Source:http://linkedlifedata.com/resource/pubmed/id/15917458
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
21
|
| pubmed:dateCreated |
2005-5-26
|
| pubmed:abstractText |
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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| pubmed:grant | |
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Drosophila Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Eye Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Retinol-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Rhodopsin,
http://linkedlifedata.com/resource/pubmed/chemical/Tretinoin,
http://linkedlifedata.com/resource/pubmed/chemical/ninaE protein, Drosophila
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| pubmed:status |
MEDLINE
|
| pubmed:month |
May
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| pubmed:issn |
1529-2401
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| pubmed:author | |
| pubmed:issnType |
Electronic
|
| pubmed:day |
25
|
| pubmed:volume |
25
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
5187-94
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| pubmed:dateRevised |
2007-11-14
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| pubmed:meshHeading |
pubmed-meshheading:15917458-Animals,
pubmed-meshheading:15917458-Animals, Genetically Modified,
pubmed-meshheading:15917458-Blotting, Northern,
pubmed-meshheading:15917458-Blotting, Western,
pubmed-meshheading:15917458-Chromosome Mapping,
pubmed-meshheading:15917458-Cloning, Molecular,
pubmed-meshheading:15917458-Dose-Response Relationship, Drug,
pubmed-meshheading:15917458-Drosophila,
pubmed-meshheading:15917458-Drosophila Proteins,
pubmed-meshheading:15917458-Electroretinography,
pubmed-meshheading:15917458-Eye Proteins,
pubmed-meshheading:15917458-Gene Expression Regulation, Developmental,
pubmed-meshheading:15917458-Genotype,
pubmed-meshheading:15917458-In Situ Hybridization,
pubmed-meshheading:15917458-Light,
pubmed-meshheading:15917458-Mutation,
pubmed-meshheading:15917458-Pigment Epithelium of Eye,
pubmed-meshheading:15917458-Protein Binding,
pubmed-meshheading:15917458-Protein Structure, Tertiary,
pubmed-meshheading:15917458-Radioligand Assay,
pubmed-meshheading:15917458-Retinol-Binding Proteins,
pubmed-meshheading:15917458-Rhodopsin,
pubmed-meshheading:15917458-Sequence Alignment,
pubmed-meshheading:15917458-Tretinoin
|
| pubmed:year |
2005
|
| pubmed:articleTitle |
Rhodopsin formation in Drosophila is dependent on the PINTA retinoid-binding protein.
|
| pubmed:affiliation |
Department of Biological Chemistry, The Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, USA.
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| pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.,
Research Support, N.I.H., Extramural
|