All cells require a membrane to separate them from their neighboring cells or the environment. While this compartmentalization is essential for life and its processes, it also poses problems: Not only do chemicals need to cross the barrier to get in and out of the cell, but communication also needs to take place between the cell and its environment. These transport and communication tasks are being carried out by proteins in the membrane that form transporters, pores, channels and signal transducers.

Research in Dr. Poget’s lab focuses on understanding a few of these membrane proteins and their function on an atomic level of structural detail. We employ nuclear magnetic resonance spectroscopy (NMR) and a range of ancillary biophysical techniques to study these proteins. While the main focus in the lab is on understanding the biological systems under study, significant effort is also devoted to developing the NMR methodology to tackle these questions.

Current projects in the lab focus on the interactions of ion channels with animal peptide toxins that target these channels. Ion channels are membrane proteins that allow the flow of specific ions through the membrane. The voltage-gated potassium and sodium channels are two examples of these channels that are specific for potassium and sodium, respectively, and that together are responsible for generating the action potential that allows nerve signal transmission along nerve cells to occur. Many animals therefore have developed toxins that affect these channels and as a consequence disrupt nerve transmission in their prey. The Poget lab seeks to identify novel toxins from animal venom sources and to investigate their mode of action and the structural details of their interaction with the channels. The goal of this research is to better understand how channel activity can be modulated and to find and characterize new tools for doing so. This knowledge may eventually lead to the development of drugs for conditions that involve ion channels, such as epilepsy, cardiac arrhythmias and pain.


Ph.D in Chemsitry, University of Cambridge, UK (2001)

Diploma in Chemistry, University of Basel, Switzerland (1997)

Scholarship / Publications

Selected publications:

Leffler, A. E., Kuryatov, A., Zebroski, H. A., Powell, S. R., Filipenko, P., Hussein, A. K., Gorson, J., Heizmann, A., Lyskov, S., Tsien, R. W., Poget, S. F., Nicke, A., Lindstrom, J., Rudy, B., Bonneau, R. & Holford, M. Discovery of peptide ligands through docking and virtual screening at nicotinic acetylcholine receptor homology models. Proc. Natl. Acad. Sci. 114, E8100–E8109 (2017).

Rivera-Torres, I. O., Jin, T. B., Cadene, M., Chait, B. T. & Poget, S. F. Discovery and characterisation of a novel toxin from Dendroaspis angusticeps, named Tx7335, that activates the potassium channel KcsA. Sci. Rep. 6, (2016).

Chen, X., Liu, Y., Xu, Q., Zhu, J., Poget, S. F. & Lyons, A. M. High-Precision Dispensing of Nanoliter Biofluids on Glass Pedestal Arrays for Ultrasensitive Biomolecule Detection. ACS Appl. Mater. Interfaces 8, (2016).

McCoy, J., Ren, Z., Stanevich, V., Lee, J., Mitra, S., Levin, E. J., Poget, S., Quick, M., Im, W. & Zhou, M. The Structure of a Sugar Transporter of the Glucose EIIC Superfamily Provides Insight into the Elevator Mechanism of Membrane Transport. Structure (2016).

Kim, K., Mitra, S., Wu, G., Berka, V., Song, J., Yu, Y., Poget, S., Wang, D.-N., Tsai, A.-L. & Zhou, M. Six-Transmembrane Epithelial Antigen of Prostate 1 (STEAP1) Has a Single b Heme and Is Capable of Reducing Metal Ion Complexes and Oxygen. Biochemistry 55, 6673–6684 (2016).

Anand, P., Grigoryan, A., Bhuiyan, M. H., Ueberheide, B., Russell, V., Quinoñez, J., Moy, P., Chait, B. T., Poget, S. F. & Holford, M. Sample Limited Characterization of a Novel Disulfide-Rich Venom Peptide Toxin from Terebrid Marine Snail Terebra variegata. PLoS One 9, e94122 (2014).

Poget, S. F., Harris, R., Cahill, S. M. & Girvin, M. E. 1H, 13C, 15N backbone NMR assignments of the Staphylococcus aureus small multidrug-resistance pump (Smr) in a functionally active conformation. Biomol. NMR Assign. 4, 139–142 (2010).

Poget, S. F., Cahill, S. M. & Girvin, M. E. Isotropic bicelles stabilize the functional form of a small multidrug-resistance pump for NMR structural studies. J. Am. Chem. Soc. 129, 2432–3 (2007).

Poget, S. F. & Girvin, M. E. Solution NMR of membrane proteins in bilayer mimics: small is beautiful, but sometimes bigger is better. Biochim. Biophys. Acta 1768, 3098–106 (2007).

Poget, S. F., Freund, S. M., Howard, M. J. & Bycroft, M. The ligand-binding loops in the tunicate C-type lectin TC14 are rigid. Biochemistry 40, 10966–72 (2001).

Poget, S. F., Legge, G. B., Proctor, M. R., Butler, P. J., Bycroft, M. & Williams, R. L. The structure of a tunicate C-type lectin from Polyandrocarpa misakiensis complexed with D-galactose. J. Mol. Biol. 290, 867–879 (1999).