Light-Dependent Redistribution of Arrestin in Vertebrate Rods Is an Energy-Independent Process Governed by Protein-Protein Interactions
Copyright policy )Light-Dependent Redistribution of Arrestin in Vertebrate Rods Is an Energy-Independent Process Governed by Protein-Protein Interactions
In rod photoreceptors, arrestin localizes to the outer segment (OS) in the light and to the inner segment (IS) in the dark. Here, we demonstrate that redistribution of arrestin between these compartments can proceed in ATP-depleted photoreceptors. Translocation of transducin from the IS to the OS also does not require energy, but depletion of ATP or GTP inhibits its reverse movement. A sustained presence of activated rhodopsin is required for sequestering arrestin in the OS, and the rate of arrestin relocalization to the OS is determined by the amount and the phosphorylation status of photolyzed rhodopsin. Interaction of arrestin with microtubules is increased in the dark. Mutations that enhance arrestin-microtubule binding attenuate arrestin translocation to the OS. These results indicate that the distribution of arrestin in rods is controlled by its dynamic interactions with rhodopsin in the OS and microtubules in the IS and that its movement occurs by simple diffusion.
- Miami University United States
- University of California System United States
- Vanderbilt University United States
- University of Mary United States
- University of Washington United States
Arrestin, Binding Sites, Light, G-Protein-Coupled Receptor Kinase 1, Neuroscience(all), Blotting, Western, Green Fluorescent Proteins, Fluorescent Antibody Technique, Dark Adaptation, Hydroxylamine, Deoxyglucose, In Vitro Techniques, Enzyme Activation, Mice, Inbred C57BL, Mice, Adenosine Triphosphate, Glucose, Animals, Energy Metabolism, Eye Proteins, Cytoskeleton
Arrestin, Binding Sites, Light, G-Protein-Coupled Receptor Kinase 1, Neuroscience(all), Blotting, Western, Green Fluorescent Proteins, Fluorescent Antibody Technique, Dark Adaptation, Hydroxylamine, Deoxyglucose, In Vitro Techniques, Enzyme Activation, Mice, Inbred C57BL, Mice, Adenosine Triphosphate, Glucose, Animals, Energy Metabolism, Eye Proteins, Cytoskeleton
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