Opn5L1 is a retinal receptor that behaves as a reverse and self-regenerating photoreceptor

Keita Sato, Takahiro Yamashita, Hideyo Ohuchi, Atsuko Takeuchi, Hitoshi Gotoh, Katsuhiko Ono, Misao Mizuno, Yasuhisa Mizutani, Sayuri Tomonari, Kazumi Sakai, Yasushi Imamoto, Akimori Wada and Yoshinori Shichida ()
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Keita Sato: Okayama University Graduate School of Medicine, Dentistry and Pharmaceutical Sciences
Takahiro Yamashita: Kyoto University
Hideyo Ohuchi: Okayama University Graduate School of Medicine, Dentistry and Pharmaceutical Sciences
Atsuko Takeuchi: Kobe Pharmaceutical University
Hitoshi Gotoh: Kyoto Prefectural University of Medicine
Katsuhiko Ono: Kyoto Prefectural University of Medicine
Misao Mizuno: Osaka University
Yasuhisa Mizutani: Osaka University
Sayuri Tomonari: Tokushima University
Kazumi Sakai: Kyoto University
Yasushi Imamoto: Kyoto University
Akimori Wada: Kobe Pharmaceutical University
Yoshinori Shichida: Kyoto University

Nature Communications, 2018, vol. 9, issue 1, 1-10

Abstract: 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.

Date: 2018
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DOI: 10.1038/s41467-018-03603-3

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