University of Bristol
Ion channels are specialized membrane spanning proteins that open and form ion permeable pores in response to various stimuli, including binding by diffusible ligands. Many of these ion channels are located on the plasma membrane enveloping all cells, and by conducting the movement of ions such as Na+, K+, and Ca2+ can regulate a diversity of intracellular processes, such as neuronal action potential propagation, secretion, muscle contraction, and gene expression. My current research interests are focused on elucidating the structure and function of ion channels that are activated in response to extracellular ligands, such as neurotransmitters. Understanding the molecular basis by which ion channels are activated and consequently select and conduct ions is an important step towards designing new drugs capable of targeting these proteins for therapeutic purposes. Some of these ion channels have been shown to transport relatively large ionic species into cells, and an additional goal of the laboratory is to see whether this property can be exploited in order to facilitate drug delivery into tumor cells.
Publications (last 5 years)
- K.L. Poetz, H.S. Mohammed, G. Liddil, D.S.K. Samways, and D.A. Shipp (2014). A Study of the Degradation Product from Polyanhydrides Synthesized by Thiol-Ene Polymerization. Biomacromolecules. 15, 2573-82
- L. Zhang, H. Xu, Y. Jie, C. Gao, W. Chen, S. Yin, D.S.K. Samways, and Z. Li (2014). Involvement of Residue L214 of P2X4 Receptor in ATP Binding and Channel Gating. J. Biol. Chem. 53, 3012-9
- D.S.K. Samways (2014). Applications for mass spectrometry in the study of ion channel structure and function. Adv Exp Med Biol. 806, 237-61. doi: 10.1007/978-3-319-06068-2_10.
- D.S.K. Samways, Z. Li and T.M. Egan (2014). (Invited review) Principles and properties of ion flow in P2X receptors. Front. Cell. Neurosci. 5;8:6. doi: 10.3389/fncel.2014.00006
- Z. Lin, P. Perez, J-J. Liu, J.H. Shin, K.L. Hyrc, D.S.K Samways, T.M. Egan, M.C. Holley, and J. Bao (2012). Reprogramming of single-cell-derived mesenchymal stem cells into hair cell-like cells. Otol. Neurotol. 33, 1648-55
- D.S.K. Samways, B.S. Khakh, and T.M. Egan (2012). Allosteric modulation of Ca2+ flux in a ligand-gated cation channel (P2X4) by actions on lateral portals. J. Biol. Chem. In press
- D.S.K. Samways, B.S. Khakh, S. Dutertre, and T.M. Egan (2011). Preferential use of unobstructed lateral portals as the access route to the pore of human ATP-gated ion channels (P2X receptors). Proc. Natl. Acad. Sci. 108, 13800-5
- D.S.K. Samways and T.M. Egan (2011). Calcium-dependent decrease in the single-channel conductance of TRPV1. Pflugers Arch. 462, 681-91
- E. Toulme, A. Garcia, D.S.K. Samways, T.M. Egan, M.J. Carson, and B.S. Khakh (2010). P2X4 receptor specificity, functional properties, trafficking and pharmacology of upregulated P2X responses in activated cerebellar microglia. J. Gen. Physiol. 135, 333-53. (PMID: 20231374)
- D.S.K. Samways, A.B. Harkins and T.M. Egan (2009). ASIC1a receptors conduct negligible Ca2+ entry. Cell Calcium. 45, 319-25 (PMID: 19189309)