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

Crystal structure of sensory rhodopsin II at 2.4 angstroms: insights into color tuning and transducer interaction.

Luecke H, Schobert B, Lanyi JK, Spudich EN, Spudich JL.

Science. 2001 Aug 24;293(5534):1499-503. Epub 2001 Jul 12.

PMID: 11452084

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Three strategically placed hydrogen-bonding residues convert a proton pump into a sensory receptor.

Sudo Y, Spudich JL.

Proc Natl Acad Sci U S A. 2006 Oct 31;103(44):16129-34. Epub 2006 Oct 18.

PMID: 17050685

 

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A Schiff base connectivity switch in sensory rhodopsin signaling.

Sineshchekov OA, Sasaki J, Phillips BJ, Spudich JL.

Proc Natl Acad Sci U S A. 2008 Oct 21;105(42):16159-64. doi: 10.1073/pnas.0807486105. Epub 2008 Oct 13.

PMID: 18852467

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