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The Journal of Neuroscience, April 15, 2003, 23(8):3124
BRIEF COMMUNICATION
Light-Dependent Translocation of Arrestin in the Absence of Rhodopsin Phosphorylation and Transducin SignalingAna Mendez1, Janis Lem4, Melvin Simon5, and Jeannie Chen1, 2, 3 1 Zilkha Neurogenetic Institute, The Mary D. Allen Laboratory for Vision Research, Beckman Macular Research Center, Doheny Eye Institute and Departments of 2 Ophthalmology and 3 Cell and Neurobiology, Keck School of Medicine of the University of Southern California, Los Angeles, California 90089, 4 Department of Ophthalmology, Molecular Cardiology Research Institute and Program in Genetics, New England Medical Center and Tufts University School of Medicine, Boston, Massachusetts 02111, and 5 Division of Biology, California Institute of Technology, Pasadena, California 91125
Visual arrestin plays a crucial role in the termination of the light response in vertebrate photoreceptors by binding selectively to light-activated, phosphorylated rhodopsin. Arrestin localizes predominantly to the inner segments and perinuclear region of dark-adapted rod photoreceptors, whereas light induces redistribution of arrestin to the rod outer segments. The mechanism by which arrestin redistributes in response to light is not known, but it is thought to be associated with the ability of arrestin to bind photolyzed, phosphorylated rhodopsin in the outer segment. In this study, we show that light-driven translocation of arrestin is unaffected in two different mouse models in which rhodopsin phosphorylation is lacking. We further show that arrestin movement is initiated by rhodopsin but does not require transducin signaling. These results exclude passive diffusion and point toward active transport as the mechanism for light-dependent arrestin movement in rod photoreceptor cells.
Key words: arrestin; transducin; RPE65; rhodopsin phosphorylation; rod photoreceptor; retina
Copyright © 2003 Society for Neuroscience 0270-6474/03/2383124-06$05.00/0
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