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

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.

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.

Binding site affinity and transcription factor levels are finely tuned in nature to regulate stochastic expression, setting the ratio of alternative photoreceptor fates and determining color preference.

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.

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.

A combination of state-of-the-art biochemical, biophysical, and computational methods revealed that water molecules play a central role in signal propagation through G protein-coupled receptors.

Engineered anion-conducting channelrhodopsins with enhanced red-light sensitivity and accelerated kinetics enable precise, low-intensity optical silencing of neurons, advancing optogenetic control in neuroscience research.

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.

The mechanism of signaling receptor delivery to primary cilia involves a specific cellular role of a Rab protein that is critical for vertebrate development.