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J. Biol. Chem., Vol. 280, Issue 33, 29874-29884, August 19, 2005

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The Retinal G Protein-coupled Receptor (RGR) Enhances Isomerohydrolase Activity Independent of Light^*

From the ^aLaboratory for Retinal Cell Biology, University Hospital Zurich, Eye Clinic, 8091 Zurich, Switzerland, the ^cUniversity of Freiburg, Institute of Biology I, Animal Physiology and Neurobiology, 79104 Freiburg, Germany, the ^dDepartment of Ophthalmology, FM Kirby Center, Philadelphia, Pennsylvania 19104, the ^hJohn Curtin School of Medical Research, Australian National University, ACT 2601 Canberra, Australia, and the ⁱRetinal Electrodiagnostics Research Group, University Eye Hospital Tuebingen, Department of Pathophysiology of Vision and Neuroophthalmology, 72076 Tuebingen, Germany

Rod and cone visual pigments use 11-cis-retinal, a vitamin A derivative, as their chromophore. Light isomerizes 11-cis- into all-trans-retinal, triggering a conformational transition of the opsin molecule that initiates phototransduction. After bleaching all-trans-retinal leaves the opsin, and light sensitivity must be restored by regeneration of 11-cis-retinal. Under bright light conditions the retinal G protein-coupled receptor (RGR) was reported to support this regeneration by acting as a photoisomerase in a proposed photic visual cycle. We analyzed the contribution of RGR to rhodopsin regeneration under different light regimes and show that regeneration, during light exposure and in darkness, is slowed about 3-fold in Rgr^-/- mice. These findings are not in line with the proposed function of RGR as a photoisomerase. Instead, RGR, independent of light, accelerates the conversion of retinyl esters to 11-cis-retinal by positively modulating isomerohydrolase activity, a key step in the "classical" visual cycle. Furthermore, we find that light accelerates rhodopsin regeneration, independent of RGR.

Received for publication, April 1, 2005 , and in revised form, June 9, 2005.

^* The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The on-line version of this article (available at http://www.jbc.org) contains Figs. S1-S4.

^e Supported by the National Institutes of Health Grant EY02660 and the Research to Prevent Blindness Foundation.

^f Supported by Human Frontier Science Program Grant RGP0003/2003.

^g Supported by Australian Research Council Grant FF0344672.

^l Supported by the Ministry of Science, Research, and the Arts, Baden-Württemberg.

^j Supported by German Research Council Grants LI 9561/2, SE 837/4, and RE 318/2.

^k Supported by Swiss National Science Foundation Grant 3100-64917 and the Velux Foundation, Glarus, Switzerland.

^b To whom correspondence should be addressed: Laboratory for Retinal Cell Biology, ONO-EM, H-Lab-13, Sternwartstr. 14, 8091 Zurich, Switzerland. Tel.: 41-1-2553905; Fax: 41-1-2554385; E-mail: awenzel{at}opht.unizh.ch.

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