Phosphorylation of non-bleached rhodopsin in intact retinas and living frogs.

@article{Binder1996PhosphorylationON,
  title={Phosphorylation of non-bleached rhodopsin in intact retinas and living frogs.},
  author={Brad M Binder and T M O'Connor and M. Deric Bownds and Vadim Y Arshavsky},
  journal={The Journal of biological chemistry},
  year={1996},
  volume={271 33},
  pages={19826-30}
}
The photoresponse in retinal photoreceptors begins when a molecule of rhodopsin is excited by a photon of light. Photoexcited rhodopsin activates an enzymatic cascade including the G-protein transducin and cyclic GMP phosphodiesterase. As a result, cytoplasmic cyclic GMP concentration is decreased and the photoresponse is initiated. This process is terminated when rhodopsin is phosphorylated by rhodopsin kinase and subsequently blocked by a protein called arrestin. It has been noted by several… CONTINUE READING

Citations

Publications citing this paper.
Showing 1-10 of 11 extracted citations

G Protein-Coupled Receptor Genetics

Methods in Pharmacology and Toxicology • 2014
View 20 Excerpts
Highly Influenced

Rhodopsin phosphorylation: 30 years later.

Progress in retinal and eye research • 2003
View 4 Excerpts
Highly Influenced

Effect of Rhodopsin Phosphorylation on Dark Adaptation in Mouse Rods.

The Journal of neuroscience : the official journal of the Society for Neuroscience • 2016
View 1 Excerpt

Involvement of distinct arrestin-1 elements in binding to different functional forms of rhodopsin.

Proceedings of the National Academy of Sciences of the United States of America • 2013

Similar Papers

Loading similar papers…