Activating an invertebrate bistable opsin with the all-trans 6.11 retinal analog.

Autor:	Rodrigues MJ; Laboratory of Biomolecular Research, Department of Biology and Chemistry, Paul Scherrer Institute, Villigen 5232, Switzerland., Tejero O; Laboratory of Biomolecular Research, Department of Biology and Chemistry, Paul Scherrer Institute, Villigen 5232, Switzerland.; Department of Biology, ETH-Zurich, Zurich, Switzerland., Mühle J; Laboratory of Biomolecular Research, Department of Biology and Chemistry, Paul Scherrer Institute, Villigen 5232, Switzerland., Pamula F; Laboratory of Biomolecular Research, Department of Biology and Chemistry, Paul Scherrer Institute, Villigen 5232, Switzerland., Das I; Department of Molecular Chemistry and Materials Science, Weizmann Institute of Science, 76100 Rehovot, Israel., Tsai CJ; Laboratory of Biomolecular Research, Department of Biology and Chemistry, Paul Scherrer Institute, Villigen 5232, Switzerland., Terakita A; Department of Biology, Graduate School of Science, Osaka Metropolitan University, Osaka 558-8585, Japan.; The Osaka Metropolitan University Advanced Research Institute for Natural Science and Technology, Osaka Metropolitan University, Osaka 558-8585, Japan., Sheves M; Department of Molecular Chemistry and Materials Science, Weizmann Institute of Science, 76100 Rehovot, Israel., Schertler GFX; Laboratory of Biomolecular Research, Department of Biology and Chemistry, Paul Scherrer Institute, Villigen 5232, Switzerland.
Jazyk:	angličtina
Zdroj:	Proceedings of the National Academy of Sciences of the United States of America [Proc Natl Acad Sci U S A] 2024 Jul 30; Vol. 121 (31), pp. e2406814121. Date of Electronic Publication: 2024 Jul 23.
DOI:	10.1073/pnas.2406814121
Abstrakt:	Animal vision depends on opsins, a category of G protein-coupled receptor (GPCR) that achieves light sensitivity by covalent attachment to retinal. Typically binding as an inverse agonist, 11-cis retinal photoisomerizes to the all-trans isomer and activates the receptor, initiating downstream signaling cascades. Retinal bound to bistable opsins isomerizes back to the 11-cis state after absorption of a second photon, inactivating the receptor. Bistable opsins are essential for invertebrate vision and nonvisual light perception across the animal kingdom. While crystal structures are available for bistable opsins in the inactive state, it has proven difficult to form homogeneous populations of activated bistable opsins either via illumination or reconstitution with all-trans retinal. Here, we show that a nonnatural retinal analog, all-trans retinal 6.11 (ATR6.11), can be reconstituted with the invertebrate bistable opsin, Jumping Spider Rhodopsin-1 (JSR1). Biochemical activity assays demonstrate that ATR6.11 functions as a JSR1 agonist. ATR6.11 binding also enables complex formation between JSR1 and signaling partners. Our findings demonstrate the utility of retinal analogs for biophysical characterization of bistable opsins, which will deepen our understanding of light perception in animals. Competing Interests: Competing interests statement:The authors declare no competing interest.
Databáze:	MEDLINE
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