Reference Report
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| Citation | Wang, T., Montell, C. (2005). Rhodopsin formation in Drosophila is dependent on the PINTA retinoid-binding protein. J. Neurosci. 25(21): 5187--5194. (Export to RIS) | ||
| FlyBase ID | FBrf0187905 | ||
| Publication Type | Research paper | ||
| PubMed ID | 15917458 | ||
| PubMed Abstract | Retinoids participate in many essential processes including the initial event in photoreception. 11-cis-retinal binds to opsin and undergoes a light-driven isomerization to all-trans-retinal. In mammals, the all-trans-retinal is converted to vitamin A (all-trans-retinol) and is transported to the retinal pigment epithelium (RPE), where along with dietary vitamin A, it is converted into 11-cis-retinal. Although this cycle has been studied extensively in mammals, many questions remain, including the specific roles of retinoid-binding proteins. Here, we establish the Drosophila visual system as a genetic model for characterizing retinoid-binding proteins. In a genetic screen for mutations that affect the biosynthesis of rhodopsin, we identified a novel CRAL-TRIO domain protein, prolonged depolarization afterpotential is not apparent (PINTA), which binds to all-trans-retinol. We demonstrate that PINTA functions subsequent to the production of vitamin A and is expressed and required in the retinal pigment cells. These results represent the first genetic evidence for a role for the retinal pigment cells in the visual response. Moreover, our data implicate Drosophila retinal pigment cells as functioning in the conversion of dietary all-trans-retinol to 11-cis-retinal and suggest that these cells are the closest invertebrate equivalent to the RPE. | ||
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| Language of Publication | English | ||
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| Publication Type | Journal | ||
| Abbreviation | J. Neurosci. | ||
| Title | Journal of Neuroscience | ||
| Publication Year | 1981- | ||
| ISBN/ISSN | 0270-6474 1529-2401 | ||
Data from Reference
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Aberrations (4)
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Alleles (16)
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Constructs (3)
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Genes (14)
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Insertions (5)
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Natural transposons (1)
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