The light response of drosophila photoreceptors is accompanied by an increase in cellular calcium: Effects of specific mutations

Peretz, Asher; Suss-Toby, Edith; Rom-Glas, A.; Arnon, Assaf; Payne, Richard; Minke, Baruch

doi:10.1016/0896-6273(94)90442-1

Cited by 131 publications

(113 citation statements)

References 48 publications

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“…The potential of the pupil mechanism as an endogenous, intracellular calcium probe has so far only been exploited in a small number of Drosophila phototransduction mutants. The transient receptor potential mutant, trp, has a transient pupillary response (Lo and Pak, 1981), quite similar to the light-induced change in calcium measured photometrically (Peretz et al, 1994a, b); see Fig. 18.…”

Section: Pupillary Pigmentmentioning

confidence: 80%

“…isolated photoreceptors loaded with fluorescent calcium indicators, Peretz et al (1994a, b) and Ranganathan et al (1994) obtained direct proof of a substantial light-induced increase of the intracellular calcium coneentratiion.…”

Section: Light-induced Current and Late Receptor Potentialmentioning

confidence: 99%

“…A severe norpA (no receptor potential A) photoreceptor cell remains electrically silent, and a dark-adapted trp mutant features only a transient receptor potential when illuminated with a bright step of light. The magnitude and time course of the light-induced calcium changes appears to depend critically on these mutations (Peretz et al, 1994a, b). In a severe norpA mutant, intraeellular calcium remains low, which is intelligible when phototransduction is fully blocked by the defective PLC.…”

Section: Photoreceptor Mutantsmentioning

confidence: 99%

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Insect retinal pigments: Spectral characteristics and physiological functions

Stavenga

1995

Progress in Retinal and Eye Research

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Section: Pupillary Pigmentmentioning

confidence: 80%

Section: Light-induced Current and Late Receptor Potentialmentioning

confidence: 99%

Section: Photoreceptor Mutantsmentioning

confidence: 99%

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Insect retinal pigments: Spectral characteristics and physiological functions

Stavenga

1995

Progress in Retinal and Eye Research

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“…Therefore, the presence of TRP seems to be required for TRPL internalization. If the lack of PLC blocks TRPL translocation as found in TRPL-eGFP fusion experiments, then the block of TRPL translocation (Hardie and Minke, 1992;Peretz et al, 1994), by the absence of either TRP or PLC, suggests that light-induced Ca 2+ influx is the trigger for TRPL translocation.…”

Section: Light-regulated Translocation Of the Trpl Channelmentioning

confidence: 90%

“…The dissociation of Arr2 from rhodopsin requires photoconversion of metarhodopsin back to rhodopsin, followed by dephosphorylation of rhodospsin by the Ca 2+ dependent protein phosphatase RDGC (retinat degeneration C) (Byk et al, 1993;Dolph et al, 1993;Steele et al, 1992;Yamada et al, 1990). Arr2 is phosphorylated by calcium/calmodulin-dependent kinase II (CamKII) (Matsumoto et al, 1994;Yamada et al, 1990), which is activated by Ca 2+ influx through the light activated TRP and TRPL channels (Alloway and Dolph, 1999;Byk et al, 1993;Kiselev et al, 2000;Peretz et al, 1994). Mutations which cause stable association between Arr2 and metarhodopsin result in clathrin-dependent endocytosis of the metarhodopsin-Arr2 complexes into the cell body that eventually lead to degeneration of the photoreceptor cell (Alloway and Dolph, 1999;Alloway et al, 2000;Kiselev et al, 2000;Orem and Dolph, 2002).…”

Section: Light Adaptation Through Phosphoinositide and Ninac Myosin Imentioning

confidence: 99%

Light-regulated translocation of signaling proteins in Drosophila photoreceptors

Frechter

Minke

2006

Journal of Physiology-Paris

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Illumination of Drosophila photoreceptor cells induces multi-facet responses, which include generation of the photoreceptor potential, screening pigment migration and translocation of signaling proteins which is the focus of recent extensive research. Translocation of three signaling molecules is covered in this review: (1) Light-dependent translocation of arrestin from the cytosol to the signaling membrane, the rhabdomere, determines the lifetime of activated rhodopsin. Arrestin translocates in PIP 3 and NINAC myosin III dependent manner, and specific mutations which disrupt the interaction between arrestin and PIP 3 or NINAC also impair the light-dependant translocation of arrestin and the termination of the response to light. (2) Activation of Drosophila visual G protein, DGq, causes a massive and reversible, translocation of the α subunit from the signaling membrane to the cytosol, accompanied by activity-dependent architectural changes. Analysis of the translocation and the recovery kinetics of DGq α in wild-type flies and specific visual mutants indicated that DGq α is necessary but not sufficient for the architectural changes. (3) The TRP-like (TRPL) but not TRP channels translocate in a light-dependent manner between the rhabdomere and the cell body. As a physiological consequence of this light-dependent modulation of the TRP/TRPL ratio, the photoreceptors of dark-adapted flies operate at a wider dynamic range, which allows the photoreceptors enriched with TRPL to function better in darkness and dim background illumination. Altogether, signal-dependent movement of signaling proteins plays a major role in the maintenance and function of photoreceptor cells.

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Distribution of ryanodine receptor Ca2+ channels in insect photoreceptor cells

Baumann

2000

J. Comp. Neurol.

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Physiological studies have provided evidence for the existence of ryanodine receptor (RyR) Ca2+ channels in compound eyes of insects. The present study identifies and localizes RyR in insect photoreceptors by use of an affinity‐purified antibody against lobster muscle RyR. Western blotting and indirect immunofluorescence staining confirm cross‐reactivity of the antibody with insect muscle RyR. In both honeybee and fly eyes, the antibody identifies a single protein that comigrates with muscle RyR on sodium dodecylsulfate (SDS) polyacrylamide gels demonstrating that RyR is present in this tissue. By confocal immunofluorescence microscopy on honeybee eyes, RyR is detected within the photoreceptors and shows a nonhomogeneous distribution over the endoplasmic reticulum (ER). Double labeling studies have demonstrated further that RyR is localized at distinct ER elements close to the light‐sensitive microvilli and juxtaposed to adherens junctions. RyR has also been observed within the remaining soma of honeybee photoreceptors, being concentrated on ER cisternae close to mitochondria and the nonreceptive plasma membrane. For comparative purposes, the distribution of RyR has also been assayed in compound eyes of flies. In both Calliphora and Drosophila photoreceptors, the anti‐RyR antibody provides punctate labeling throughout the cell body. The submicrovillar ER cisternae associated with the base of the microvilli, however, are only lightly labeled for RyR. These results suggest that RyR is involved with Ca2+ regulation in the nonreceptive cell area of both fly and honeybee photoreceptors, but that it may contribute to Ca2+ regulation close to the phototransduction compartment only in the latter cell. J. Comp. Neurol. 421:347–361, 2000. © 2000 Wiley‐Liss, Inc.

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The light response of drosophila photoreceptors is accompanied by an increase in cellular calcium: Effects of specific mutations

Cited by 131 publications

References 48 publications

Insect retinal pigments: Spectral characteristics and physiological functions

Insect retinal pigments: Spectral characteristics and physiological functions

Light-regulated translocation of signaling proteins in Drosophila photoreceptors

Distribution of ryanodine receptor Ca2+ channels in insect photoreceptor cells

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