Peter Snyder, M.D.

Professor of Medicine and Molecular Physiology & Biophysics

University of Iowa College of Medicine, 1989

Research Interests

The epithelial sodium channel (ENaC) forms the pathway for sodium absorption in the kidney and other epithelia. ENaC plays a key role in the control of blood volume and blood pressure. This is emphasized by two genetic disorders. Mutations in ENaC that increase channel activity cause Liddle's syndrome, an autosomal dominant form of hypertension. Conversely, loss-of-function mutations cause pseudohypoaldosteronism type I, a disorder of salt wasting and hypotension. Research in my lab is focused on the structure and function of the epithelial sodium channel to understand its role in hypertension and other disorders of sodium homeostasis. My laboratory has identified the molecular mechanisms by which mutations in ENaC cause hypertension. Current research in my laboratory focuses on; a) regulation of ENaC and dysfunction of the channel in disease, b) determination of the structure of the channel complex and ion conduction pathway, and c) structure and function of related DEG/ENaC ion channels that play a role in mechanosensation and nociception. A number of approaches are used to accomplish these goals, including techniques of molecular biology, electrophysiology, cell biology, and protein biochemistry.

Selected Publications

1. Knight, K.K, Olson, D.R., Zhou, R., Snyder, P.M: Liddle's syndrome mutations increase Na+ transport through dual effects on epithelial Na+ channel surface expression and proteolytic cleavage. Proc. Natl. Acad. Sci. U.S.A. 2006 Feb 21; 103 (8):2805-2808. Epub 2006 Feb 13.

2. Snyder, P.M., Steines, J.C., and Olson, D.R.: Relative Contribution of Nedd4 and Nedd4-2 to ENaC Regulation in Epithelia Determined by RNA Interference. J. Biol. Chem. 279:5042-5046, 2004.

3. Snyder, P.M., Olson, D.R., Kabra, R., Zhou, R., and Steines, J.C.: cAMP and Serum and Glucocorticoid-induced Kinase (SGK) Regulate the Epithelial Na+ Channel through Convergent Phosphorylation of Nedd4-2. J. Biol. Chem. 279:45753-45758, 2004.

4. Zhou, R. and Snyder, P.M.: Nedd4-2 Phosphorylation Induces Serum and Glucocorticoid-regulated Kinase (SGK) Ubiquitination and Degradation. J. Biol. Chem., 280:4518-4523, 2005.