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Updated: Jul 19, 2026

A Rhodopsin Transport Assay by High-Content Imaging Analysis
Published on: January 16, 2019
The multitalented microbial sensory rhodopsins
1Center for Membrane Biology, Department of Biochemistry and Molecular Biology, University of Texas Medical School at Houston, Houston, TX 77030, USA. john.L.spudich@uth.tmc.edu
Abstract:
Sensory rhodopsins are photoactive, membrane-embedded seven-transmembrane helix receptors that use retinal as a chromophore. They are widespread in the microbial world in each of the three domains of life: Archaea, Bacteria and Eukarya. A striking characteristic of these photoreceptors is their different modes of signaling in different organisms, including interaction with other membrane proteins, interaction with cytoplasmic transducers and light-controlled Ca(2+) channel activity. More than two decades since the discovery of the first sensory rhodopsins in the archaeon Halobacterium salinarum, genome projects have revealed a widespread presence of homologous photosensors. New work on cyanobacteria, algae, fungi and marine proteobacteria is revealing how evolution has modified the common design of these proteins to produce a remarkably rich diversity in their signaling biochemistry.
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