TY - JOUR
T1 - Rhodopsin formation in Drosophila is dependent on the PINTA retinoid-binding protein
AU - Wang, Tao
AU - Montell, Craig
PY - 2005/5/25
Y1 - 2005/5/25
N2 - 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 after potential 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.
AB - 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 after potential 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.
KW - CRAL-TRIO domain
KW - Phototransduction
KW - Pigment cells
KW - Retinal
KW - Retinoid-binding protein
KW - Rhodopsin
UR - http://www.scopus.com/inward/record.url?scp=19444378657&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=19444378657&partnerID=8YFLogxK
U2 - 10.1523/JNEUROSCI.0995-05.2005
DO - 10.1523/JNEUROSCI.0995-05.2005
M3 - Article
C2 - 15917458
AN - SCOPUS:19444378657
SN - 0270-6474
VL - 25
SP - 5187
EP - 5194
JO - Journal of Neuroscience
JF - Journal of Neuroscience
IS - 21
ER -