Serine and threonine phosphorylation sites work in concert to provide rapid and reproducible desensitization of the G-protein coupled receptor rhodopsin.

UV-Vis- and IR-spectroscopy provides insights into the light-induced enzyme activity of a rhodopsin guanylyl cyclase by tracking the substrate turnover with atomic resolution in real-time and correlating it with the structural changes of the protein.

Through a single mutation at position 188, vertebrate rhodopsin acquires the ability to recover the dark state from the active state by a thermal reaction and by a photoreaction.

Photoreceptor genomic binding of a 20 base-pair-long DNA sequence by a synthetic DNA-binding protein turns off Rhodopsin expression.

Rather than relying on intrinsic intracellular targeting information, the key phototransduction enzyme guanylate cyclase 1 is delivered to the photosensory cilium with the visual pigment rhodopsin.

A membrane protein complex in the endoplasmic reticulum is a key factor for the biogenesis of multi-pass transmembrane proteins, including Rh1, and its loss causes retinal degeneration.

The evolution of the light-sensitive visual pigment rhodopsin involved functional tradeoffs that may have sacrificed rod photosensitivity for active-state protein stability to mitigate phototoxicity in tetrapods, but not in fishes.

Animal G-protein-coupled bistable rhodopsins can regulate Gq- and Gi-mediated signaling in a light-dependent manner in neurons and cardiomyocytes, making them useful for analyzing the roles of GPCR signaling in vivo.

Functional assays using zebrafish reveal that various microbial channelrhodopsins, guanylyl cyclase rhodopsin, and photoactivated adenylyl cyclases function as potent optogenetic tools, effectively controlling neural activity and cardiac function in zebrafish.

The structure of a light-sensitive G protein-coupled receptor in complex with a Gi-protein heterotrimer provides a structural foundation for the role of the receptor C-terminal tail in scaffolding and signaling.