Light-dependent redistribution of arrestin in vertebrate rods is an energy-independent process governed by protein-protein interactions.

Nair KS, Hanson SM, Mendez A, Gurevich EV, Kennedy MJ, Shestopalov VI, Vishnivetskiy SA, Chen J, Hurley JB, Gurevich VV, Slepak VZ
Neuron. 2005 46 (4): 555-67

PMID: 15944125 · PMCID: PMC2752952 · DOI:10.1016/j.neuron.2005.03.023

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.

MeSH Terms (34)

Adenosine Triphosphate Animals Arrestin Binding Sites Blotting, Western Cytoskeleton Dark Adaptation Deoxyglucose Energy Metabolism Enzyme Activation Eye Proteins Fluorescent Antibody Technique G-Protein-Coupled Receptor Kinase 1 Glucose Green Fluorescent Proteins Hydroxylamine In Vitro Techniques Light Mice Mice, Inbred C57BL Mice, Transgenic Microtubules Mutagenesis Phosphorylation Potassium Cyanide Protein Binding Protein Kinases Protein Transport Retina Retinal Rod Photoreceptor Cells Rhodopsin Rod Opsins Time Factors Transducin

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