MEMBRANE PROTEIN STRUCTURE AND FUNCTION
The primary interest in our laboratory is the mechanism by which photosensory receptors sense and transmit information concerning the color, intensity, and pattern of light in the environment. We study a widespread class of photoactive receptor proteins (rhodopsins) that consist of seven transmembrane helices connected by interhelical loops. The helices form a pocket for the photosensitive molecule vitamin-A aldehyde (retinal), and the receptor proteins physically couple to protein transducers that relay signals to sensory pathways in the cytoplasm. These photosensitive heptahelical proteins are used for visual processes of various degrees of sophistication, ranging from detection of light-dark boundaries, light gradients, and light direction by single-cell microorganisms to high-resolution color image detection by higher animal eyes.
Left: Sensory Rhodopsin II and its transducer, responsible for phototaxis signaling in haloarchaea. Middle: A cyanobacterial sensory rhodopsin of unknown function and its interacting partner (in Anabaena).
Right: ChR1, one of the channelrhodopsins that mediates phototaxis in eukaryotic algae. Channelrhodopsins have begun to be used extensively for photocontrol of neuronal activity in brain circuitry mapping and vision restoration experiments.
UTHealth Medical School
Department of Biochemistry and Molecular Biology
Center for Membrane Biology
6431 Fannin Street, MSB 6.200
Houston, Texas 77030
713-500-5473 Direct 713-500-0652 Fax
Ph.D. - University of California, Berkeley
Jane Coffin Childs Postdoctoral Fellow - Harvard Medical School
Light sensors & photosensory transduction, Microbial rhodopsins, Membrane receptor structure/function, Optogenetics
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