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The Journal of Neuroscience, July 9, 2003, 23(14):6152-6160
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GRK1-Dependent Phosphorylation of S and M Opsins and Their Binding to Cone Arrestin during Cone Phototransduction in the Mouse Retina
Xuemei Zhu,1 Bruce Brown,1 Aimin Li,1 Alan J. Mears,2,3 Anand Swaroop,2,3 andCheryl M. Craft1 1The Mary D. Allen Laboratory for Vision Research, Doheny Eye Institute, Department of Cell and Neurobiology, the Keck School of Medicine of the University of Southern California, Los Angeles, California 90089-9112, and Departments of 2Ophthalmology and Visual Sciences and 3Human Genetics, University of Michigan, Ann Arbor, Michigan 48105
The shutoff mechanisms of the rod visual transduction cascade involve G-protein-coupled receptor (GPCR) kinase 1 (GRK1) phosphorylation of light-activated rhodopsin (R*) followed by rod arrestin binding. Deactivation of the cone phototransduction cascade in the mammalian retina is delineated poorly. In this study we sought to explore the potential mechanisms underlying the quenching of the phototransduction cascade in cone photoreceptors by using mouse models lacking rods and/or GRK1. Using the "pure-cone" retinas of the neural retina leucine zipper (Nrl) knock-out (KO, -/-) mice (Mears et al., 2001), we have demonstrated the light-dependent, multi-site phosphorylation of both S and M cone opsins by in situ phosphorylation and isoelectric focusing. Immunoprecipitation with affinity-purified polyclonal antibodies against either mouse cone arrestin (mCAR) or mouse S and M cone opsins revealed specific binding of mCAR to light-activated, phosphorylated cone opsins. To elucidate the potential role of GRK1 in cone opsin phosphorylation, we created Nrl and Grk1 double knock-out (Nrl-/-Grk1-/-) mice by crossing the Nrl-/- mice with Grk1-/- mice (Chen et al., 1999). We found that, in the retina of these mice, the light-activated cone opsins were neither phosphorylated nor bound with mCAR. Our results demonstrate, for the first time in a mammalian species, that cone opsins are phosphorylated and that CAR binds to phosphorylated cone opsins after light activation.
Key words: cone opsin; phosphorylation; cone arrestin; phototransduction; coimmunoprecipitation; mouse retina
Received Jan. 16, 2003; revised May. 20, 2003; accepted May. 23, 2003.
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