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Zuker, C.S.1
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TRPC1, a human homolog of a Drosophila store-operated channel
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Wes PD, Chevesich J, Jeromin A, Rosenberg C, Stetten G, Montell C. TRPC1, a human homolog of a Drosophila store-operated channel. Proc Natl Acad Sci USA. 92:1995;9652-9656.
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0029094168
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Putative capacitative calcium entry channels - Expression of Drosophila trp and evidence for the existence of vertebrate homologs
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Petersen CC, Berridge MJ, Borgese MF, Bennett DL. Putative capacitative calcium entry channels - expression of Drosophila trp and evidence for the existence of vertebrate homologs. Biochem J. 311:1995;31-44.
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Petersen, C.C.1
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2+ channel in Drosophila photoreceptors
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2+ channel in Drosophila photoreceptors. Neuron. 8:1992;643-651.
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Neuron
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Hardie, R.C.1
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Calmodulin regulation of calcium stores in phototransduction of Drosophila
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Arnon A, Cook B, Montell C, Selinger Z, Minke B. Calmodulin regulation of calcium stores in phototransduction of Drosophila. Science. 275:1997;1119-1121.
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Science
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Arnon, A.1
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Tracing the roots of ion channels
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Jan L, Jan Y. Tracing the roots of ion channels. Cell. 69:1992;715-718.
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Jan, Y.2
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Molecular characterization of the Drosophila trp locus: A putative integral membrane protein required for phototransduction
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Montell C, Rubin GM. Molecular characterization of the Drosophila trp locus: a putative integral membrane protein required for phototransduction. Neuron. 2:1989;1313-1323.
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Montell, C.1
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Identification of a Drosophila gene encoding a calmodulin-binding protein with homology to the trp phototransduction gene
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Phillips A, Bull A, Kelly L. Identification of a Drosophila gene encoding a calmodulin-binding protein with homology to the trp phototransduction gene. Neuron. 8:1992;631-642.
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Phillips, A.1
Bull, A.2
Kelly, L.3
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0029927299
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The Drosophila light-activated conductance is composed of the two channels TRP and TRPL
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of outstanding interest. This paper provides the first demonstration that TRPL and TRP comprise the light-activated ion channels in vivo. The isolation and characterization of trpl mutants showed that trpl encodes a minor component of the light-activated conductance. A combination of genetic and electrophysiological approaches demonstrated that together TRP and TRPL account for all light-induced currents in photoreceptors.
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Niemeyer BA, Suzuki E, Scott K, Jalink K, Zuker CS. The Drosophila light-activated conductance is composed of the two channels TRP and TRPL. of outstanding interest Cell. 85:1996;651-659 This paper provides the first demonstration that TRPL and TRP comprise the light-activated ion channels in vivo. The isolation and characterization of trpl mutants showed that trpl encodes a minor component of the light-activated conductance. A combination of genetic and electrophysiological approaches demonstrated that together TRP and TRPL account for all light-induced currents in photoreceptors.
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(1996)
Cell
, vol.85
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Niemeyer, B.A.1
Suzuki, E.2
Scott, K.3
Jalink, K.4
Zuker, C.S.5
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16
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0028284467
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The light response of Drosophila photoreceptors is accompanied by an increase in cellular calcium: Effects of specific mutations
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Peretz A, Suss-Toby E, Rom-Glas A, Arnon A, Payne R, Minke B. The light response of Drosophila photoreceptors is accompanied by an increase in cellular calcium: effects of specific mutations. Neuron. 12:1994;1257-1267.
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Neuron
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Peretz, A.1
Suss-Toby, E.2
Rom-Glas, A.3
Arnon, A.4
Payne, R.5
Minke, B.6
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17
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0014683485
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Abnormal electroretinogram from a Drosophila mutant
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Cosens D, Manning A. Abnormal electroretinogram from a Drosophila mutant. Nature. 224:1969;285-287.
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Nature
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Cosens, D.1
Manning, A.2
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18
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0030665081
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Calmodulin regulation of Drosophila light-activated channels and receptor function mediates termination of the light response in vivo
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of outstanding interest. CAM mediates the calcium-dependent feedback of multiple steps in the phototransduction cascade, orchestrating the termination of receptor function and ion channel activity. Light responses in cam mutants, and in a variety of transgenic and mutant backgrounds, were analyzed to map the sites of action of CAM to specific transduction proteins. One site of CAM action is TRPL, and this can account for the transient response of the trp mutant.
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Scott K, Sun YM, Beckingham K, Zuker CS. Calmodulin regulation of Drosophila light-activated channels and receptor function mediates termination of the light response in vivo. of outstanding interest Cell. 91:1997;375-383 CAM mediates the calcium-dependent feedback of multiple steps in the phototransduction cascade, orchestrating the termination of receptor function and ion channel activity. Light responses in cam mutants, and in a variety of transgenic and mutant backgrounds, were analyzed to map the sites of action of CAM to specific transduction proteins. One site of CAM action is TRPL, and this can account for the transient response of the trp mutant.
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(1997)
Cell
, vol.91
, pp. 375-383
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Scott, K.1
Sun, Y.M.2
Beckingham, K.3
Zuker, C.S.4
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19
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0031459042
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In vivo analysis of the Drosophila light-sensitive channels, TRP and TRPL
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of outstanding interest. Biophysical studies of light responses in wild type and trp and trpl mutants showed that the light-activated conductance can be explained as the sum of separate TRP and TRPL activities. This detailed characterization of light responses in the absence of external calcium, or near the reversal potential of the current, provided a number of independent estimates of the relative contributions of TRP and TRPL, and the first demonstration of a phenotype for trpl.
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Reuss H, Mojet MH, Chyb S, Hardie RC. In vivo analysis of the Drosophila light-sensitive channels, TRP and TRPL. of outstanding interest Neuron. 19:1997;1249-1259 Biophysical studies of light responses in wild type and trp and trpl mutants showed that the light-activated conductance can be explained as the sum of separate TRP and TRPL activities. This detailed characterization of light responses in the absence of external calcium, or near the reversal potential of the current, provided a number of independent estimates of the relative contributions of TRP and TRPL, and the first demonstration of a phenotype for trpl.
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(1997)
Neuron
, vol.19
, pp. 1249-1259
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Reuss, H.1
Mojet, M.H.2
Chyb, S.3
Hardie, R.C.4
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20
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0028819281
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2+ facilitates and inactivates but does not directly excite light-sensitive channels in Drosophila photoreceptors
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2+ facilitates and inactivates but does not directly excite light-sensitive channels in Drosophila photoreceptors. J Neurosci. 15:1995;889-902.
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(1995)
J Neurosci
, vol.15
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Hardie, R.1
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21
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0029866944
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Identification and characterization of two distinct calmodulin-binding sites in the Trpl ion-channel of Drosophila melanogaster
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of special interest. Biochemical studies mapped the two CAM-binding sites of TRPL to regions of its carboxyl terminus. The first CAM binding site displays strong calcium-dependent CAM binding, whereas the second CAM binding site is a novel site with calcium-independent CAM-binding properties.
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Warr CG, Kelly LE. Identification and characterization of two distinct calmodulin-binding sites in the Trpl ion-channel of Drosophila melanogaster. of special interest Biochem J. 314:1996;497-503 Biochemical studies mapped the two CAM-binding sites of TRPL to regions of its carboxyl terminus. The first CAM binding site displays strong calcium-dependent CAM binding, whereas the second CAM binding site is a novel site with calcium-independent CAM-binding properties.
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(1996)
Biochem J
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Warr, C.G.1
Kelly, L.E.2
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0030467257
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2+ entry
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2+ entry. Proc Natl Acad Sci USA. 93:1996;14146-14151.
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(1996)
Proc Natl Acad Sci USA
, vol.93
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Gillo, B.1
Chorna, I.2
Cohen, H.3
Cook, B.4
Manistersky, I.5
Chorev, M.6
Arnon, A.7
Pollock, J.A.8
Selinger, Z.9
Minke, B.10
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23
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0031587878
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Coassembly of TRP and TRPL produces a distinct store-operated conductance
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Xu XZ, Li HS, Guggino WB, Montell C. Coassembly of TRP and TRPL produces a distinct store-operated conductance. Cell. 89:1997;1155-1164.
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(1997)
Cell
, vol.89
, pp. 1155-1164
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Xu, X.Z.1
Li, H.S.2
Guggino, W.B.3
Montell, C.4
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24
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0030841932
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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
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of outstanding interest. The properties of TRPL conductance in heterologous systems are identical to the properties of the light-activated conductance of the trp mutant, providing strong evidence that the current in the trp mutant is carried by TRPL.
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Hardie RC, Reuss H, Lansdell SJ, Millar NS. 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. of outstanding interest Cell Calcium. 21:1997;431-440 The properties of TRPL conductance in heterologous systems are identical to the properties of the light-activated conductance of the trp mutant, providing strong evidence that the current in the trp mutant is carried by TRPL.
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(1997)
Cell Calcium
, vol.21
, pp. 431-440
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Hardie, R.C.1
Reuss, H.2
Lansdell, S.J.3
Millar, N.S.4
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25
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0030835610
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A multivalent PDZ-domain protein assembles signalling complexes in a G-protein-coupled cascade
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of outstanding interest. These studies demonstrated that inactivation-no-afterpotential D (INAD) functions as the organizing scaffold for photoreceptor signaling complexes in vivo. Each PDZ domain of INAD binds a different signaling component, including the TRP light-activated ion channel, the effector PLC and PKC. Mutants lacking INAD have a dramatic redistribution of signaling molecules and a complete loss of transduction complexes. Also, mutants defective in a single PDZ domain display corresponding defects in the localization of a single target, demonstrating that INAD functions as a modular protein.
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Tsunoda S, Sierralta J, Sun Y, Bodner R, Suzuki E, Becker A, Socolich M, Zuker CS. A multivalent PDZ-domain protein assembles signalling complexes in a G-protein-coupled cascade. of outstanding interest Nature. 388:1997;243-249 These studies demonstrated that inactivation-no-afterpotential D (INAD) functions as the organizing scaffold for photoreceptor signaling complexes in vivo. Each PDZ domain of INAD binds a different signaling component, including the TRP light-activated ion channel, the effector PLC and PKC. Mutants lacking INAD have a dramatic redistribution of signaling molecules and a complete loss of transduction complexes. Also, mutants defective in a single PDZ domain display corresponding defects in the localization of a single target, demonstrating that INAD functions as a modular protein.
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(1997)
Nature
, vol.388
, pp. 243-249
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Tsunoda, S.1
Sierralta, J.2
Sun, Y.3
Bodner, R.4
Suzuki, E.5
Becker, A.6
Socolich, M.7
Zuker, C.S.8
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26
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0027397544
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Inositol trisphosphate and calcium signaling
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Berridge M. Inositol trisphosphate and calcium signaling. Nature. 361:1993;315-325.
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(1993)
Nature
, vol.361
, pp. 315-325
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Berridge, M.1
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27
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0027422088
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The signal for capacitative calcium entry
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Putney JW, Bird GSJ. The signal for capacitative calcium entry. Cell. 75:1993;199-201.
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(1993)
Cell
, vol.75
, pp. 199-201
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Putney, J.W.1
Bird, G.S.J.2
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0028826727
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Capacitative calcium entry
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Berridge MJ. Capacitative calcium entry. Biochem J. 312:1995;1-11.
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Biochem J
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Berridge, M.J.1
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0028831997
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Calcium signaling
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Clapham DE. Calcium signaling. Cell. 80:1995;259-268.
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(1995)
Cell
, vol.80
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Clapham, D.E.1
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31
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0030218120
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The roles of TRP and calcium in regulating photoreceptor function in Drosophila
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Minke B, Selinger Z. The roles of TRP and calcium in regulating photoreceptor function in Drosophila. Curr Opin Neurobiol. 6:1996;459-466.
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Curr Opin Neurobiol
, vol.6
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Minke, B.1
Selinger, Z.2
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32
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0030810066
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Store depletion and calcium influx
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of special interest. This comprehensive review provides a detailed description of store-operated calcium currents, focusing on the electrophysiological properties of SOCs. The review discusses current models of activation and regulation of SOCs, and critically examines the role of TRP in capacitative calcium entry.
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Parekh AB, Penner R. Store depletion and calcium influx. of special interest Physiol Rev. 77:1997;901-930 This comprehensive review provides a detailed description of store-operated calcium currents, focusing on the electrophysiological properties of SOCs. The review discusses current models of activation and regulation of SOCs, and critically examines the role of TRP in capacitative calcium entry.
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(1997)
Physiol Rev
, vol.77
, pp. 901-930
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Parekh, A.B.1
Penner, R.2
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0030175896
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TRP is cracked but is CRAC TRP?
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Clapham DE. TRP is cracked but is CRAC TRP? Neuron. 16:1996;1069-1072.
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(1996)
Neuron
, vol.16
, pp. 1069-1072
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Clapham, D.E.1
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35
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0028955687
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The Drosophila cation channel trpl expressed in insect Sf9 cells is stimulated by agonists of G-protein-coupled receptors
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Harteneck C, Obukhov AG, Zobel A, Kalkbrenner F, Schultz G. The Drosophila cation channel trpl expressed in insect Sf9 cells is stimulated by agonists of G-protein-coupled receptors. FEBS Lett. 358:1995;297-300.
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(1995)
FEBS Lett
, vol.358
, pp. 297-300
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Harteneck, C.1
Obukhov, A.G.2
Zobel, A.3
Kalkbrenner, F.4
Schultz, G.5
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36
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0028817757
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3 activates a Drosophila cation channel Trpl in recombinant baculovirus-infected Sf9 insect cells
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3 activates a Drosophila cation channel Trpl in recombinant baculovirus-infected Sf9 insect cells. Am J Physiol. 269:1995;1332-1339.
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(1995)
Am J Physiol
, vol.269
, pp. 1332-1339
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Dong, Y.1
Kunze, D.L.2
Vaca, L.3
Schilling, W.P.4
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37
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0027996645
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Cytosolic calcium transients: Spatial localization and role in Drosophila photoreceptor cell function
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Ranganathan R, Bacskai BJ, Tsien RY, Zuker CS. Cytosolic calcium transients: spatial localization and role in Drosophila photoreceptor cell function. Neuron. 13:1994;837-848.
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(1994)
Neuron
, vol.13
, pp. 837-848
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Ranganathan, R.1
Bacskai, B.J.2
Tsien, R.Y.3
Zuker, C.S.4
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38
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0029923620
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2+ concentration in Drosophila photoreceptors
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2+ concentration in Drosophila photoreceptors. J Neurosci. 16:1996;2924-2933.
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(1996)
J Neurosci
, vol.16
, pp. 2924-2933
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Hardie, R.C.1
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39
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0029411985
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2+ chelation on the light response in Drosophila photoreceptors
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2+ chelation on the light response in Drosophila photoreceptors. J Comp Physiol A. 177:1995;707-721.
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(1995)
J Comp Physiol a
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Hardie, R.C.1
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40
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0030612593
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InsP3 receptor is essential for growth and differentiation but not for vision in Drosophila
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3R does not play a role in the activation or the regulation of the light response.
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3R does not play a role in the activation or the regulation of the light response.
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(1997)
Neuron
, vol.18
, pp. 881-887
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Acharya, J.K.1
Jalink, K.2
Hardy, R.W.3
Hartenstein, V.4
Zuker, C.S.5
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41
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0027201549
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Protein kinase C is required for light adaptation in Drosophila photoreceptors
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Hardie RC, Peretz A, Suss-Toby E, Rom GA, Bishop SA, Selinger Z, Minke B. Protein kinase C is required for light adaptation in Drosophila photoreceptors. Nature. 363:1993;634-637.
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(1993)
Nature
, vol.363
, pp. 634-637
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Hardie, R.C.1
Peretz, A.2
Suss-Toby, E.3
Rom, G.A.4
Bishop, S.A.5
Selinger, Z.6
Minke, B.7
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42
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0028861452
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A novel protein encoded by the InaD gene regulates recovery of visual transduction in Drosophila
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Shieh B-H, Niemeyer B. A novel protein encoded by the InaD gene regulates recovery of visual transduction in Drosophila. Neuron. 14:1995;201-210.
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(1995)
Neuron
, vol.14
, pp. 201-210
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Shieh B-H1
Niemeyer, B.2
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43
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0030475794
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2+ channel essential for phosphoinositide-mediated photoreception, forms a signaling complex with NorpA, InaC and InaD
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of outstanding interest. The paper provides the first description of the INAD macromolecular signaling complex. Immunoprecipitation experiments showed that TRP is tightly associated with INAD, PKC and PLC and immunohistochemistry studies showed that these signaling components co-localize to the microvillar organelle where phototransduction occurs.
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2+ channel essential for phosphoinositide-mediated photoreception, forms a signaling complex with NorpA, InaC and InaD. of outstanding interest EMBO J. 15:1996;7036-7045 The paper provides the first description of the INAD macromolecular signaling complex. Immunoprecipitation experiments showed that TRP is tightly associated with INAD, PKC and PLC and immunohistochemistry studies showed that these signaling components co-localize to the microvillar organelle where phototransduction occurs.
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(1996)
EMBO J
, vol.15
, pp. 7036-7045
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Huber, A.1
Sander, P.2
Gobert, A.3
Bahner, M.4
Hermann, R.5
Paulsen, R.6
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44
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0029664550
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2+ channel by INAD in Drosophila photoreceptors
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215 mutants have a mutation in this PDZ domain and do not interact with TRP in vitro.
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215 mutants have a mutation in this PDZ domain and do not interact with TRP in vitro.
-
(1996)
Neuron
, vol.16
, pp. 991-998
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Shieh, B.H.1
Zhu, M.Y.2
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45
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0030856343
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Association of INAD with NORPA is essential for controlled activation and deactivation of Drosophila phototransduction in vivo
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of special interest. These studies mapped the interaction site of PLC with INAD to the carboxyl region of PLC. Transgenic animals with a disruption in the PLC - INAD interaction have severely defective light responses, arguing that the proper localization of PLC is important for rapid signaling.
-
Shieh BH, Zhu MY, Lee JK, Kelly IM, Bahiraei F. Association of INAD with NORPA is essential for controlled activation and deactivation of Drosophila phototransduction in vivo. of special interest Proc Natl Acad Sci USA. 94:1997;12682-12687 These studies mapped the interaction site of PLC with INAD to the carboxyl region of PLC. Transgenic animals with a disruption in the PLC - INAD interaction have severely defective light responses, arguing that the proper localization of PLC is important for rapid signaling.
-
(1997)
Proc Natl Acad Sci USA
, vol.94
, pp. 12682-12687
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Shieh, B.H.1
Zhu, M.Y.2
Lee, J.K.3
Kelly, I.M.4
Bahiraei, F.5
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46
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0031037164
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Requirement for the PDZ domain protein, INAD, for localization of the TRP store-operated channel to a signaling complex
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of outstanding interest. of special interest. This paper showed that the TRP ion channel associated in a complex with CAM, INAD, PKC and PLC. Rhodopsin is also proposed to be included in this signaling complex; however, similar studies were unable to detect this association [25,43].
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of outstanding interest Chevesich J, Kreuz AJ, Montell C. Requirement for the PDZ domain protein, INAD, for localization of the TRP store-operated channel to a signaling complex. of special interest Neuron. 18:1997;95-105 This paper showed that the TRP ion channel associated in a complex with CAM, INAD, PKC and PLC. Rhodopsin is also proposed to be included in this signaling complex; however, similar studies were unable to detect this association [25,43].
-
(1997)
Neuron
, vol.18
, pp. 95-105
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Chevesich, J.1
Kreuz, A.J.2
Montell, C.3
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47
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0030820681
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Molecular characterization of a novel human PDZ domain protein with homology to INAD from Drosophila melanogaster
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Philipp S, Flockerzi V. Molecular characterization of a novel human PDZ domain protein with homology to INAD from Drosophila melanogaster. FEBS Lett. 413:1997;243-248.
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(1997)
FEBS Lett
, vol.413
, pp. 243-248
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Philipp, S.1
Flockerzi, V.2
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