Assistant Professor of Biochemistry

BS 1995, University of Auckland, New Zealand
PhD 1999, University of Auckland
Postdoctoral 2002, Harvard Medical School

206 616 7565 voice
206 685 1792 fax
tgonen@u.washington.edu

Our laboratory uses molecular electron microscopy to study structures of large protein complexes that function as molecular machines. Our main focus is related to two fundamental questions in cell biology: How do cells interact with each other and with their environment, and how do they obtain the nutrients essential for cell survival? We focus on integral membrane proteins because they play a crucial role in mediating information transfer between cells and between compartments within cells; and they are involved in vital processes such as energy conversion, sensing, fusion, nutrient and solute uptake. More than 20% of the genes in the human genome encode membrane-traversing proteins and so it is critical to study structures of membrane proteins to unravel important biological and physiological processes. Our model system is the eye lens, whose cells are rich in junction-forming membrane proteins and transporters needed for nutrient uptake.

Selected Publications

Zheng H., Olia A.S., Gonen M., Andrews S., Cingolani G. and Gonen T. (2008) A conformational switch in bacteriophage P22 portal protein primes genome injection. Molecular Cell - In Press.

Reichow L.S. and Gonen T. (2008) Non-canonical binding of calmodulin to aquaporin-0: implications for channel regulation. Submitted.

Andrews, S., Reichow, L.S. and Gonen T. (2008) Electron crystallography of aquaporins. IUBMB Life - In Press.

Gonen T., Hite R.K., Cheng Y., Petre B.M., Kistler J. and Walz T. (2007) Polymorphic assemblies and crystalline arrays of lens tetraspanin MP20. Journal of Molecular Biology - In Press.

Gonen T. and Walz T. (2006) The structure of aquaporins. Quarterly Reviews of Biophysics 39, 4: 361-396.

Gonen T., Cheng Y., Sliz P., Hiroaki Y., Fujiyoshi Y., Harrison SC., Walz T (2005) Lipid–protein interactions in double layered two dimensional crystals of AQP0. Nature 438: 633-638. See also News and Views feature and front cover.

Gonen T., Cheng Y., Kistler J. and Walz T. (2004) Aquaporin-0 membrane junctions form upon proteolytic cleavage. Journal of Molecular Biology 342(4):1337-45. See also front cover.

Gonen T., Sliz P., Cheng Y., Kistler J. and Walz T. (2004) Aquaporin-0 membrane junctions reveal the structure of a closed water pore. Nature. 429 (6988):193-7. See also News and Views feature.

Grey AC., Jacobs MD., Gonen T., Kistler J. and Donaldson PJ. (2003) Insertion of MP20 into lens fibre cell plasma membranes correlates with the formation of an extracellular diffusion barrier. Experimental Eye Research. 77(5):567-74.

Gonen T., Grey AC., Jacobs MD., Donaldson PJ. and Kistler J. (2001) MP20, the second most abundant lens membrane protein and member of the tetraspanin superfamily, joins the list of ligands of galectin-3. BioMed Central - Cell Biology 2: 17.

Gonen T., Donaldson PJ. and Kistler J. (2000) Galectin-3 – a new adhesion molecule in the lens. Investigative Ophthalmology and Visual Science 41: 199-203. See also Front Cover.