RRC ID 52719
Author Sato K, Yamashita T, Ohuchi H, Takeuchi A, Gotoh H, Ono K, Mizuno M, Mizutani Y, Tomonari S, Sakai K, Imamoto Y, Wada A, Shichida Y.
Title Opn5L1 is a retinal receptor that behaves as a reverse and self-regenerating photoreceptor.
Journal Nat Commun
Abstract Most opsins are G protein-coupled receptors that utilize retinal both as a ligand and as a chromophore. Opsins' main established mechanism is light-triggered activation through retinal 11-cis-to-all-trans photoisomerization. Here we report a vertebrate non-visual opsin that functions as a Gi-coupled retinal receptor that is deactivated by light and can thermally self-regenerate. This opsin, Opn5L1, binds exclusively to all-trans-retinal. More interestingly, the light-induced deactivation through retinal trans-to-cis isomerization is followed by formation of a covalent adduct between retinal and a nearby cysteine, which breaks the retinal-conjugated double bond system, probably at the C11 position, resulting in thermal re-isomerization to all-trans-retinal. Thus, Opn5L1 acts as a reverse photoreceptor. We conclude that, like vertebrate rhodopsin, Opn5L1 is a unidirectional optical switch optimized from an ancestral bidirectional optical switch, such as invertebrate rhodopsin, to increase the S/N ratio of the signal transduction, although the direction of optimization is opposite to that of vertebrate rhodopsin.
Volume 9(1)
Pages 1255
Published 2018-3-28
DOI 10.1038/s41467-018-03603-3
PII 10.1038/s41467-018-03603-3
PMID 29593298
PMC PMC5871776
MeSH Animals Chickens Chromatography, High Pressure Liquid Factor Xa / chemistry HEK293 Cells Humans In Situ Hybridization Light Male Opsins / chemistry* Photoreceptor Cells Photoreceptor Cells, Vertebrate / chemistry* Protein Binding Recombinant Proteins / chemistry Regeneration Retinaldehyde / metabolism Rhodopsin / chemistry Signal Transduction Vitamin A / chemistry Xenopus / metabolism
IF 12.121
Times Cited 0
Resource
Clawed frogs / Newts Xenopus tropicalis