Control of rhodopsin activity in vision

Denis A. Baylor, Marie E Burns

Research output: Contribution to journalArticle

39 Scopus citations

Abstract

Although rhodopsin's role in activating the phototransduction cascade is well known, the processes that deactivate rhodopsin, and thus the rest of the cascade, are less well understood. At least three proteins appear to play a role: rhodopsin kinase, arrestin and recoverin. Here we review recent physiological studies of the molecular mechanisms of rhodopsin deactivation. The approach was to monitor the light responses of individual mouse rods in which rhodopsin was altered or arrestin was deleted by transgenic techniques. Removal of rhodopsin's carboxy-terminal residues which contain phosphorylation sites implicated in deactivation, prolonged the flash response 20-fold and caused it to become highly variable. In rods that did not express arrestin the flash response recovered partially, but final recovery was slowed over 100-fold. These results are consistent with the notion that phosphorylation initiates rhodopsin deactivation and that arrestin binding completes the process. The stationary night blindness of Oguchi disease, associated with null mutations in the genes for arrestin or rhodopsin kinase, presumably results from impaired rhodopsin deactivation, like that revealed by the experiments on transgenic animals.

Original languageEnglish (US)
Pages (from-to)521-525
Number of pages5
JournalEye
Volume12
Issue number3 B
StatePublished - Jun 1998
Externally publishedYes

Keywords

  • Arrestin
  • Kinase
  • Night blindness
  • Rhodopsin
  • Rod
  • Transgenic

ASJC Scopus subject areas

  • Ophthalmology
  • Sensory Systems

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    Baylor, D. A., & Burns, M. E. (1998). Control of rhodopsin activity in vision. Eye, 12(3 B), 521-525.