An all-trans-retinal-binding opsin peropsin as a potential dark-active and light-inactivated G protein-coupled receptor

Abstract Peropsin or retinal pigment epithelium-derived rhodopsin homolog, found in many animals, belongs to the opsin family. Most opsins bind to 11-cis-retinal as a chromophore and act as light-activated G protein-coupled receptors. Some peropsins, however, bind all-trans-retinal and isomerise it...

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Autores principales:	Takashi Nagata, Mitsumasa Koyanagi, Robert Lucas, Akihisa Terakita
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2018
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/d18520f553714f13b8282823c4ba8f83
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spelling	oai:doaj.org-article:d18520f553714f13b8282823c4ba8f832021-12-02T15:08:17ZAn all-trans-retinal-binding opsin peropsin as a potential dark-active and light-inactivated G protein-coupled receptor10.1038/s41598-018-21946-12045-2322https://doaj.org/article/d18520f553714f13b8282823c4ba8f832018-02-01T00:00:00Zhttps://doi.org/10.1038/s41598-018-21946-1https://doaj.org/toc/2045-2322Abstract Peropsin or retinal pigment epithelium-derived rhodopsin homolog, found in many animals, belongs to the opsin family. Most opsins bind to 11-cis-retinal as a chromophore and act as light-activated G protein-coupled receptors. Some peropsins, however, bind all-trans-retinal and isomerise it into 11-cis form by light, and peropsin has been suggested to supply other visual opsins with 11-cis-retinal. Additionally, peropsin has some amino acid sequence motifs that are highly conserved among G protein-coupled opsins. Here, using chimeric mutant peropsins, we found that peropsin potentially generates an “active form” that drives G-protein signalling in the dark by binding to all-trans-retinal and that the active form photo-converts to an inactive form containing 11-cis-retinal. Comparative spectroscopic analysis demonstrated that spider peropsin exhibited catalytic efficiency for retinal photoisomerisation that was much lower than a retinal photoisomerase, squid retinochrome. The chimeric peropsins, constructed by replacing the third intracellular loop region with that of Gs- or Gi-coupled opsin, were active and drove Gs- or Gi-mediated signalling in the dark, respectively, and were inactivated upon illumination in mammalian cultured cells. These results suggest that peropsin acts as a dark-active, light-inactivated G protein-coupled receptor and is useful as a novel optogenetic tool.Takashi NagataMitsumasa KoyanagiRobert LucasAkihisa TerakitaNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 8, Iss 1, Pp 1-7 (2018)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Takashi Nagata Mitsumasa Koyanagi Robert Lucas Akihisa Terakita An all-trans-retinal-binding opsin peropsin as a potential dark-active and light-inactivated G protein-coupled receptor
description	Abstract Peropsin or retinal pigment epithelium-derived rhodopsin homolog, found in many animals, belongs to the opsin family. Most opsins bind to 11-cis-retinal as a chromophore and act as light-activated G protein-coupled receptors. Some peropsins, however, bind all-trans-retinal and isomerise it into 11-cis form by light, and peropsin has been suggested to supply other visual opsins with 11-cis-retinal. Additionally, peropsin has some amino acid sequence motifs that are highly conserved among G protein-coupled opsins. Here, using chimeric mutant peropsins, we found that peropsin potentially generates an “active form” that drives G-protein signalling in the dark by binding to all-trans-retinal and that the active form photo-converts to an inactive form containing 11-cis-retinal. Comparative spectroscopic analysis demonstrated that spider peropsin exhibited catalytic efficiency for retinal photoisomerisation that was much lower than a retinal photoisomerase, squid retinochrome. The chimeric peropsins, constructed by replacing the third intracellular loop region with that of Gs- or Gi-coupled opsin, were active and drove Gs- or Gi-mediated signalling in the dark, respectively, and were inactivated upon illumination in mammalian cultured cells. These results suggest that peropsin acts as a dark-active, light-inactivated G protein-coupled receptor and is useful as a novel optogenetic tool.
format	article
author	Takashi Nagata Mitsumasa Koyanagi Robert Lucas Akihisa Terakita
author_facet	Takashi Nagata Mitsumasa Koyanagi Robert Lucas Akihisa Terakita
author_sort	Takashi Nagata
title	An all-trans-retinal-binding opsin peropsin as a potential dark-active and light-inactivated G protein-coupled receptor
title_short	An all-trans-retinal-binding opsin peropsin as a potential dark-active and light-inactivated G protein-coupled receptor
title_full	An all-trans-retinal-binding opsin peropsin as a potential dark-active and light-inactivated G protein-coupled receptor
title_fullStr	An all-trans-retinal-binding opsin peropsin as a potential dark-active and light-inactivated G protein-coupled receptor
title_full_unstemmed	An all-trans-retinal-binding opsin peropsin as a potential dark-active and light-inactivated G protein-coupled receptor
title_sort	all-trans-retinal-binding opsin peropsin as a potential dark-active and light-inactivated g protein-coupled receptor
publisher	Nature Portfolio
publishDate	2018
url	https://doaj.org/article/d18520f553714f13b8282823c4ba8f83
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An all-trans-retinal-binding opsin peropsin as a potential dark-active and light-inactivated G protein-coupled receptor

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