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J. Biol. Chem., Vol. 280, Issue 8, 6861-6871, February 25, 2005

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Dynamics of Arrestin-Rhodopsin Interactions

ARRESTIN AND RETINAL RELEASE ARE DIRECTLY LINKED EVENTS^*

Martha E. Sommer, W. Clay Smith, and David L. Farrens¶

From the Department of Biochemistry and Molecular Biology, Oregon Health and Science University, Portland, Oregon 97239-3098 and the Departments of Ophthalmology and Neuroscience, University of Florida, Gainesville, Florida 32610-0284

In this study, we address the mechanism of visual arrestin release from light-activated rhodopsin using fluorescently labeled arrestin mutants. We find that two mutants, I72C and S251C, when labeled with the small, solvent-sensitive fluorophore monobromobimane, exhibit spectral changes only upon binding light-activated, phosphorylated rhodopsin. Our analysis indicates that these changes are probably due to a burying of the probes at these sites in the rhodopsin-arrestin or phospholipid-arrestin interface. Using a fluorescence approach based on this observation, we demonstrate that arrestin and retinal release are linked and are described by similar activation energies. However, at physiological temperatures, we find that arrestin slows the rate of retinal release 2-fold and abolishes the pH dependence of retinal release. Using fluorescence, EPR, and biochemical approaches, we also find intriguing evidence that arrestin binds to a post-Meta II photodecay product, possibly Meta III. We speculate that arrestin regulates levels of free retinal in the rod cell to help limit the formation of damaging oxidative retinal adducts. Such adducts may contribute to diseases like atrophic age-related macular degeneration (AMD). Thus, arrestin may serve to both attenuate rhodopsin signaling and protect the cell from excessive retinal levels under bright light conditions.

Received for publication, October 5, 2004 , and in revised form, December 6, 2004.

^* This work was supported in part by National Institutes of Health Grants EY12095 and DA14896 (to D. L. F.) and EY06225 (to W. C. S.), an unrestricted grant from Research to Prevent Blindness (to the Department of Ophthalmology at the University of Florida), a National Defense Science and Engineering Graduate Fellowship, and an N. L. Tartar Research Fellowship (to M. E. S.). 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.

^¶ To whom correspondence should be addressed. Tel.: 503-494-0583; Fax: 503-494-8393; E-mail: farrensd{at}ohsu.edu.

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