John Spudich, Ph.D.
Professor and Robert A. Welch Distinguished Chair in Chemistry; Director, Center for Membrane Biology; Fellow, American Academy of Arts & Sciences


Description of Research

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.

spudich_webfig

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.

Contact Information

John.L.Spudich@uth.tmc.edu

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

Education

Ph.D. - University of California, Berkeley

Jane Coffin Childs Postdoctoral Fellow - Harvard Medical School

Research Interests

Light sensors & photosensory transduction, Microbial rhodopsins, Membrane receptor structure/function, Optogenetics

Publications

Characterization of a highly efficient blue-shifted channelrhodopsin from the marine alga Platymonas subcordiformis.

Govorunova EG, Sineshchekov OA, Li H, Janz R, Spudich JL.

J Biol Chem. 2013 Oct 11;288(41):29911-22. doi: 10.1074/jbc.M113.505495. Epub 2013 Aug 30.

PMCID:  PMC3795289

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Cross-protomer interaction with the photoactive site in oligomeric proteorhodopsin complexes.

Ran T, Ozorowski G, Gao Y, Sineshchekov OA, Wang W, Spudich JL, Luecke H.

Acta Crystallogr D Biol Crystallogr. 2013 Oct;69(Pt 10):1965-80. doi: 10.1107/S0907444913017575. Epub 2013 Sep 20.

PMID: 24100316

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Mechanism divergence in microbial rhodopsins.

Spudich JL, Sineshchekov OA, Govorunova EG.

Biochim Biophys Acta. 2013 Jul 3. doi:pii: S0005-2728(13)00103-5. 10.1016/j.bbabio.2013.06.006.

PMCID:  PMC3844102

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