메뉴 건너뛰기




Volumn 91, Issue 3, 1997, Pages 375-383

Calmodulin regulation of drosophila light-activated channels and receptor function mediates termination of the light response in vivo

Author keywords

[No Author keywords available]

Indexed keywords

CALMODULIN;

EID: 0030665081     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0092-8674(00)80421-3     Document Type: Article
Times cited : (174)

References (59)
  • 1
    • 0030612593 scopus 로고    scopus 로고
    • InsP(3) receptor is essential for growth and differentiation but not for vision in Drosophila
    • Acharya, J.K., Jalink, K., Hardy, R.W., Hartenstein, V., and Zuker, C.S. (1997). lnsP(3) receptor is essential for growth and differentiation but not for vision in Drosophila. Neuron 18, 881-887.
    • (1997) Neuron , vol.18 , pp. 881-887
    • Acharya, J.K.1    Jalink, K.2    Hardy, R.W.3    Hartenstein, V.4    Zuker, C.S.5
  • 2
    • 0031036871 scopus 로고    scopus 로고
    • Calmodulin regulation of calcium stores in phototransduction of Drosophila
    • Arnon, A., Cook, B., Montell, C., Selinger, Z., and Minke, B. (1997). Calmodulin regulation of calcium stores in phototransduction of Drosophila. Science 275, 1119-1121.
    • (1997) Science , vol.275 , pp. 1119-1121
    • Arnon, A.1    Cook, B.2    Montell, C.3    Selinger, Z.4    Minke, B.5
  • 4
    • 0018333003 scopus 로고
    • Responses of retinal rods to single photons
    • Baylor, D.A., Lamb, T.D., and Yau, K.-W. (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
  • 5
    • 0023062987 scopus 로고
    • Inositol trisphosphate and diacylglycerol: Two interacting second messengers
    • Berridge, M.J. (1987). Inositol trisphosphate and diacylglycerol: two interacting second messengers. Annu. Rev. Biochem. 56, 159-193.
    • (1987) Annu. Rev. Biochem. , vol.56 , pp. 159-193
    • Berridge, M.J.1
  • 6
    • 0028826727 scopus 로고
    • Capacitative calcium entry
    • Berridge, M.J. (1995). Capacitative calcium entry. Biochem. J. 312, 1-11.
    • (1995) Biochem. J. , vol.312 , pp. 1-11
    • Berridge, M.J.1
  • 7
    • 0024297823 scopus 로고
    • Isolation of a putative phospholipase C gene of drosophila, norpA, and its role in phototransduction
    • Bloomquist, B., Shortridge, R., Schneuwly, S., Perdew, M., Montell, C., Steller, H., Rubin, G., and Pak, W. (1988). Isolation of a putative phospholipase C gene of Drosophila, norpA, and its role in phototransduction. Cell 54, 723-733.
    • (1988) Cell , vol.54 , pp. 723-733
    • Bloomquist, B.1    Shortridge, R.2    Schneuwly, S.3    Perdew, M.4    Montell, C.5    Steller, H.6    Rubin, G.7    Pak, W.8
  • 8
    • 0027401240 scopus 로고
    • Regulatory arrestin cycle secures the fidelity and maintenance of the photoreceptor cell
    • Byk, T., Bar-Yaacov, M., Doza, Y.N., Minke, B., and Selinger, Z. (1993). Regulatory arrestin cycle secures the fidelity and maintenance of the photoreceptor cell. Proc. Natl. Acad. Sci. USA 90, 1907-1911.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 1907-1911
    • Byk, T.1    Bar-Yaacov, M.2    Doza, Y.N.3    Minke, B.4    Selinger, Z.5
  • 9
    • 0031037164 scopus 로고    scopus 로고
    • Requirement for the PDZ domain protein, INAD, for localization of the TRP storeoperated channel to a signaling complex
    • Chevesich, J., Kreuz, A.J., and Montell, C. (1997). Requirement for the PDZ domain protein, INAD, for localization of the TRP storeoperated channel to a signaling complex. Neuron 18, 95-105.
    • (1997) Neuron , vol.18 , pp. 95-105
    • Chevesich, J.1    Kreuz, A.J.2    Montell, C.3
  • 10
    • 0028831997 scopus 로고
    • Calcium signaling
    • Clapham, D.E. (1995). Calcium signaling. Cell 80, 259-268.
    • (1995) Cell , vol.80 , pp. 259-268
    • Clapham, D.E.1
  • 12
    • 0014683485 scopus 로고
    • Abnormal electroretinogram from a Drosophila mutant
    • Cosens, D., and Manning, A. (1969). Abnormal electroretinogram from a Drosophila mutant. Nature 224, 285-287.
    • (1969) Nature , vol.224 , pp. 285-287
    • Cosens, D.1    Manning, A.2
  • 13
    • 0027316899 scopus 로고
    • Arrestin function in inactivation of G protein-coupled receptor rhodopsin in vivo
    • Dolph, P.J., Ranganathan R., Colley N.J., Hardy R.W., Socolich, M., and Zuker C.S. (1993). Arrestin function in inactivation of G protein-coupled receptor rhodopsin in vivo. Science 260, 1910-1916.
    • (1993) Science , vol.260 , pp. 1910-1916
    • Dolph, P.J.1    Ranganathan, R.2    Colley, N.J.3    Hardy, R.W.4    Socolich, M.5    Zuker, C.S.6
  • 14
    • 0025376141 scopus 로고
    • Drosophila melanogaster contains a single calmodulin gene. Further structure and expression studies
    • Doyle, K.E., Kovalick, G.E., Lee, E., and Beckingham, K. (1990). Drosophila melanogaster contains a single Calmodulin gene. Further structure and expression studies. J. Molec. Biol. 213, 599-605.
    • (1990) J. Molec. Biol. , vol.213 , pp. 599-605
    • Doyle, K.E.1    Kovalick, G.E.2    Lee, E.3    Beckingham, K.4
  • 15
    • 0025886689 scopus 로고
    • Whole-cell recordings of the light induced current in dissociated Drosophila photoreceptors - Evidence for feedback by calcium permeating the light-sensitive channels
    • Hardie, R. (1991). Whole-cell recordings of the light induced current in dissociated Drosophila photoreceptors - evidence for feedback by calcium permeating the light-sensitive channels. Proc. R. Soc. Lond. Biol. 245, 203-210.
    • (1991) Proc. R. Soc. Lond. Biol. , vol.245 , pp. 203-210
    • Hardie, R.1
  • 16
    • 0029923620 scopus 로고    scopus 로고
    • 2+ concentration in Drosophila photoreceptors
    • 2+ concentration in Drosophila photoreceptors. J. Neurosci. 16, 2924-2933.
    • (1996) J. Neurosci. , vol.16 , pp. 2924-2933
    • Hardie, R.C.1
  • 17
    • 0026583241 scopus 로고
    • 2+ channel in Drosophila photoreceptors
    • 2+ channel in Drosophila photoreceptors. Neuron 8, 643-651.
    • (1992) Neuron , vol.8 , pp. 643-651
    • Hardie, R.C.1    Minke, B.2
  • 20
    • 0030841932 scopus 로고    scopus 로고
    • Functional equivalence of native light-sensitive channels in the Drosophila trp(301) mutant and TRPL cation channels expressed in a stably transfected Drosophila cell line
    • Hardie, R.C., Reuss, H., Lansdell, S.J., and Millar, N.S. (1997). Functional equivalence of native light-sensitive channels in the Drosophila trp(301) mutant and TRPL cation channels expressed in a stably transfected Drosophila cell line. Cell Calcium 21, 431-440.
    • (1997) Cell Calcium , vol.21 , pp. 431-440
    • Hardie, R.C.1    Reuss, H.2    Lansdell, S.J.3    Millar, N.S.4
  • 22
    • 0030229149 scopus 로고    scopus 로고
    • Differential effects of NINAC proteins (p132 and p174) on light-activated currents in Drosophila photoreceptors
    • Hofstee, C.A., Henderson, S., Hardie, R.C., and Stavenga, D.G. (1996). Differential effects of NINAC proteins (p132 and p174) on light-activated currents in Drosophila photoreceptors. Vis. Neurosci. 13, 897-906.
    • (1996) Vis. Neurosci. , vol.13 , pp. 897-906
    • Hofstee, C.A.1    Henderson, S.2    Hardie, R.C.3    Stavenga, D.G.4
  • 23
    • 0031019067 scopus 로고    scopus 로고
    • Calcium/calmodulin-dependent kinase II phosphorylates Drosophila visual arrestin
    • Kahn, E.S., and Matsumoto, H. (1997). Calcium/calmodulin-dependent kinase II phosphorylates Drosophila visual arrestin. J. Neurochem. 68, 169-175.
    • (1997) J. Neurochem. , vol.68 , pp. 169-175
    • Kahn, E.S.1    Matsumoto, H.2
  • 24
    • 0021473294 scopus 로고
    • Analysis of P transposable element functions in Drosophila
    • Karess, R.E., and Rubin, G.M. (1984). Analysis of P transposable element functions in Drosophila. Cell 38, 135-146.
    • (1984) Cell , vol.38 , pp. 135-146
    • Karess, R.E.1    Rubin, G.M.2
  • 26
    • 0028047175 scopus 로고
    • Calcium controls light-triggered formation of catalytically active rhodopsin
    • Lagnado, L., and Baylor, D.A. (1994). Calcium controls light-triggered formation of catalytically active rhodopsin. Nature 367, 273-277.
    • (1994) Nature , vol.367 , pp. 273-277
    • Lagnado, L.1    Baylor, D.A.2
  • 27
    • 0025633502 scopus 로고
    • dgq: A Drosophila gene encoding a visual system-specific Ga molecule
    • Lee, Y.-J., Dobbs, M.B., Verardi, M.L., and Hyde, D.R. (1990). dgq: a Drosophila gene encoding a visual system-specific Ga molecule. Neuron 5, 889-898.
    • (1990) Neuron , vol.5 , pp. 889-898
    • Lee, Y.-J.1    Dobbs, M.B.2    Verardi, M.L.3    Hyde, D.R.4
  • 28
    • 0025679166 scopus 로고
    • Isolation of a novel visual system-specific arrestin: An in vivo substrate for light-dependent phosphorylation
    • LeVine, H.D., Smith, D.P., Whitney, M., Malicki, D.M., Dolph, P.J., Smith, G.F., Burkhart, W., and Zuker, C.S. (1990). Isolation of a novel visual system-specific arrestin: an in vivo substrate for light-dependent phosphorylation. Mech. Dev. 33, 19-25.
    • (1990) Mech. Dev. , vol.33 , pp. 19-25
    • LeVine, H.D.1    Smith, D.P.2    Whitney, M.3    Malicki, D.M.4    Dolph, P.J.5    Smith, G.F.6    Burkhart, W.7    Zuker, C.S.8
  • 30
    • 0025830524 scopus 로고
    • Phosrestins I and II: Arrestin homologs which undergo differential light-induced phosphorylation in the Drosophila photoreceptors in vivo
    • Matsumoto, H., and Yamada,T. (1991). Phosrestins I and II: arrestin homologs which undergo differential light-induced phosphorylation in the Drosophila photoreceptors in vivo. Biochem. Biophys. Res. Comm. 177, 1306-1312.
    • (1991) Biochem. Biophys. Res. Comm. , vol.177 , pp. 1306-1312
    • Matsumoto, H.1    Yamada, T.2
  • 31
    • 0028244771 scopus 로고
    • Phosrestin I undergoes the earliest light-induced phosphorylation by a calcium/calmodulin-dependent protein kinase in Drosophila photoreceptors
    • Matsumoto, H., Kurien, B.T., Takagi, Y., Kahn, E.S., Kinumi, T., Komori, N., Yamada, T., Hayashi, F., Isono, K., and Pak, W.L. (1994). Phosrestin I undergoes the earliest light-induced phosphorylation by a calcium/calmodulin-dependent protein kinase in Drosophila photoreceptors. Neuron 12, 997-1010.
    • (1994) Neuron , vol.12 , pp. 997-1010
    • Matsumoto, H.1    Kurien, B.T.2    Takagi, Y.3    Kahn, E.S.4    Kinumi, T.5    Komori, N.6    Yamada, T.7    Hayashi, F.8    Isono, K.9    Pak, W.L.10
  • 32
    • 0030218120 scopus 로고    scopus 로고
    • The roles of TRP and calcium in regulating photoreceptor function in Drosophila
    • Minke, B., and Selinger, Z. (1996). The roles of TRP and calcium in regulating photoreceptor function in Drosophila. Curr. Opin. Neurobiol. 6, 459-466.
    • (1996) Curr. Opin. Neurobiol. , vol.6 , pp. 459-466
    • Minke, B.1    Selinger, Z.2
  • 33
    • 0024642547 scopus 로고
    • Molecular characterization of the Drosophila trp locus: A putative integral membrane protein required for phototransduction
    • Montell, C., and Rubin, G.M. (1989). Molecular characterization of the Drosophila trp locus: a putative integral membrane protein required for phototransduction. Neuron 2, 1313-1323.
    • (1989) Neuron , vol.2 , pp. 1313-1323
    • Montell, C.1    Rubin, G.M.2
  • 34
    • 0022347577 scopus 로고
    • Rescue of the Drosophila phototransduction mutation trp by germline transformation
    • Montell, C., Jones, K., Hafen, E., and Rubin, G. (1985). Rescue of the Drosophila phototransduction mutation trp by germline transformation. Science 230, 1040-1043.
    • (1985) Science , vol.230 , pp. 1040-1043
    • Montell, C.1    Jones, K.2    Hafen, E.3    Rubin, G.4
  • 35
    • 0029927299 scopus 로고    scopus 로고
    • The Drosophila light-activated conductance is composed of the two channels TRP and TRPL
    • Niemeyer, B.A., Suzuki, E., Scott, K., Jalink, K., and Zuker, C.S. (1996). The Drosophila light-activated conductance is composed of the two channels TRP and TRPL. Cell 85, 651-659.
    • (1996) Cell , vol.85 , pp. 651-659
    • Niemeyer, B.A.1    Suzuki, E.2    Scott, K.3    Jalink, K.4    Zuker, C.S.5
  • 36
    • 0028284467 scopus 로고
    • The light response of Drosophila photoreceptors is accompanied by an increase in cellular calcium: Effects of specific mutations
    • Peretz, A., Suss-Toby, E., Rom-Glas, A., Arnon, A., Payne, R., and Minke, B. (1994). The light response of Drosophila photoreceptors is accompanied by an increase in cellular calcium: effects of specific mutations. Neuron 12, 1257-1267.
    • (1994) Neuron , vol.12 , pp. 1257-1267
    • Peretz, A.1    Suss-Toby, E.2    Rom-Glas, A.3    Arnon, A.4    Payne, R.5    Minke, B.6
  • 37
    • 0029094168 scopus 로고
    • Putative capacitative calcium entry channels - Expression of Drosophila trp and evidence for the existence of vertebrate homologs
    • Petersen, C.H., Bennett, D.L., Borgese, F., and Berridge, M.J. (1995). Putative capacitative calcium entry channels - expression of Drosophila trp and evidence for the existence of vertebrate homologs. Biochem. J. 311, 31-44.
    • (1995) Biochem. J. , vol.311 , pp. 31-44
    • Petersen, C.H.1    Bennett, D.L.2    Borgese, F.3    Berridge, M.J.4
  • 38
    • 0026508664 scopus 로고
    • Identification of a Drosophila gene encoding a calmodulin binding protein with homology to the trp phototransduction gene
    • Phillips, A.M., Bull, A., and Kelly, L.E. (1992). Identification of a Drosophila gene encoding a calmodulin binding protein with homology to the trp phototransduction gene. Neuron 8, 631-642.
    • (1992) Neuron , vol.8 , pp. 631-642
    • Phillips, A.M.1    Bull, A.2    Kelly, L.E.3
  • 39
    • 0027768695 scopus 로고
    • Dependence of calmodulin localization in the retina on the NINAC unconventional myosin
    • Porter, J.A., Yu, M., Doberstein, S.K., Pollard, T.D., and Montell, C. (1993). Dependence of calmodulin localization in the retina on the NINAC unconventional myosin. Science 262, 1038-1042.
    • (1993) Science , vol.262 , pp. 1038-1042
    • Porter, J.A.1    Yu, M.2    Doberstein, S.K.3    Pollard, T.D.4    Montell, C.5
  • 40
    • 0029114653 scopus 로고
    • Calmodulin binding to Drosophila NinaC required for termination of phototransduction
    • Porter, J.A., Minke, B., and Montell, C. (1995). Calmodulin binding to Drosophila NinaC required for termination of phototransduction. EMBO J. 14, 4450-4459.
    • (1995) EMBO J. , vol.14 , pp. 4450-4459
    • Porter, J.A.1    Minke, B.2    Montell, C.3
  • 41
    • 0027422088 scopus 로고
    • The signal for capacitative calcium entry
    • Putney, J.W., and Bird, G.S.J. (1993). The signal for capacitative calcium entry. Cell 75, 199-201.
    • (1993) Cell , vol.75 , pp. 199-201
    • Putney, J.W.1    Bird, G.S.J.2
  • 42
    • 0029017431 scopus 로고
    • Arrestin binding determines the rate of inactivation of the G protein-coupled receptor rhodopsin in vivo
    • Ranganathan, R., and Stevens, C.F. (1995). Arrestin binding determines the rate of inactivation of the G protein-coupled receptor rhodopsin in vivo. Cell 81, 841-848.
    • (1995) Cell , vol.81 , pp. 841-848
    • Ranganathan, R.1    Stevens, C.F.2
  • 43
    • 0026040308 scopus 로고
    • A Drosophila mutant defective in extracellular calcium dependent photoreceptor inactivation and rapid desensitization
    • Ranganathan, R., Harris, G.L., Stevens, C.F., and Zuker, C.S. (1991). A Drosophila mutant defective in extracellular calcium dependent photoreceptor inactivation and rapid desensitization. Nature 354, 230-232.
    • (1991) Nature , vol.354 , pp. 230-232
    • Ranganathan, R.1    Harris, G.L.2    Stevens, C.F.3    Zuker, C.S.4
  • 44
    • 0027996645 scopus 로고
    • Cytosolic calcium transients: Spatial localization and role in Drosophila photoreceptor cell function
    • Ranganathan, R., Bacskai, B.J., Tsien, R.Y., and Zuker, C.S. (1994). Cytosolic calcium transients: spatial localization and role in Drosophila photoreceptor cell function. Neuron 13, 837-848.
    • (1994) Neuron , vol.13 , pp. 837-848
    • Ranganathan, R.1    Bacskai, B.J.2    Tsien, R.Y.3    Zuker, C.S.4
  • 46
    • 0028972614 scopus 로고
    • Gαq protein function in vivo: Genetic dissection of its role in photoreceptor cell physiology
    • Scott, K., Leslie, A., Sun, Y., Hardy, R., and Zuker, C. (1995). Gαq protein function in vivo: genetic dissection of its role in photoreceptor cell physiology. Neuron 15, 919-927.
    • (1995) Neuron , vol.15 , pp. 919-927
    • Scott, K.1    Leslie, A.2    Sun, Y.3    Hardy, R.4    Zuker, C.5
  • 47
    • 0026418433 scopus 로고
    • Photoreceptor deactivation and retinal degeneration mediated by a photoreceptor-specific protein kinase C
    • Smith, D.P., Ranganathan, R., Hardy, R.W., Marx, J., Tsuchida, T., and Zuker, C.S. (1991). Photoreceptor deactivation and retinal degeneration mediated by a photoreceptor-specific protein kinase C. Science 254, 1478-1484.
    • (1991) Science , vol.254 , pp. 1478-1484
    • Smith, D.P.1    Ranganathan, R.2    Hardy, R.W.3    Marx, J.4    Tsuchida, T.5    Zuker, C.S.6
  • 48
    • 0025907054 scopus 로고
    • The cyclophilin homolog ninaa is a tissue-specific integral membrane protein required for the proper synthesis of a subset of Drosophila rhodopsins
    • Stamnes, M.A., Shieh, B.-H., Chuman, L., Harris, G.L., and Zuker, C.S. (1991). The cyclophilin homolog ninaA is a tissue-specific integral membrane protein required for the proper synthesis of a subset of Drosophila rhodopsins. Cell 65, 219-227.
    • (1991) Cell , vol.65 , pp. 219-227
    • Stamnes, M.A.1    Shieh, B.-H.2    Chuman, L.3    Harris, G.L.4    Zuker, C.S.5
  • 49
    • 0025245420 scopus 로고
    • Calcium channels, stores, and oscillations
    • Tsien, R.W., and Tsien, R.Y. (1990). Calcium channels, stores, and oscillations. Annu. Rev. Cell Biol. 6, 715-760.
    • (1990) Annu. Rev. Cell Biol. , vol.6 , pp. 715-760
    • Tsien, R.W.1    Tsien, R.Y.2
  • 50
    • 0030835610 scopus 로고    scopus 로고
    • A multivalent PDZ-domain protein assembles signaling complexes in a G protein-coupled cascade
    • Tsunoda, S., Sierralta, J., Sun, Y.M., Bodner, R., Suzuki, E., Becker, A., Socolich, M., and Zuker, C.S. (1997). A multivalent PDZ-domain protein assembles signaling complexes in a G protein-coupled cascade. Nature V388, 243-249.
    • (1997) Nature , vol.V388 , pp. 243-249
    • Tsunoda, S.1    Sierralta, J.2    Sun, Y.M.3    Bodner, R.4    Suzuki, E.5    Becker, A.6    Socolich, M.7    Zuker, C.S.8
  • 51
    • 0029866944 scopus 로고    scopus 로고
    • Identification and characterization of two distinct calmodulin binding sites in theTrpl ion-channel of Drosophila melanogaster
    • Warr, C.G., and Kelly, L.E. (1996). Identification and characterization of two distinct calmodulin binding sites in theTrpl ion-channel of Drosophila melanogaster. Biochem. J. 314, 497-503.
    • (1996) Biochem. J. , vol.314 , pp. 497-503
    • Warr, C.G.1    Kelly, L.E.2
  • 53
    • 0027267041 scopus 로고
    • Analysis of genetic mosaics in developing and adult Drosophila tissues
    • Xu,T., and Rubin, G.M. (1993). Analysis of genetic mosaics in developing and adult Drosophila tissues. Development 117, 1223-1237.
    • (1993) Development , vol.117 , pp. 1223-1237
    • Xu, T.1    Rubin, G.M.2
  • 54
    • 0031587878 scopus 로고    scopus 로고
    • Coassembly of TRP and TRPL produces a distinct store-operated conductance
    • Xu, X.Z.S., Li, H.S., Guggino, W.B., and Montell, C. (1997). Coassembly of TRP and TRPL produces a distinct store-operated conductance. Cell V89, 1155-1164.
    • (1997) Cell , vol.V89 , pp. 1155-1164
    • Xu, X.Z.S.1    Li, H.S.2    Guggino, W.B.3    Montell, C.4
  • 57
    • 0020631375 scopus 로고
    • Defective phospholipid metabolism in the retinular cell membrane of norpA (no receptor potential) visual transduction mutants of Drosophila
    • Yoshioka, T., Inoue, H., and Hotta, Y. (1983). Defective Phospholipid metabolism in the retinular cell membrane of norpA (no receptor potential) visual transduction mutants of Drosophila. Biochem. Biophys. Res. Comm. 111, 567-573.
    • (1983) Biochem. Biophys. Res. Comm. , vol.111 , pp. 567-573
    • Yoshioka, T.1    Inoue, H.2    Hotta, Y.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.