OHSU
Eric Gouaux

Eric Gouaux, Ph.D.

Senior Scientist, Vollum Institute
Investigator, Howard Hughes Medical Institute

Email: gouauxe@ohsu.edu
Phone: 503-494-5535
Lab Phone: 503-494-6721
Office: Vollum Institute, Rm 1423A

Gouaux Lab Page

PubMed Listing

 

Background

Eric Gouaux completed his B.A. and Ph.D. degrees in Chemistry at Harvard University in 1984 and 1989, respectively. He remained at Harvard for a year as a postdoctoral fellow, and then continued his postdoctoral studies at the Massachusetts Institute of Technology. In 1993, he was appointed assistant professor at the University of Chicago Department of Biochemistry and Molecular Biology.

In 1996, he joined the Department of Biochemistry and Molecular Biology at Columbia University as an assistant professor. In 2000, he was appointed Investigator with the Howard Hughes Medical Institute and associate professor with Columbia, reaching full professor the following year. He came to Oregon Health & Science University in 2005 as a Senior Scientist at the Vollum Institute and continuing his position with Howard Hughes. He joined the graduate faculty in the Department of Biochemistry and Molecular Biology in 2006.

 

Summary of Current Research

The work in the Gouaux Lab is concentrated on developing molecular mechanisms for the function of receptors and transporters at chemical synapses. At chemical synapses, neurotransmitters released from one neuron diffuse throughout a small space—the synaptic cleft—to receptors on adjacent neurons. At many synapses, the neurotransmitter binds to a receptor that is a ligand-gated ion channel, and this binding event leads to the opening of a transmembrane pore, which in turn results in depolarization of the nerve cell and generation of an electrical signal. Neurotransmitter transporters surrounding the synapse clear the transmitters from the cleft by coupling the thermodynamically unfavorable uptake to the favorable co-transport of one or more sodium ions.

Glutamate, glycine and the biogenic amines are neurotransmitters of particular significance and currently we are focusing our efforts on eukaryotic glutamate receptors and on bacterial homologs of the transporters for glutamate, glycine and the biogenic amines. While our primary tool is x-ray crystallography, we also utilize electrophysiology as well as other biophysical and biochemical methods.

 

Selected Publications

Chen L, Dürr KL, Gouaux E. (2014) X-ray structures of AMPA receptor-cone snail toxin complexes illuminate activation mechanism. Science 345:1021-1026.

Althoff T, Hibbs RE, Banerjee S, Gouaux E. (2014) X-ray structures of GluCl in apo states reveal a gating mechanism of Cys-loop receptors. Nature 512:333-337.

Dürr KL*, Chen L*, Stein RA, De Zorzi R, Folea IM, Walz T, Mchaourab HS, Gouaux E. (2014) Structure and dynamics of AMPA receptor GluA2 in resting, pre-open, and desensitized states. Cell 158:778-792. (*co-first author)

Lee CH, Lü W, Michel JC, Goehring A, Du J, Song X, Gouaux E. (2014) NMDA receptor structures reveal subunit arrangement and pore architecture. Nature 511:191-197.

Baconguis I, Bohlen CJ, Goehring A, Julius D and Gouaux E. (2014) X-ray structure of acid-sensing ion channel 1–snake toxin complex reveals open state of a Na+-selective channel. Cell 156:717-729.

Wang H, Goehring A, Wang KH, Penmatsa A, Ressler R and Gouaux E. (2013) Structural basis for action by diverse antidepressants on biogenic amine transporters. Nature 503:141-145.

Penmatsa A, Wang KH, and Gouaux E. (2013) X-ray structure of dopamine transporter elucidates antidepressant mechanism. Nature 503:85-90.

Baconguis I and Gouaux E. (2012) Structural plasticity and dynamic selectivity of acid-sensing ion channel–spider toxin complexes. Nature 489:400-405.

Hattori M and Gouaux E. (2012) Molecular mechanism of ATP binding and ion channel activation in P2X receptors. Nature 485:207-212.

Krishnamurthy H and Gouaux E. (2012) X-ray structures of LeuT in substrate-free outward-open and apo inward-open states. Nature 481:469-474.

Hibbs RE and Gouaux E. (2011) Principles of activation and permeation in an anion-selective Cys-loop receptor. Nature 474:54-60.

Back to Faculty List