Ectopic expression of a minor Drosophila opsin in the major photoreceptor cell class: Distinguishing the role of primary receptor and cellular context

Zuker, Charles S.; Mismer, Drzislav; Hardy, Robert W.; Rubin, Gerald M.

doi:10.1016/0092-8674(88)90167-5

Cited by 46 publications

(26 citation statements)

References 33 publications

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“…This may reflect either the presence of intermolecular disulfide bond(s), or a requirement for the correct 'folded' state in one of these two proteins. In this regard, Khorana and co-workers (Kamik et al, 1988;Kamik and Khorana, 1990) (Feiler et al, 1988 (Feiler et al, 1988(Feiler et al, , 1992Zuker et al, 1988). If the ninaE gene is deleted in these flies, Rhl rhodopsin is effectively replaced by one of the minor opsins.…”

Section: Resultsmentioning

confidence: 99%

“…The modified genes were placed under the control of the Rhl promoter as described previously (Feiler et al, 1988(Feiler et al, , 1992Zuker et al, 1988). Following DNA sequencing of the reconstructed fragments, the modified opsins were subcloned into a Pelement transformation vector containing the rosv+ gene as a selectable marker (Karess and Rubin, 1984).…”

Section: Dna Constructs and Transgenic Animalsmentioning

confidence: 99%

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The cyclophilin homolog NinaA functions as a chaperone, forming a stable complex in vivo with its protein target rhodopsin.

1994

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Section: Resultsmentioning

confidence: 99%

Section: Dna Constructs and Transgenic Animalsmentioning

confidence: 99%

The cyclophilin homolog NinaA functions as a chaperone, forming a stable complex in vivo with its protein target rhodopsin.

1994

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“…In contrast to most ommatidia, the dorsal margin of the compound eye contains ommatidia that express Rh3 in both the R7 and R8 cells [45]. A violet-absorbing rhodopsin, Rh2, is expressed exclusively in the photoreceptor cells of the three ocelli, the simpler eyes localized on the vertex of the fly head [53][54][55][56].…”

Section: Diversity Of Drosophila Rhodopsinsmentioning

confidence: 99%

“…The minor rhodopsins are also bistable pigments. Misexpression of a minor opsin in the R1-6 photoreceptor cells, in the absence of Rh1, results in the production of a PDA according to the spectral characteristics of the minor rhodopsin [54,56,101]. For example, introduction of Rh2 in the R1-R6 cells results in a PDA that is produced at ∼420 nm and terminated at ∼520 nm, respectively.…”

Section: The Rhodopsin Cycle In Drosophilamentioning

confidence: 99%

Phototransduction and retinal degeneration in Drosophila

Wang

Montell

2007

Pflugers Arch - Eur J Physiol

261

303

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Drosophila visual transduction is the fastest known G-protein-coupled signaling cascade and has therefore served as a genetically tractable animal model for characterizing rapid responses to sensory stimulation. Mutations in over 30 genes have been identified, which affect activation, adaptation, or termination of the photoresponse. Based on analyses of these genes, a model for phototransduction has emerged, which involves phosphoinoside signaling and culminates with opening of the TRP and TRPL cation channels. Many of the proteins that function in phototransduction are coupled to the PDZ containing scaffold protein INAD and form a supramolecular signaling complex, the signalplex. Arrestin, TRPL, and Gα q undergo dynamic light-dependent trafficking, and these movements function in long-term adaptation. Other proteins play important roles either in the formation or maturation of rhodopsin, or in regeneration of phosphatidylinositol 4,5-bisphosphate (PIP 2 ), which is required for the photoresponse. Mutation of nearly any gene that functions in the photoresponse results in retinal degeneration. The underlying bases of photoreceptor cell death are diverse and involve mechanisms such as excessive endocytosis of rhodopsin due to stable rhodopsin/arrestin complexes and abnormally low or high levels of Ca 2+ . Drosophila visual transduction appears to have particular relevance to the cascade in the intrinsically photosensitive retinal ganglion cells in mammals, as the photoresponse in these latter cells appears to operate through a remarkably similar mechanism.

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“…Opsin genes and cDNAs have been isolated and characterized in a number of vertebrate and invertebrate species including bovine, human and Drosophila [3]. Regulation of opsin gene expression has been studied extensively in Drosophila [4], but not in mammalian systems. The mouse opsin gene is particularly well suited for regulatory studies concerning gene expression.…”

Section: Introductionmentioning

confidence: 99%

Isolation and analysis of the mouse opsin gene

et al. 1988

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We have identified three overlapping S-truncated mouse opsin cDNA clones by immunologically screening a hgtl 1 retina expression library. Using one of the cDNA clones as a probe, we isolated a 5 kb genomic fragment that encompassed the complete coding sequence for mouse opsin. The coding region for opsin was interrupted by four introns positioned precisely as those previously described for other mammalian opsins. In contrast to the single major opsin mRNA in the bovine and human retina, Northern analysis of mouse retina RNA demonstrated the presence of at least five distinct species of polyadenylated opsin mRNAs. Their sizes ranged from 1.7 kb to 5.1 kb.

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Ectopic expression of a minor Drosophila opsin in the major photoreceptor cell class: Distinguishing the role of primary receptor and cellular context

Cited by 46 publications

References 33 publications

The cyclophilin homolog NinaA functions as a chaperone, forming a stable complex in vivo with its protein target rhodopsin.

The cyclophilin homolog NinaA functions as a chaperone, forming a stable complex in vivo with its protein target rhodopsin.

Phototransduction and retinal degeneration in Drosophila

Isolation and analysis of the mouse opsin gene

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