Our goal is to understand the structure and function of cotransporter
proteins. These are responsible for the active transport of molecules and ions into cells.
Specifically, we study sodium glucose cotransporters (SGLTs). We use a combination of
biophysical, biochemical, molecular, and structural,
techniques to unravel how these molecular machines convert the energy stored in sodium
gradients to drive the uphill transport of solutes. We also study genetic diseases of
SGLTs where our goal is to determine how mutations cause transport defects.
The cotransporters are expressed either in Xenopus laevis oocytes and mammalian cells
for biophysical and biochemical studies, and Escherichia coli for the isolation of
protein for structural studies. We are now imaging SGLT function in human subjects.
Abramson J, Wright EM. (2009) Structure and function of Na(+)-symporters with inverted repeats. Curr Opin Struct Biol. Aug;19(4):425-32. Epub 2009 Jul 22
Faham S, Watanabe A, Besserer GM, Cascio D, Specht A, Hirayama BA, Wright EM., Abramson J. (2008) The crystal structure of a sodium galactose transporter reveals mechanistic insights into Na+/sugar symport. Science. Aug 8;321(5890):810-4. Epub 2008 Jul 3.
Loo DD, Hirayama BA, Sala-Rabanal M, Wright EM.. (2008) How drugs interact with transporters: SGLT1 as a model. J Membr Biol. May;223(2):87-106. Epub 2008 Jul 1
Link to my PubMed bibliography