Light intensity-dependent arrestin switching for inactivation of a light-sensitive GPCR, bistable opsin
Summary: Inactivation of most light-sensitive G protein-coupled receptor (GPCR) opsins involves arrestin binding to terminate cell responses. In the zebrafish pineal organ, UV sensitive parapinopsin 1 (PP1)-expressing cells exhibit color opponency through photoequilibria between two photo-interconve...
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| Format: | Article |
| Language: | English |
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Elsevier
2025-02-01
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| Series: | iScience |
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| Online Access: | http://www.sciencedirect.com/science/article/pii/S258900422402933X |
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| author | Baoguo Shen Seiji Wada Tomohiro Sugihara Takashi Nagata Haruka Nishioka Emi Kawano-Yamashita Takeaki Ozawa Mitsumasa Koyanagi Akihisa Terakita |
| author_facet | Baoguo Shen Seiji Wada Tomohiro Sugihara Takashi Nagata Haruka Nishioka Emi Kawano-Yamashita Takeaki Ozawa Mitsumasa Koyanagi Akihisa Terakita |
| author_sort | Baoguo Shen |
| collection | DOAJ |
| description | Summary: Inactivation of most light-sensitive G protein-coupled receptor (GPCR) opsins involves arrestin binding to terminate cell responses. In the zebrafish pineal organ, UV sensitive parapinopsin 1 (PP1)-expressing cells exhibit color opponency through photoequilibria between two photo-interconvertible states of PP1. The amount of visible light-sensitive active states (photoproducts) is crucial for generating color opponency, raising questions about how and what arrestins are involved in PP1 inactivation. Here, we found two arrestins, Arr3a and Sagb competitively bind to PP1. Photoresponse analyses of the PP1 cells using gene-knockdown larvae revealed Arr3a-involved quick inactivation was switched to Sagb-involved moderate inactivation depending on increased light intensity. Furthermore, we found photoregeneration of PP1 facilitates the dissociation of the PP1-arrestin complex, allowing for continuous arrestin supply in the photoequilibria under strong light. These regulations for the active photoproduct amounts of PP1 may help maintain appropriate color opponency. The current findings provide insight into the dynamics of GPCR inactivation involving multiple arrestins. |
| format | Article |
| id | doaj-art-f47ff154a34d4b50bbb791620881072d |
| institution | Kabale University |
| issn | 2589-0042 |
| language | English |
| publishDate | 2025-02-01 |
| publisher | Elsevier |
| record_format | Article |
| series | iScience |
| spelling | doaj-art-f47ff154a34d4b50bbb791620881072d2025-01-26T05:04:33ZengElsevieriScience2589-00422025-02-01282111706Light intensity-dependent arrestin switching for inactivation of a light-sensitive GPCR, bistable opsinBaoguo Shen0Seiji Wada1Tomohiro Sugihara2Takashi Nagata3Haruka Nishioka4Emi Kawano-Yamashita5Takeaki Ozawa6Mitsumasa Koyanagi7Akihisa Terakita8Department of Biology, Graduate School of Science, Osaka Metropolitan University, 3-3-138 Sugimoto, Sumiyoshi-ku, Osaka 558-8585, Japan; Department of Biology and Geosciences, Graduate School of Science, Osaka City University, 3-3-138 Sugimoto, Sumiyoshi-ku, Osaka 558-8585, JapanDepartment of Biology, Graduate School of Science, Osaka Metropolitan University, 3-3-138 Sugimoto, Sumiyoshi-ku, Osaka 558-8585, Japan; Department of Biology and Geosciences, Graduate School of Science, Osaka City University, 3-3-138 Sugimoto, Sumiyoshi-ku, Osaka 558-8585, Japan; The OMU Advanced Research Institute for Natural Science and Technology, Osaka Metropolitan University, 3-3-138 Sugimoto, Sumiyoshi-ku, Osaka 558-8585, JapanDepartment of Biology, Graduate School of Science, Osaka Metropolitan University, 3-3-138 Sugimoto, Sumiyoshi-ku, Osaka 558-8585, Japan; Department of Biology and Geosciences, Graduate School of Science, Osaka City University, 3-3-138 Sugimoto, Sumiyoshi-ku, Osaka 558-8585, JapanDepartment of Biology and Geosciences, Graduate School of Science, Osaka City University, 3-3-138 Sugimoto, Sumiyoshi-ku, Osaka 558-8585, JapanDepartment of Biology and Geosciences, Graduate School of Science, Osaka City University, 3-3-138 Sugimoto, Sumiyoshi-ku, Osaka 558-8585, JapanDepartment of Biology and Geosciences, Graduate School of Science, Osaka City University, 3-3-138 Sugimoto, Sumiyoshi-ku, Osaka 558-8585, JapanDepartment of Chemistry, School of Science, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-0033, JapanDepartment of Biology, Graduate School of Science, Osaka Metropolitan University, 3-3-138 Sugimoto, Sumiyoshi-ku, Osaka 558-8585, Japan; Department of Biology and Geosciences, Graduate School of Science, Osaka City University, 3-3-138 Sugimoto, Sumiyoshi-ku, Osaka 558-8585, Japan; The OMU Advanced Research Institute for Natural Science and Technology, Osaka Metropolitan University, 3-3-138 Sugimoto, Sumiyoshi-ku, Osaka 558-8585, JapanDepartment of Biology, Graduate School of Science, Osaka Metropolitan University, 3-3-138 Sugimoto, Sumiyoshi-ku, Osaka 558-8585, Japan; Department of Biology and Geosciences, Graduate School of Science, Osaka City University, 3-3-138 Sugimoto, Sumiyoshi-ku, Osaka 558-8585, Japan; The OMU Advanced Research Institute for Natural Science and Technology, Osaka Metropolitan University, 3-3-138 Sugimoto, Sumiyoshi-ku, Osaka 558-8585, Japan; Corresponding authorSummary: Inactivation of most light-sensitive G protein-coupled receptor (GPCR) opsins involves arrestin binding to terminate cell responses. In the zebrafish pineal organ, UV sensitive parapinopsin 1 (PP1)-expressing cells exhibit color opponency through photoequilibria between two photo-interconvertible states of PP1. The amount of visible light-sensitive active states (photoproducts) is crucial for generating color opponency, raising questions about how and what arrestins are involved in PP1 inactivation. Here, we found two arrestins, Arr3a and Sagb competitively bind to PP1. Photoresponse analyses of the PP1 cells using gene-knockdown larvae revealed Arr3a-involved quick inactivation was switched to Sagb-involved moderate inactivation depending on increased light intensity. Furthermore, we found photoregeneration of PP1 facilitates the dissociation of the PP1-arrestin complex, allowing for continuous arrestin supply in the photoequilibria under strong light. These regulations for the active photoproduct amounts of PP1 may help maintain appropriate color opponency. The current findings provide insight into the dynamics of GPCR inactivation involving multiple arrestins.http://www.sciencedirect.com/science/article/pii/S258900422402933XBiochemistryProtein |
| spellingShingle | Baoguo Shen Seiji Wada Tomohiro Sugihara Takashi Nagata Haruka Nishioka Emi Kawano-Yamashita Takeaki Ozawa Mitsumasa Koyanagi Akihisa Terakita Light intensity-dependent arrestin switching for inactivation of a light-sensitive GPCR, bistable opsin iScience Biochemistry Protein |
| title | Light intensity-dependent arrestin switching for inactivation of a light-sensitive GPCR, bistable opsin |
| title_full | Light intensity-dependent arrestin switching for inactivation of a light-sensitive GPCR, bistable opsin |
| title_fullStr | Light intensity-dependent arrestin switching for inactivation of a light-sensitive GPCR, bistable opsin |
| title_full_unstemmed | Light intensity-dependent arrestin switching for inactivation of a light-sensitive GPCR, bistable opsin |
| title_short | Light intensity-dependent arrestin switching for inactivation of a light-sensitive GPCR, bistable opsin |
| title_sort | light intensity dependent arrestin switching for inactivation of a light sensitive gpcr bistable opsin |
| topic | Biochemistry Protein |
| url | http://www.sciencedirect.com/science/article/pii/S258900422402933X |
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