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

Sato, Keita, Yamashita, Takahiro, Ohuchi, Hideyo, Takeuchi, Atsuko, Gotoh, Hitoshi, Ono, Katsuhiko, Mizuno, Misao, Mizutani, Yasuhisa, Tomonari, Sayuri, Sakai, Kazumi, Imamoto, Yasushi, Wada, Akimori, Shichida, Yoshinori

doi:10.1038/s41467-018-03603-3

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.

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

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