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The Journal of Neuroscience, May 25, 2005, 25(21):5187-5194; doi:10.1523/JNEUROSCI.0995-05.2005
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Cellular/Molecular
Rhodopsin Formation in Drosophila Is Dependent on the PINTA Retinoid-Binding Protein
Tao Wang and
Craig Montell
Department of Biological Chemistry, The Johns Hopkins University School of Medicine, Baltimore, Maryland 21205
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.
Key words: rhodopsin; phototransduction; retinoid-binding protein; pigment cells; CRAL-TRIO domain; retinal
Received March 14, 2005;
revised April 14, 2005;
accepted April 20, 2005.
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