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Volumn 33, Issue 5-6, 2003, Pages 385-393

TRP channels in Drosophila photoreceptors: The lipid connection

Author keywords

Arachidonic acid; Calcium influx; Diacylglycerol; Inositol lipids; Phospholipase C; Phototransduction; PIP2; PUFAs; rdgA

Indexed keywords

CALCIUM CHANNEL; CELL MEMBRANE PROTEIN; DIACYLGLYCEROL; DIACYLGLYCEROL KINASE; GUANINE NUCLEOTIDE BINDING PROTEIN; LIPID; PHOSPHATIDYLINOSITOL 4,5 BISPHOSPHATE; PHOSPHOLIPASE C; POLYUNSATURATED FATTY ACID; TRANSIENT RECEPTOR POTENTIAL CHANNEL; TRANSIENT RECEPTOR POTENTIAL CHANNEL PROTEIN; UNCLASSIFIED DRUG;

EID: 0037974491     PISSN: 01434160     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0143-4160(03)00051-4     Document Type: Review
Times cited : (28)

References (56)
  • 1
    • 0024642547 scopus 로고
    • Molecular characterization of Drosophila trp locus, a putative integral membrane protein required for phototransduction
    • C. Montell, G.M. Rubin, Molecular characterization of Drosophila trp locus, a putative integral membrane protein required for phototransduction, Neuron 2 (1989) 1313-1323.
    • (1989) Neuron , vol.2 , pp. 1313-1323
    • Montell, C.1    Rubin, G.M.2
  • 2
    • 0026583241 scopus 로고
    • 2+ channel in Drosophila photoreceptors
    • 2+ channel in Drosophila photoreceptors, Neurol 8 (1992) 643-651.
    • (1992) Neurol. , vol.8 , pp. 643-651
    • Hardie, R.C.1    Minke, B.2
  • 3
    • 0026508664 scopus 로고
    • Identification of a Drosophila gene encoding a calmodulin-binding protein with homology to the trp phototransduction gene
    • A.M. Phillips, A. Bull, L.E. Kelly, Identification of a Drosophila gene encoding a calmodulin-binding protein with homology to the trp phototransduction gene, Neuron 8 (1992) 631-642.
    • (1992) Neuron , vol.8 , pp. 631-642
    • Phillips, A.M.1    Bull, A.2    Kelly, L.E.3
  • 4
    • 0029927299 scopus 로고    scopus 로고
    • The Drosophila light-activated conductance is composed of the two channels TRP and TRPL
    • B.A. Niemeyer, E. Suzuki, K. Scott, K. Jalink, C.S. Zuker, The Drosophila light-activated conductance is composed of the two channels TRP and TRPL, Cell 85 (1996) 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
  • 5
    • 0031459042 scopus 로고    scopus 로고
    • In vivo analysis of the Drosophila light-sensitive channels, TRP and TRPL
    • H. Reuss, M.H. Mojet, S. Chyb, R.C. Hardie, In vivo analysis of the Drosophila light-sensitive channels, TRP and TRPL, Neuron 19 (1997) 1249-1259.
    • (1997) Neuron , vol.19 , pp. 1249-1259
    • Reuss, H.1    Mojet, M.H.2    Chyb, S.3    Hardie, R.C.4
  • 6
    • 0033623942 scopus 로고    scopus 로고
    • TRP gamma, a Drosophila TRP-related subunit, forms a regulated cation channel with TRPL
    • X.Z.S. Xu, F. Chien, A. Butler, L. Salkoff, C. Montell, TRP gamma, a Drosophila TRP-related subunit, forms a regulated cation channel with TRPL, Neuron 26 (2000) 647-657.
    • (2000) Neuron , vol.26 , pp. 647-657
    • Xu, X.Z.S.1    Chien, F.2    Butler, A.3    Salkoff, L.4    Montell, C.5
  • 7
    • 0030665081 scopus 로고    scopus 로고
    • Calmodulin regulation of Drosophila light-activated channels and receptor function mediates termination of the light response in vivo
    • K. Scott, Y.M. Sun, K. Beckingham, C.S. Zuker, Calmodulin regulation of Drosophila light-activated channels and receptor function mediates termination of the light response in vivo, Cell 91 (1997) 375-383.
    • (1997) Cell , vol.91 , pp. 375-383
    • Scott, K.1    Sun, Y.M.2    Beckingham, K.3    Zuker, C.S.4
  • 9
    • 0034177642 scopus 로고    scopus 로고
    • From worm to man: Three subfamilies of TRP channels
    • C. Harteneck, T.D. Plant, G. Schultz, From worm to man: three subfamilies of TRP channels, Trends Neurosci. 23 (2000) 159-166.
    • (2000) Trends Neurosci. , vol.23 , pp. 159-166
    • Harteneck, C.1    Plant, T.D.2    Schultz, G.3
  • 10
    • 0035838673 scopus 로고    scopus 로고
    • Physiology, phylogeny, and functions of the TRP superfamily of cation channels
    • (2001) RE1
    • C. Montell, Physiology, phylogeny, and functions of the TRP superfamily of cation channels, Sci. STKE 2001 (2001) RE1.
    • (2001) Sci. STKE
    • Montell, C.1
  • 12
    • 0035855910 scopus 로고    scopus 로고
    • Visual transduction in Drosophila
    • R.C. Hardie, P. Raghu, Visual transduction in Drosophila, Nature 413 (2001) 186-193.
    • (2001) Nature , vol.413 , pp. 186-193
    • Hardie, R.C.1    Raghu, P.2
  • 13
    • 0028819281 scopus 로고
    • 2+ facilitates and inactivates but does not directly excite light-sensitive channels in Drosophila photoreceptors
    • 2+ facilitates and inactivates but does not directly excite light-sensitive channels in Drosophila photoreceptors, J. Neurosci. 15 (1995) 889-902.
    • (1995) J. Neurosci. , vol.15 , pp. 889-902
    • Hardie, R.C.1
  • 15
    • 0027996645 scopus 로고
    • Cytosolic calcium transients: Spatial localization and role in Drosophila photoreceptor cell function
    • R. Ranganathan, B.J. Bacskai, R.Y. Tsien, C.S. Zuker, Cytosolic calcium transients: spatial localization and role in Drosophila photoreceptor cell function, Neuron 13 (1994) 837-848.
    • (1994) Neuron , vol.13 , pp. 837-848
    • Ranganathan, R.1    Bacskai, B.J.2    Tsien, R.Y.3    Zuker, C.S.4
  • 17
    • 0030612593 scopus 로고    scopus 로고
    • InsP(3) receptor is essential for growth and differentiation but not for vision in Drosophila
    • J.K. Acharya, K. Jalink, R.W. Hardy, V. Hartenstein, C.S. Zuker, InsP(3) receptor is essential for growth and differentiation but not for vision in Drosophila, Neuron 18 (1997) 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
  • 18
    • 0034705143 scopus 로고    scopus 로고
    • The ryanodine receptor is essential for larval development in Drosophila melanogaster
    • K.M.C. Sullivan, K. Scott, C.S. Zuker, G.M. Rubin, The ryanodine receptor is essential for larval development in Drosophila melanogaster, Proc. Natl. Acad. Sci. U.S.A. 97 (2000) 5942-5947.
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 5942-5947
    • Sullivan, K.M.C.1    Scott, K.2    Zuker, C.S.3    Rubin, G.M.4
  • 19
    • 0028284467 scopus 로고
    • The light response of Drosophila photoreceptors is accompanied by an increase in cellular calcium: Effects of specific mutations
    • A. Peretz, E. SussToby, A. RomGlas, A. Arnon, R. Payne, B. Minke, The light response of Drosophila photoreceptors is accompanied by an increase in cellular calcium: effects of specific mutations, Neuron 12 (1994) 1257-1267.
    • (1994) Neuron , vol.12 , pp. 1257-1267
    • Peretz, A.1    SussToby, E.2    RomGlas, A.3    Arnon, A.4    Payne, R.5    Minke, B.6
  • 20
    • 0029923620 scopus 로고    scopus 로고
    • 2+ concentration in Drosophila photoreceptors
    • 2+ concentration in Drosophila photoreceptors, J. Neurosci. 16 (1996) 2924-2933.
    • (1996) J. Neurosci. , vol.16 , pp. 2924-2933
    • Hardie, R.C.1
  • 21
    • 0034161517 scopus 로고    scopus 로고
    • Calcium transients in the rhabdomeres of dark- and light-adapted fly photoreceptor cells
    • J. Oberwinkler, D.G. Stavenga, Calcium transients in the rhabdomeres of dark- and light-adapted fly photoreceptor cells, J. Neurosci. 20 (2000) 1701-1709.
    • (2000) J. Neurosci. , vol.20 , pp. 1701-1709
    • Oberwinkler, J.1    Stavenga, D.G.2
  • 22
    • 0033082798 scopus 로고    scopus 로고
    • TRP and calcium stores in Drosophila phototransduction
    • B. Cook, B. Minke, TRP and calcium stores in Drosophila phototransduction, Cell Calcium 25 (1999) 161-171.
    • (1999) Cell Calcium , vol.25 , pp. 161-171
    • Cook, B.1    Minke, B.2
  • 24
    • 0024413045 scopus 로고
    • Chemical excitation and inactivation in photoreceptors of the fly mutants trp and nss
    • E. Suss, S. Barash, D.G. Stavenga, H. Stieve, Z. Selinger, B. Minke, Chemical excitation and inactivation in photoreceptors of the fly mutants trp and nss, J. Gen. Physiol. 94 (1989) 465-491.
    • (1989) J. Gen. Physiol. , vol.94 , pp. 465-491
    • Suss, E.1    Barash, S.2    Stavenga, D.G.3    Stieve, H.4    Selinger, Z.5    Minke, B.6
  • 26
    • 77956734477 scopus 로고    scopus 로고
    • Phototransduction mechanisms in microvillar and ciliary photoreceptors of invertebrates
    • D.G. Stavenga, W.J. de Grip, E.N. Pugh (Eds.), Elsevier
    • E. Nasi, M. del Pilar Gomez, R. Payne, Phototransduction mechanisms in microvillar and ciliary photoreceptors of invertebrates, in: D.G. Stavenga, W.J. de Grip, E.N. Pugh (Eds.), Handbook of Biological Physics, vol. 3, Elsevier, 2000, pp. 389-448.
    • (2000) Handbook of Biological Physics , vol.3 , pp. 389-448
    • Nasi, E.1    del Pilar Gomez, M.2    Payne, R.3
  • 28
    • 0026418433 scopus 로고
    • Photoreceptor deactivation and retinal degeneration mediated by a photoreceptor-specific protein-kinase-C
    • D.P. Smith, R. Ranganathan, R.W. Hardy, J. Marx, T. Tsuchida, C.S. Zuker, Photoreceptor deactivation and retinal degeneration mediated by a photoreceptor-specific protein-kinase-C, Science 254 (1991) 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
  • 30
    • 0036277884 scopus 로고    scopus 로고
    • Vanilloid and TRP channels: A family of lipid-gated cation channels
    • C.D. Benham, J.B. Davis, A.D. Randall, Vanilloid and TRP channels: a family of lipid-gated cation channels, Neuropharmacology 42 (2002) 873-888.
    • (2002) Neuropharmacology , vol.42 , pp. 873-888
    • Benham, C.D.1    Davis, J.B.2    Randall, A.D.3
  • 31
    • 0027429547 scopus 로고
    • Drosophila retinal degeneration A gene encodes an eye-specific diacylglycerol kinase with cysteine-rich zinc-finger motifs and ankyrin repeats
    • I. Masai, A. Okazaki, T. Hosoya, Y. Hotta, Drosophila retinal degeneration A gene encodes an eye-specific diacylglycerol kinase with cysteine-rich zinc-finger motifs and ankyrin repeats, Proc. Natl. Acad. Sci. U.S.A. 90 (1993) 11157-11161.
    • (1993) Proc. Natl. Acad. Sci. U.S.A. , vol.90 , pp. 11157-11161
    • Masai, I.1    Okazaki, A.2    Hosoya, T.3    Hotta, Y.4
  • 32
    • 0033597338 scopus 로고    scopus 로고
    • Mammalian diacylglycerol kinases, a family of lipid kinases with signaling functions
    • M.K. Topham, S.M. Prescott, Mammalian diacylglycerol kinases, a family of lipid kinases with signaling functions, J. Biol. Chem. 274 (1999) 11447-11450.
    • (1999) J. Biol. Chem. , vol.274 , pp. 11447-11450
    • Topham, M.K.1    Prescott, S.M.2
  • 33
    • 0017332739 scopus 로고
    • Hereditary retinal degeneration in Drosophila melanogaster. A mutant defect associated with the phototransduction process
    • W.A. Harris, W.S. Stark, Hereditary retinal degeneration in Drosophila melanogaster. A mutant defect associated with the phototransduction process, J. Gen. Physiol. 69 (1977) 261-291.
    • (1977) J. Gen. Physiol. , vol.69 , pp. 261-291
    • Harris, W.A.1    Stark, W.S.2
  • 34
    • 0024005966 scopus 로고
    • Structure of retinular cells in a Drosophila melanogaster visual mutant, Rdga, at early stages of degeneration
    • E. Matsumoto, K. Hirosawa, K. Takagawa, Y. Hotta, Structure of retinular cells in a Drosophila melanogaster visual mutant, Rdga, at early stages of degeneration, Cell Tissue Res. 252 (1988) 293-300.
    • (1988) Cell Tissue Res. , vol.252 , pp. 293-300
    • Matsumoto, E.1    Hirosawa, K.2    Takagawa, K.3    Hotta, Y.4
  • 35
    • 0033679832 scopus 로고    scopus 로고
    • Constitutive activity of the light-sensitive channels TRP and TRPL in the Drosophila diacylglycerol kinase mutant, rdgA
    • P. Raghu, K. Usher, S. Jonas, S. Chyb, A. Polyanovsky, R.C. Hardie, Constitutive activity of the light-sensitive channels TRP and TRPL in the Drosophila diacylglycerol kinase mutant, rdgA, Neuron 26 (2000) 169-179.
    • (2000) Neuron , vol.26 , pp. 169-179
    • Raghu, P.1    Usher, K.2    Jonas, S.3    Chyb, S.4    Polyanovsky, A.5    Hardie, R.C.6
  • 36
    • 0037079075 scopus 로고    scopus 로고
    • Molecular basis of amplification in Drosophila phototransduction. Roles for G protein, phospholipase C, and diacylglycerol kinase
    • R.C. Hardie, F. Martin, G.W. Cochrane, M. Juusola, P. Georgiev, P. Raghu, Molecular basis of amplification in Drosophila phototransduction. Roles for G protein, phospholipase C, and diacylglycerol kinase, Neuron 36 (2002) 689-701.
    • (2002) Neuron , vol.36 , pp. 689-701
    • Hardie, R.C.1    Martin, F.2    Cochrane, G.W.3    Juusola, M.4    Georgiev, P.5    Raghu, P.6
  • 38
    • 0032558776 scopus 로고    scopus 로고
    • Assembly of the Drosophila phototransduction cascade into a signalling complex shapes elementary responses
    • K. Scott, C.S. Zuker, Assembly of the Drosophila phototransduction cascade into a signalling complex shapes elementary responses, Nature 395 (1998) 805-808.
    • (1998) Nature , vol.395 , pp. 805-808
    • Scott, K.1    Zuker, C.S.2
  • 39
    • 0033590449 scopus 로고    scopus 로고
    • Polyunsaturated fatty acids activate the Drosophila light-sensitive channels TRP and TRPL
    • S. Chyb, P. Raghu, R.C. Hardie, Polyunsaturated fatty acids activate the Drosophila light-sensitive channels TRP and TRPL, Nature 397 (1999) 255-259.
    • (1999) Nature , vol.397 , pp. 255-259
    • Chyb, S.1    Raghu, P.2    Hardie, R.C.3
  • 40
    • 0034777494 scopus 로고    scopus 로고
    • Regulation of Drosophila transient receptor potential-like (TrpL) channels by phospholipase C-dependent mechanisms
    • M. Estacion, W.G. Sinkins, W.P. Schilling, Regulation of Drosophila transient receptor potential-like (TrpL) channels by phospholipase C-dependent mechanisms, J. Physiol. 530 (2001) 1-19.
    • (2001) J. Physiol. , vol.530 , pp. 1-19
    • Estacion, M.1    Sinkins, W.G.2    Schilling, W.P.3
  • 42
    • 0034255456 scopus 로고    scopus 로고
    • Metabolic stress reversibly activates the Drosophila light-sensitive channels TRP and TRPL in vivo
    • K. Agam, M. von Campenhausen, S. Levy, H.C. Ben-Ami, B. Cook, K. Kirschfeld, B. Minke, Metabolic stress reversibly activates the Drosophila light-sensitive channels TRP and TRPL in vivo, J. Neurosci. 20 (2000) 5748-5755.
    • (2000) J. Neurosci. , vol.20 , pp. 5748-5755
    • Agam, K.1    von Campenhausen, M.2    Levy, S.3    Ben-Ami, H.C.4    Cook, B.5    Kirschfeld, K.6    Minke, B.7
  • 43
    • 0028294559 scopus 로고
    • Spontaneous activation of light-sensitive channels in Drosophila photoreceptors
    • R.C. Hardie, B. Minke, Spontaneous activation of light-sensitive channels in Drosophila photoreceptors, J. Gen. Physiol. 103 (1994) 389-407.
    • (1994) J. Gen. Physiol. , vol.103 , pp. 389-407
    • Hardie, R.C.1    Minke, B.2
  • 44
    • 0036080482 scopus 로고    scopus 로고
    • TRP channel proteins and signal transduction
    • B. Minke, B. Cook, TRP channel proteins and signal transduction, Physiol. Rev. 82 (2002) 429-472.
    • (2002) Physiol. Rev. , vol.82 , pp. 429-472
    • Minke, B.1    Cook, B.2
  • 48
    • 0036683972 scopus 로고    scopus 로고
    • Recovery from muscarinic modulation of M current channels requires phosphatidylinositol 4,5-bisphosphate synthesis
    • B.C. Sub, B. Hille, Recovery from muscarinic modulation of M current channels requires phosphatidylinositol 4,5-bisphosphate synthesis, Neuron 35 (2002) 507-520.
    • (2002) Neuron , vol.35 , pp. 507-520
    • Sub, B.C.1    Hille, B.2
  • 49
    • 0035927651 scopus 로고    scopus 로고
    • Bradykinin and nerve growth factor release the capsaicin receptor from PtdIns(4,5)P2-mediated inhibition
    • H.H. Chuang, E.D. Prescott, H. Kong, S. Shields, S.E. Jordt, A.I. Basbaum, M.V. Chao, D. Julius, Bradykinin and nerve growth factor release the capsaicin receptor from PtdIns(4,5)P2-mediated inhibition, Nature 411 (2001) 957-962.
    • (2001) Nature , vol.411 , pp. 957-962
    • Chuang, H.H.1    Prescott, E.D.2    Kong, H.3    Shields, S.4    Jordt, S.E.5    Basbaum, A.I.6    Chao, M.V.7    Julius, D.8
  • 50
    • 0036092076 scopus 로고    scopus 로고
    • The TRPM7 channel is inactivated by PIP2 hydrolysis
    • L.W. Runnels, L.X. Yue, D.E. Clapham, The TRPM7 channel is inactivated by PIP2 hydrolysis, Nat. Cell Biol. 4 (2002) 329-336.
    • (2002) Nat. Cell Biol. , vol.4 , pp. 329-336
    • Runnels, L.W.1    Yue, L.X.2    Clapham, D.E.3
  • 51
    • 0028812325 scopus 로고
    • Regulation of PLC-mediated signalling in vivo by CDP-diacylglycerol synthase
    • L. Wu, B. Niemeyer, N. Colley, M. Socolich, C.S. Zuker, Regulation of PLC-mediated signalling in vivo by CDP-diacylglycerol synthase, Nature 373 (1995) 216-222.
    • (1995) Nature , vol.373 , pp. 216-222
    • Wu, L.1    Niemeyer, B.2    Colley, N.3    Socolich, M.4    Zuker, C.S.5
  • 52
    • 0036417241 scopus 로고    scopus 로고
    • Scaffolding proteins organize multimolecular protein complexes for sensory signal transduction
    • A. Huber, Scaffolding proteins organize multimolecular protein complexes for sensory signal transduction, Eur. J. Neurosci. 14 (2001) 769-776.
    • (2001) Eur. J. Neurosci. , vol.14 , pp. 769-776
    • Huber, A.1
  • 54
    • 0032589396 scopus 로고    scopus 로고
    • 2+ reach millimolar concentrations after single photon absorption in Drosophila photoreceptor microvilli?
    • 2+ reach millimolar concentrations after single photon absorption in Drosophila photoreceptor microvilli? Biophys. J. 77 (1999) 1811-1823.
    • (1999) Biophys. J. , vol.77 , pp. 1811-1823
    • Postma, M.1    Oberwinkler, J.2    Stavenga, D.G.3
  • 55
    • 0032571011 scopus 로고    scopus 로고
    • 2+ channel assembled in a signaling complex by the PDZ domain protein INAD is phosphorylated through the interaction with protein kinase C (ePKC)
    • 2+ channel assembled in a signaling complex by the PDZ domain protein INAD is phosphorylated through the interaction with protein kinase C (ePKC), FEBS Lett. 425 (1998) 317-322.
    • (1998) FEBS Lett. , vol.425 , pp. 317-322
    • Huber, A.1    Sander, P.2    Bahner, M.3    Paulsen, R.4
  • 56
    • 15844382709 scopus 로고    scopus 로고
    • Phosphorylation of the InaD gene product, a photoreceptor membrane protein required for recovery of visual excitation
    • A. Huber, P. Sander, R. Paulsen, Phosphorylation of the InaD gene product, a photoreceptor membrane protein required for recovery of visual excitation, J. Biol. Chem. 271 (1996) 11710-11717.
    • (1996) J. Biol. Chem. , vol.271 , pp. 11710-11717
    • Huber, A.1    Sander, P.2    Paulsen, R.3


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