Journal
NATURE GENETICS
Volume 28, Issue 3, Pages 256-260Publisher
NATURE AMERICA INC
DOI: 10.1038/90089
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- NEI NIH HHS [EY03040, EY08364] Funding Source: Medline
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During visual excitation, rhodopsin undergoes photoactivation and bleaches to opsin and all-trans-retinal(1,2). To regenerate rhodopsin and maintain normal visual sensitivity, the all-trans isomer must be metabolized and reisomerized to produce the chromophore 11-cis-retinal in biochemical steps that constitute the visual cycle and involve the retinal pigment epithelium (RPE; refs, 3-8). A key step in the visual cycle is isomerization of an all-trans retinoid to 11-cis-retinol in the RPE (refs, 9-11). It could be that the retinochrome-like opsins. peropsin, or the retinal G protein-coupled receptor (RGR) opsin12-16 are isomerases in the RPE. In contrast to visual pigments. RGR is bound predominantly to endogenous all-transretinal, and irradiation of RGR in vitro results in stereospecific conversion of the bound all-trans isomer to 11-cis-retinal(17). Here we show that RGR is involved in the formation of 11-cis-retinal in mice and functions in a light-dependent pathway of the rod visual cycle. Mutations in the human gene encoding RGR are associated with retinitis pigmentosa(18).
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