Putative inositol 1,4,5-trisphosphate receptor localized to endoplasmic reticulum in Limulus photoreceptors

Ukhanov, Kirill; Ukhanova, M; Taylor, Colin W.; Payne, Richard

doi:10.1016/s0306-4522(98)00164-x

Cited by 11 publications

(5 citation statements)

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“…Although the subcellular distribution of InsP 3 R has not yet been determined for any insect photoreceptor by immunocytochemistry, results of physiological experiments suggest that InsP 3 ‐stimulated Ca 2+ release is associated with the submicrovillar ER of honeybee photoreceptors (Baumann and Walz, 1989a). This conclusion is in accordance with the data on Limulus photoreceptors, demonstrating anti‐InsP 3 R immunoreactivity at the submicrovillar cisternae (Ukhanov et al, 1998). Moreover, localization of InsP 3 R at the submicrovillar ER, close to the microvilli, appears reasonable as the phospholipase C involved with the light‐dependent production of InsP 3 is present in the microvilli (Schneuwly et al, 1991).…”

Section: Discussionsupporting

confidence: 93%

“…Moreover, Ca 2+ is released from the endoplasmic reticulum (ER) upon photostimulation of arthropod photoreceptors (Payne and Fein, 1987; Baumann et al, 1991; Walz and Baumann, 1995; Ukhanov and Payne, 1995). It is well documented for some arthropod photoreceptors that this Ca 2+ release from the ER results from the light‐induced activition of the phosphoinositide cascade and the opening of inositol (1,4,5)‐trisphosphate receptor (InsP 3 R) Ca 2+ channels within the ER membrane (Payne and Fein, 1987; Baumann and Walz, 1989a; Ukhanov and Payne, 1997; Ukhanov et al, 1998).…”

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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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Section: Discussionsupporting

confidence: 93%

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confidence: 99%

Distribution of ryanodine receptor Ca2+ channels in insect photoreceptor cells

Baumann

2000

J. Comp. Neurol.

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“…The phototransducing region is localized to the rhabdomeral area. The diagram was adapted from Ukhanov et al (1998). The scale bar ϭ 10 mm in A-C. similar to LCNG1.…”

Section: Lcng1 and Drosophila Cgmp-gated Channelsmentioning

confidence: 99%

A cGMP-gated channel subunit in Limulus photoreceptors

Chen

Baumann²,

Payne³

et al. 2001

Vis Neurosci

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The phototransduction cascade in invertebrate photoreceptors has not been fully elucidated. It has been proposed that in Limulus ventral photoreceptor cGMP is the intracellular second messenger that directly controls the gating of the light-dependent channels (Johnson et al., 1986: Bacigalupo et al., 1991). Recently, a putative cGMP-gated channel cDNA, Lcng1, has been cloned from Limulus and shown to be expressed in the brain and the ventral eye (Chen et al., 1999). In this study, we sought to more specifically localize the LCNG1 transcript and protein. In situ hybridization was used to determine whether the gene is expressed in glia or photoreceptor cells in the ventral eye. The results clearly demonstrated that Lcngl mRNA is transcribed in the ventral photoreceptors. On Western blots probed with a polyclonal antibody raised against the C-terminus of LCNGI, a 100-kDa band and an 80-kDa band was labeled in the membrane protein preparations from brain and ventral eye, respectively. The labeling of these bands was blocked by preabsorption of the antibody with the antigen, indicating the labeling specificity. Immunocytochemistry and confocal microscopy were applied to investigate the subcellular localization of this antigen. Immunolabeling was highly localized in the transducing lobes of ventral eye photoreceptors and lateral eye photoreceptors. In both cases, the labeling was associated with membrane regions specialized for phototransduction, but the exact pattern appeared to be somewhat different in the two eyes. Preabsorption of the antiserum with antigen abolished the labeling, confirming specificity. The results lend support to the hypothesis that a cGMP-gated channel is directly involved in the phototransduction process.

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“…An extensive literature details the physiology (Smith et al, 1965; Mellecchia et al, 1966; recently reviewed in Dorlöchter and Stieve, 1997) and ultrastructure (Miller, 1957; Clark et al, 1969; Fahrenbach, 1969, 1975; Calman and Chamberlain, 1982b; Chamberlain and Barlow, 1984; Herman 1991a,b) of these photoreceptors. However, relatively little is known about their biochemical organization, largely because few antibodies specific for Limulus photoreceptor proteins have been characterized (Calman and Chamberlain, 1982a; Jinks et al, 1996; Munger et al, 1997; Dorlöchter et al, 1997; Ukhanov et al, 1998; Battelle et al, 1998). Information as essential as the distribution of opsin is lacking for these cells.…”

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Immunocytochemical localization of opsin, visual arrestin, myosin III, and calmodulin in Limulus lateral eye retinular cells and ventral photoreceptors

Battelle

Dabdoub

Malone

et al. 2001

J of Comparative Neurology

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The photoreceptors of the horseshoe crab Limulus polyphemus are classical preparations for studies of the photoresponse and its modulation by circadian clocks. An extensive literature details their physiology and ultrastructure, but relatively little is known about their biochemical organization largely because of a lack of antibodies specific for Limulus photoreceptor proteins. We developed antibodies directed against Limulus opsin, visual arrestin, and myosin III, and we have used them to examine the distributions of these proteins in the Limulus visual system. We also used a commercial antibody to examine the distribution of calmodulin in Limulus photoreceptors. Fixed frozen sections of lateral eye were examined with conventional fluorescence microscopy; ventral photoreceptors were studied with confocal microscopy. Opsin, visual arrestin, myosin III, and calmodulin are all concentrated at the photosensitive rhabdomeral membrane, which is consistent with their participation in the photoresponse. Opsin and visual arrestin, but not myosin III or calmodulin, are also concentrated in extra-rhabdomeral vesicles thought to contain internalized rhabdomeral membrane. In addition, visual arrestin and myosin III were found widely distributed in the cytosol of photoreceptors, suggesting that they have functions in addition to their roles in phototransduction. Our results both clarify and raise new questions about the functions of opsin, visual arrestin, myosin III, and calmodulin in photoreceptors and set the stage for future studies of the impact of light and clock signals on the structure and function of photoreceptors.

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Putative inositol 1,4,5-trisphosphate receptor localized to endoplasmic reticulum in Limulus photoreceptors

Cited by 11 publications

References 29 publications

Distribution of ryanodine receptor Ca2+ channels in insect photoreceptor cells

Distribution of ryanodine receptor Ca2+ channels in insect photoreceptor cells

A cGMP-gated channel subunit in Limulus photoreceptors

Immunocytochemical localization of opsin, visual arrestin, myosin III, and calmodulin in Limulus lateral eye retinular cells and ventral photoreceptors

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