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

First Author  Nair KS Year  2005
Journal  Neuron Volume  46
Issue  4 Pages  555-67
PubMed ID  15944125 Mgi Jnum  J:99855
Mgi Id  MGI:3584071 Doi  10.1016/j.neuron.2005.03.023
Citation  Nair KS, et al. (2005) Light-dependent redistribution of arrestin in vertebrate rods is an energy-independent process governed by protein-protein interactions. Neuron 46(4):555-67
abstractText  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.
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