Role of noncovalent binding of 11-cis-retinal to opsin in dark adaptation of rod and cone photoreceptors

Vladimir J. Kefalov, Rosalie K. Crouch, M. Carter Cornwall

Research output: Contribution to journalArticlepeer-review

54 Scopus citations

Abstract

Regeneration of visual pigments of vertebrate rod and cone photoreceptors occurs by the initial noncovalent binding of 11-cis-retinal to opsin, followed by the formation of a covalent bond between the ligand and the protein. Here, we show that the noncovalent interaction between 11-cis-retinal and opsin affects the rate of dark adaptation. In rods, 11-cis-retinal produces a transient activation of the phototransduction cascade that precedes sensitivity recovery, thus slowing dark adaptation. In cones, 11-cis-retinal immediately deactivates phototransduction. Thus, the initial binding of the same ligand to two very similar G protein receptors, the rod and cone opsins, activates one and deactivates the other, contributing to the remarkable difference in the rates of rod and cone dark adaptation.

Original languageEnglish
Pages (from-to)749-755
Number of pages7
JournalNeuron
Volume29
Issue number3
DOIs
StatePublished - 2001

Fingerprint

Dive into the research topics of 'Role of noncovalent binding of 11-cis-retinal to opsin in dark adaptation of rod and cone photoreceptors'. Together they form a unique fingerprint.

Cite this