Rhodopsins are the members of the family of G protein-coupled receptors (GPCRs). It is considered that rhodopsins have diverged from ligand-binding GPCRs. Vertebrate rhodopsins can bind the inverse-agonist (or antagonist) 11-
cis-retinal but cannot bind the agonist
all-trans-retinal. In this study, we found that unlike vertebrate rhodopsin, amphioxus rhodopsin can bind the agonist
all-trans-retinal, showing that the amphioxus rhodopsin has characteristics of both photoreceptive rhodopsins and ligand-binding GPCRs. Mutational analyses revealed the molecular mechanism that reduces dark noise of visual cells during the molecular evolution of rhodopsins. A possibility of the amphioxus rhodopsin as a GPCR model was also discussed.
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