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, Yoshinori Shichida

Research output: Contribution to journalArticlepeer-review

2 Citations (Scopus)

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.

Original languageEnglish
Article number1255
JournalNature communications
Volume9
Issue number1
DOIs
Publication statusPublished - Dec 1 2018

ASJC Scopus subject areas

  • Chemistry(all)
  • Biochemistry, Genetics and Molecular Biology(all)
  • Physics and Astronomy(all)

Fingerprint Dive into the research topics of 'Opn5L1 is a retinal receptor that behaves as a reverse and self-regenerating photoreceptor'. Together they form a unique fingerprint.

Cite this