Evidence map›Paper›PMID 18474598›Full record

ArticleThe Journal of biological chemistry2008

Retinal pigment epithelium-retinal G protein receptor-opsin mediates light-dependent translocation of all-trans-retinyl esters for synthesis of visual chromophore in retinal pigment epithelial cells.

Roxana A Radu, Jane Hu, Jennifer Peng, Dean Bok, Nathan L Mata, Gabriel H Travis

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
58citing papers in PubMed, 1 pooled it
2.3field-weighted citation impact, top 12% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

58 citing papers in PubMed, 1 synthesis or guideline pooled it, 80 citations in OpenAlex.

  1. Pooled it
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  14. Is white the right light for the clinical electrooculogram?Documenta ophthalmologica. Advances in ophthalmology · 2021
    Article
  15. Article
  16. Rod Photoreceptors Avoid Saturation in Bright Light by the Movement of the G Protein Transducin.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2021
    Article
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  18. Review
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 1 institution in 1 country.

Roxana A RaduJules Stein Eye Institute, California, USA.
Jane Hu
Jennifer Peng
Dean Bok
Nathan L Mata
Gabriel H Travis
University of California, Los Angeles · US

Funding

The Role of Muller Cells in Visual Pigment RegenerationR01EY011713 · NEI · UNIVERSITY OF TEXAS SW MED CTR/DALLAS · PI TRAVIS, GABRIEL H · 1997 to 2017
$6.9M
NEI NIH HHS R01 EY011713NEI NIH HHS R01-EY01584
6 · The paper itself

Abstract

Visual perception begins with the absorption of a photon by an opsin pigment, inducing isomerization of its 11-cis-retinaldehyde chromophore. After a brief period of activation, the resulting all-trans-retinaldehyde dissociates from the opsin apoprotein rendering it insensitive to light. Restoring light sensitivity to apo-opsin requires thermal re-isomerization of all-trans-retinaldehyde to 11-cis-retinaldehyde via an enzyme pathway called the visual cycle in retinal pigment epithelial (RPE) cells. Vertebrates can see over a 10(8)-fold range of background illumination. This implies that the visual cycle can regenerate a visual chromophore over a similarly broad range. However, nothing is known about how the visual cycle is regulated. Here we show that RPE cells, functionally or physically separated from photoreceptors, respond to light by mobilizing all-trans-retinyl esters. These retinyl esters are substrates for the retinoid isomerase and hence critical for regenerating visual chromophore. We show in knock-out mice and by RNA interference in human RPE cells that this mobilization is mediated by a protein called "RPE-retinal G protein receptor" (RGR) opsin. These data establish that RPE cells are intrinsically sensitive to light. Finally, we show that in the dark, RGR-opsin inhibits lecithin:retinol acyltransferase and all-trans-retinyl ester hydrolase in vitro and that this inhibition is released upon exposure to light. The results of this study suggest that RGR-opsin mediates light-dependent translocation of all-trans-retinyl esters from a storage pool in lipid droplets to an "isomerase pool" in membranes of the endoplasmic reticulum. This translocation permits insoluble all-trans-retinyl esters to be utilized as substrate for the synthesis of a new visual chromophore.

Indexed as

AcyltransferasesAnimalsCarboxylic Ester HydrolasesCell Membranecis-trans-IsomerasesEndoplasmic ReticulumEpithelial CellsEye ProteinsHumansMiceMice, KnockoutPigment Epithelium of EyeReceptors, G-Protein-CoupledRetinaldehydeRetinoid IsomerohydrolaseRNA InterferenceAcyltransferasesCarboxylic Ester Hydrolasescis-trans-IsomerasesEye ProteinsG protein-coupled receptor RGRlecithin-retinol acyltransferaseReceptors, G-Protein-CoupledRetinaldehydeRetinoid Isomerohydrolaseretinyl esteraseRod Opsins

Identifiers

PMID18474598
PMCPMC2443657
OpenAlexW2087172463

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.