Active state structures of a bistable visual opsin bound to G proteins

Oliver Tejero, Filip Pamula, Mitsumasa Koyanagi, Takashi Nagata, Pavel Afanasyev, Ishita Das, Xavier Deupi, Mordechai Sheves, Akihisa Terakita, Gebhard F. X. Schertler (), Matthew J. Rodrigues () and Ching-Ju Tsai ()
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Oliver Tejero: PSI Center for Life Sciences
Filip Pamula: PSI Center for Life Sciences
Mitsumasa Koyanagi: Osaka Metropolitan University
Takashi Nagata: Osaka City University
Pavel Afanasyev: ETH Zurich
Ishita Das: Weizmann Institute of Science
Xavier Deupi: PSI Center for Life Sciences
Mordechai Sheves: Weizmann Institute of Science
Akihisa Terakita: Osaka Metropolitan University
Gebhard F. X. Schertler: PSI Center for Life Sciences
Matthew J. Rodrigues: PSI Center for Life Sciences
Ching-Ju Tsai: PSI Center for Life Sciences

Nature Communications, 2024, vol. 15, issue 1, 1-13

Abstract: Abstract Opsins are G protein-coupled receptors (GPCRs) that have evolved to detect light stimuli and initiate intracellular signaling cascades. Their role as signal transducers is critical to light perception across the animal kingdom. Opsins covalently bind to the chromophore 11-cis retinal, which isomerizes to the all-trans isomer upon photon absorption, causing conformational changes that result in receptor activation. Monostable opsins, responsible for vision in vertebrates, release the chromophore after activation and must bind another retinal molecule to remain functional. In contrast, bistable opsins, responsible for non-visual light perception in vertebrates and for vision in invertebrates, absorb a second photon in the active state to return the chromophore and protein to the inactive state. Structures of bistable opsins in the activated state have proven elusive, limiting our understanding of how they function as bidirectional photoswitches. Here we present active state structures of a bistable opsin, jumping spider rhodopsin isoform-1 (JSR1), in complex with its downstream signaling partners, the Gi and Gq heterotrimers. These structures elucidate key differences in the activation mechanisms between monostable and bistable opsins, offering essential insights for the rational engineering of bistable opsins into diverse optogenetic tools to control G protein signaling pathways.

Date: 2024
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DOI: 10.1038/s41467-024-53208-2

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