993) Neuron , vol.11 , pp. 939-949
    • Angleson, J.K.1    Wensel, T.G.2
  • 3
    • 0028340572 scopus 로고
    • Enhancement of rod outer segment GTPase accelerating protein activity by the inhibitory subunit of cGMP phosphodiesterase
    • Angleson, J.K., and Wensel, T.G. (1994). Enhancement of rod outer segment GTPase accelerating protein activity by the inhibitory subunit of cGMP phosphodiesterase. J. Biol. Chem. 269, 16290-16296.
    • (1994) J. Biol. Chem. , vol.269 , pp. 16290-16296
    • Angleson, J.K.1    Wensel, T.G.2
  • 4
    • 0027282176 scopus 로고
    • GTP hydrolysis by purified alpha-subunit of transducin and its complex with the cyclic GMP phosphodiesterase inhibitor
    • Antonny, B., Otto-Bruc, A., Chabre, M., and Vuong, T.M. (1993). GTP hydrolysis by purified alpha-subunit of transducin and its complex with the cyclic GMP phosphodiesterase inhibitor. Biochemistry 32, 8646-8653.
    • (1993) Biochemistry , vol.32 , pp. 8646-8653
    • Antonny, B.1    Otto-Bruc, A.2    Chabre, M.3    Vuong, T.M.4
  • 5
    • 0026742007 scopus 로고
    • Regulation of deactivation of photoreceptor G protein by its target enzyme and cGMP
    • Arshavsky, V.Y., and Bownds, M.D. (1992). Regulation of deactivation of photoreceptor G protein by its target enzyme and cGMP. Nature 357, 416-417.
    • (1992) Nature , vol.357 , pp. 416-417
    • Arshavsky, V.Y.1    Bownds, M.D.2
  • 6
    • 0023657956 scopus 로고
    • On the role of transducin GTPase in the quenching of a phosphodiesterase cascade of vision
    • Arshavsky, V.Y., Antoch, M.P., and Philippov, P.P. (1987). On the role of transducin GTPase in the quenching of a phosphodiesterase cascade of vision. FEBS Lett. 224, 19-22.
    • (1987) FEBS Lett. , vol.224 , pp. 19-22
    • Arshavsky, V.Y.1    Antoch, M.P.2    Philippov, P.P.3
  • 7
    • 0024406813 scopus 로고
    • Transducin GTPase provides for rapid quenching of the cGMP cascade in rod outer segments
    • Arshavsky, V.Y., Antoch, M.P., Lukjanov, K.A., and Philippov, P.P. (1989). Transducin GTPase provides for rapid quenching of the cGMP cascade in rod outer segments. FEBS Lett. 250, 353-356.
    • (1989) FEBS Lett. , vol.250 , pp. 353-356
    • Arshavsky, V.Y.1    Antoch, M.P.2    Lukjanov, K.A.3    Philippov, P.P.4
  • 9
    • 0021646399 scopus 로고
    • The photocurrent, noise and spectral sensitivity of rods of the monkey Macaca fascicularis
    • Baylor, D.A., Nunn, B.J., and Schnapf, J.L. (1984). The photocurrent, noise and spectral sensitivity of rods of the monkey Macaca fascicularis. J. Physiol. 357, 575-607.
    • (1984) J. Physiol. , vol.357 , pp. 575-607
    • Baylor, D.A.1    Nunn, B.J.2    Schnapf, J.L.3
  • 12
    • 0029843409 scopus 로고    scopus 로고
    • RGS-r, a retinal specific RGS protein, binds an intermediate conformation of transducin and enhances recycling
    • Chen, C.K., Wieland, T., and Simon, M.I. (1996). RGS-r, a retinal specific RGS protein, binds an intermediate conformation of transducin and enhances recycling. Proc. Natl. Acad. Sci. USA 93, 12885-12889.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 12885-12889
    • Chen, C.K.1    Wieland, T.2    Simon, M.I.3
  • 13
    • 0030933718 scopus 로고    scopus 로고
    • Characterization of a novel mammalian RGS protein that binds to G alpha proteins and inhibits pheromone signaling in yeast
    • Chen, C., Zheng, B., Han, J., and Lin, S.C. (1997). Characterization of a novel mammalian RGS protein that binds to G alpha proteins and inhibits pheromone signaling in yeast. J. Biol. Chem. 272, 8679-8685.
    • (1997) J. Biol. Chem. , vol.272 , pp. 8679-8685
    • Chen, C.1    Zheng, B.2    Han, J.3    Lin, S.C.4
  • 14
    • 0029559788 scopus 로고
    • GAIP, a protein that specifically interacts with the trimeric G protein G alpha i3, is a member of a protein family with a highly conserved core domain
    • De Vries, L., Mousli, M., Wurmser, A., and Farquhar, M.G. (1995). GAIP, a protein that specifically interacts with the trimeric G protein G alpha i3, is a member of a protein family with a highly conserved core domain. Proc. Natl. Acad. Sci. USA 92, 11916-11920.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 11916-11920
    • De Vries, L.1    Mousli, M.2    Wurmser, A.3    Farquhar, M.G.4
  • 15
    • 0030448762 scopus 로고    scopus 로고
    • GAIP is membrane-anchored by palmitoylation and interacts with the activated (GTP-bound) form of Gαi subunits
    • De Vries, L., Zlenko, Z., Hubler, L., Jones, T.L.Z., and Farquhar, M.E. (1996). GAIP is membrane-anchored by palmitoylation and interacts with the activated (GTP-bound) form of Gαi subunits. Proc. Natl. Acad. Sci. USA 93, 15203-15208.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 15203-15208
    • De Vries, L.1    Zlenko, Z.2    Hubler, L.3    Jones, T.L.Z.4    Farquhar, M.E.5
  • 16
    • 0029767982 scopus 로고    scopus 로고
    • SSt2, a negative regulator of pheromone signaling in the yeast Saccharomyces cerevisiae: Expression, localization and genetic interaction and physical association with Gpa1 (the G protein a subunit)
    • Dohlman, H.G., Song, J., Ma, D., Courchesne, W.Z., and Thorner, J. (1996). SSt2, a negative regulator of pheromone signaling in the yeast Saccharomyces cerevisiae: expression, localization and genetic interaction and physical association with Gpa1 (the G protein a subunit). Mol. Cell. Biol. 16, 5194-5209.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 5194-5209
    • Dohlman, H.G.1    Song, J.2    Ma, D.3    Courchesne, W.Z.4    Thorner, J.5
  • 17
    • 0023669174 scopus 로고
    • Retinal rod GTPase turnover rate increases with concentration: A key to the control of visual excitation?
    • Dratz, E.A., Lewis, J.W., Schaechter, L.E., Parker, K.R., and Kliger, D.S. (1987). Retinal rod GTPase turnover rate increases with concentration: a key to the control of visual excitation? Biochem. Biophys. Res. Commun. 146, 379-386.
    • (1987) Biochem. Biophys. Res. Commun. , vol.146 , pp. 379-386
    • Dratz, E.A.1    Lewis, J.W.2    Schaechter, L.E.3    Parker, K.R.4    Kliger, D.S.5
  • 18
    • 0030029727 scopus 로고    scopus 로고
    • Inhibition of G protein-mediated MAP kinase activation by a new mammalian gene family
    • Druey, K.M., Blumer, K.J., Kang, V.H., and Kehrl, J.H. (1996). Inhibition of G protein-mediated MAP kinase activation by a new mammalian gene family. Nature 379, 742-746.
    • (1996) Nature , vol.379 , pp. 742-746
    • Druey, K.M.1    Blumer, K.J.2    Kang, V.H.3    Kehrl, J.H.4
  • 19
    • 0030953032 scopus 로고    scopus 로고
    • The core domain of a new retina specific RGS protein stimulates the GTPase activity of transducin in vitro
    • Faurobert, E., and Hurley, J.B. (1997). The core domain of a new retina specific RGS protein stimulates the GTPase activity of transducin in vitro. Proc. Natl. Acad. Sci. USA 94, 2945-2950.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 2945-2950
    • Faurobert, E.1    Hurley, J.B.2
  • 20
    • 0030764226 scopus 로고    scopus 로고
    • Regulators of G protein signaling proteins: Region-specific expression of nine subtypes in the brain
    • Gold, S.J., Ni, Y.G., Dohlman, H.G., and Nestler, E.J. (1997). Regulators of G protein signaling proteins: region-specific expression of nine subtypes in the brain. J. Neurosci. 17, 8024-8037.
    • (1997) J. Neurosci. , vol.17 , pp. 8024-8037
    • Gold, S.J.1    Ni, Y.G.2    Dohlman, H.G.3    Nestler, E.J.4
  • 22
    • 85025386613 scopus 로고
    • Intermittent stimulation by light III. The relationship between intensity and critical fusion frequency for different retinal locations
    • Hecht, S., and Verrijp, C.D. (1933). Intermittent stimulation by light III. The relationship between intensity and critical fusion frequency for different retinal locations. J. Gen. Physiol. 17, 251-268.
    • (1933) J. Gen. Physiol. , vol.17 , pp. 251-268
    • Hecht, S.1    Verrijp, C.D.2
  • 23
    • 0031017573 scopus 로고    scopus 로고
    • RGS4 and GAIP are GTPase-activating proteins for Gqα and block activation of phospholipase Cβ by γ-thio-GTP-Gqα
    • Hepler, J.R., Berman, A.G., Gilman, A.G., and Kazasa, T. (1997). RGS4 and GAIP are GTPase-activating proteins for Gqα and block activation of phospholipase Cβ by γ-thio-GTP-Gqα. Proc. Natl. Acad. Sci. USA 94, 428-432.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 428-432
    • Hepler, J.R.1    Berman, A.G.2    Gilman, A.G.3    Kazasa, T.4
  • 24
    • 0029830014 scopus 로고    scopus 로고
    • RGS10 is a selective activator of G alpha i GTPase activity
    • Hunt, T.W., Fields, T.A., Casey, P.J., and Peralta, E.G. (1996). RGS10 is a selective activator of G alpha i GTPase activity. Nature 383, 175-177.
    • (1996) Nature , vol.383 , pp. 175-177
    • Hunt, T.W.1    Fields, T.A.2    Casey, P.J.3    Peralta, E.G.4
  • 25
    • 0030032001 scopus 로고    scopus 로고
    • EGL-10 regulates G protein signaling in the C. elegans nervous system and shares a conserved domain with many mammalian proteins
    • Koelle, M.R., and Horvitz, H.R. (1996). EGL-10 regulates G protein signaling in the C. elegans nervous system and shares a conserved domain with many mammalian proteins. Cell 84, 115-125.
    • (1996) Cell , vol.84 , pp. 115-125
    • Koelle, M.R.1    Horvitz, H.R.2
  • 26
    • 0023813716 scopus 로고
    • Photocurrents of cone photoreceptors of the golden-mantled ground squirrel
    • Kraft, T.W. (1988). Photocurrents of cone photoreceptors of the golden-mantled ground squirrel. J. Physiol. 404, 199-213.
    • (1988) J. Physiol. , vol.404 , pp. 199-213
    • Kraft, T.W.1
  • 27
    • 0026505707 scopus 로고
    • A quantitative account of the activation steps involved in phototransduction in amphibian photoreceptors
    • Lamb, T.D., and Pugh, E.N., Jr. (1992). A quantitative account of the activation steps involved in phototransduction in amphibian photoreceptors. J. Physiol. 449, 719-758.
    • (1992) J. Physiol. , vol.449 , pp. 719-758
    • Lamb, T.D.1    Pugh E.N., Jr.2
  • 28
    • 0030050756 scopus 로고    scopus 로고
    • Recovery phase of the murine rod photoresponse reconstructed from electroretinographic recordings
    • Lyubarsky, A.L., and Pugh, E.N., 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 E.N., Jr.2
  • 30
    • 0030859014 scopus 로고    scopus 로고
    • Regulation of transducin GTPase activity by human retinal RGS
    • Natochin, M., Granovsky, A.E., and Artemeyev, N.O. (1997). Regulation of transducin GTPase activity by human retinal RGS. J. Biol. Chem. 272, 17444-17449.
    • (1997) J. Biol. Chem. , vol.272 , pp. 17444-17449
    • Natochin, M.1    Granovsky, A.E.2    Artemeyev, N.O.3
  • 32
    • 85030305722 scopus 로고    scopus 로고
    • The kinetics of recovery of the dark-adapted salamander rod photoresponse
    • Nikonov, S., Engheta, N., and Pugh, E.N., Jr. (1998). The kinetics of recovery of the dark-adapted salamander rod photoresponse. J. Gen. Physiol. 111, 1-31.
    • (1998) J. Gen. Physiol. , vol.111 , pp. 1-31
    • Nikonov, S.1    Engheta, N.2    Pugh E.N., Jr.3
  • 33
    • 0028605198 scopus 로고
    • Modulation of the GTPase activity of transducin. Kinetic studies of reconstituted systems
    • Otto-Bruc, A., Antonny, B., and Vuong, T.M. (1994). Modulation of the GTPase activity of transducin. Kinetic studies of reconstituted systems. Biochemistry 33, 15215-15222.
    • (1994) Biochemistry , vol.33 , pp. 15215-15222
    • Otto-Bruc, A.1    Antonny, B.2    Vuong, T.M.3
  • 34
    • 0030200001 scopus 로고    scopus 로고
    • Pleckstrin's repeat performance: A novel domain in G protein signaling?
    • Ponting, C.P., and Bork, P. (1996). Pleckstrin's repeat performance: a novel domain in G protein signaling? Trends Biochem. Sci. 21, 245-246.
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 245-246
    • Ponting, C.P.1    Bork, P.2
  • 35
    • 0027440954 scopus 로고
    • Enhancement by phosphodiesterase subunits of the rate of GTP hydrolysis by transducin in bovine retinal rods. Essential role of the phosphodiesterase catalytic core
    • Pages, F., Deterre, P., and Pfister, C. (1993). Enhancement by phosphodiesterase subunits of the rate of GTP hydrolysis by transducin in bovine retinal rods. Essential role of the phosphodiesterase catalytic core. J. Biol. Chem. 268, 26358-26364.
    • (1993) J. Biol. Chem. , vol.268 , pp. 26358-26364
    • Pages, F.1    Deterre, P.2    Pfister, C.3
  • 36
    • 0016253492 scopus 로고
    • Rhodopsin content in the outer segment membranes of bovine and frog retinal rods
    • Papermaster, D.S., and Dreyer, W.J. (1974). Rhodopsin content in the outer segment membranes of bovine and frog retinal rods. Biochemistry 13, 2438-2444.
    • (1974) Biochemistry , vol.13 , pp. 2438-2444
    • Papermaster, D.S.1    Dreyer, W.J.2
  • 38
    • 0027407602 scopus 로고
    • Amplification and kinetics of the activation steps in phototransduction
    • Pugh, E.N., Jr., and Lamb, T.D. (1993). Amplification and kinetics of the activation steps in phototransduction. Biochim. Biophys. Acta 1141, 111-149.
    • (1993) Biochim. Biophys. Acta , vol.1141 , pp. 111-149
    • Pugh E.N., Jr.1    Lamb, T.D.2
  • 39
    • 0030867457 scopus 로고    scopus 로고
    • G protein deactivation is rate-limiting for shut-off of the phototransduction cascade
    • Sagoo, M.S., and Lagnado, L., (1997). G protein deactivation is rate-limiting for shut-off of the phototransduction cascade. Nature 389, 392-395.
    • (1997) Nature , vol.389 , pp. 392-395
    • Sagoo, M.S.1    Lagnado, L.2
  • 40
    • 0025163495 scopus 로고
    • Visual transduction in cones of the monkey Macaca fascicularis
    • Schnapf, J.L., Nunn, B.J., Meister, M., and Baylor, D.A. (1990). Visual transduction in cones of the monkey Macaca fascicularis. J. Physiol. 427, 681-713.
    • (1990) J. Physiol. , vol.427 , pp. 681-713
    • Schnapf, J.L.1    Nunn, B.J.2    Meister, M.3    Baylor, D.A.4
  • 41
    • 0025951192 scopus 로고
    • Molecular mechanism of GTP hydrolysis by bovine transducin: Pre-steady-state kinetic analysis
    • Ting, T.D., and Ho, Y.-K. (1991). Molecular mechanism of GTP hydrolysis by bovine transducin: pre-steady-state kinetic analysis. Biochemistry 30, 8996-9007.
    • (1991) Biochemistry , vol.30 , pp. 8996-9007
    • Ting, T.D.1    Ho, Y.-K.2
  • 42
    • 0025325738 scopus 로고
    • Subsecond deactivation of transducin by endogenous GTP hydrolysis
    • Vuong, T.M., and Chabre, M. (1990). Subsecond deactivation of transducin by endogenous GTP hydrolysis. Nature 335, 71-74.
    • (1990) Nature , vol.335 , pp. 71-74
    • Vuong, T.M.1    Chabre, M.2
  • 43
    • 0025938677 scopus 로고
    • Deactivation kinetics of the transduction cascade of vision
    • Vuong, T.M., and Chabre, M. (1991). Deactivation kinetics of the transduction cascade of vision. Proc. Natl. Acad. Sci. USA 88, 9813-9817.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 9813-9817
    • Vuong, T.M.1    Chabre, M.2
  • 44
    • 0029808079 scopus 로고    scopus 로고
    • RGS family members: GTPase-activating proteins for heterotrimeric G protein alpha-subunits
    • Watson, N., Linder, M.E., Druey, K.M., Kehrl, J.H., and Blumer, K.J. (1996). RGS family members: GTPase-activating proteins for heterotrimeric G protein alpha-subunits. Nature 383, 172-175.
    • (1996) Nature , vol.383 , pp. 172-175
    • Watson, N.1    Linder, M.E.2    Druey, K.M.3    Kehrl, J.H.4    Blumer, K.J.5
  • 45
    • 0030975464 scopus 로고    scopus 로고
    • The retinal specific protein RGS-r competes with the gamma subunit of cGMP phosphodiesterase for the alpha subunit of transducin and facilitates signal termination
    • Wieland, T., Chen, C.K., and Simon, M.I. (1997). The retinal specific protein RGS-r competes with the gamma subunit of cGMP phosphodiesterase for the alpha subunit of transducin and facilitates signal termination. J. Biol. Chem. 272, 8853-8856.
    • (1997) J. Biol. Chem. , vol.272 , pp. 8853-8856
    • Wieland, T.1    Chen, C.K.2    Simon, M.I.3
  • 46
    • 0027468935 scopus 로고
    • Regulation of G protein function by an effector in GTP-dependent signal transduction. An inhibitory subunit of cGMP phosphodiesterase inhibits GTP hydrolysis by transducin in vertebrate rod photoreceptors
    • Yamazaki, A., Yamazaki, M., Tsuboi, S., Kishigami, A., Umbarger, K.O., Hutson, L.D., Madland, W.T., and Hayashi, F. (1993). Regulation of G protein function by an effector in GTP-dependent signal transduction. An inhibitory subunit of cGMP phosphodiesterase inhibits GTP hydrolysis by transducin in vertebrate rod photoreceptors. J. Biol. Chem. 268, 8899-8907.
    • (1993) J. Biol. Chem. , vol.268 , pp. 8899-8907
    • Yamazaki, A.1    Yamazaki, M.2    Tsuboi, S.3    Kishigami, A.4    Umbarger, K.O.5    Hutson, L.D.6    Madland, W.T.7    Hayashi, F.8


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