Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.
Subscribe

Logo for

Science 335 (6067): 416-417

Copyright © 2012 by the American Association for the Advancement of Science

The Inner Workings of a Dynamic Duo

Hanne Poulsen, and Poul Nissen

More than 60 years ago, Hodgkin and Huxley showed that neurons maintain their negative resting membrane potential by leaking potassium ions (1). In most cells, the Na+- and K+-dependent adenosine triphosphatase (Na+, K+-ATPase) builds up high concentrations of extracellular sodium and intracellular potassium, and because the membrane is more permeable to potassium, there is a net flow of positive ions out of the cell. The channels responsible for the permeability were much later identified to be the twoépore domain potassium (K2P) channels (2). On pages 432 and 436 of this issue, Miller and Long (3) and Brohawn et al. (4) report the structures of the human K2P channels TWIK-1 and TRAAK.

Centre for Membrane Pumps in Cells and Disease-Pumpkin, Danish National Research Foundation, and Department of Molecular Biology and Genetics, Aarhus University, Gustav Wieds Vej 10C, DK-8000 Aarhus C, Denmark.

E-mail: hp{at}mb.au.dk, pn{at}mb.au.dk

To Advertise     Find Products

Science Signaling. ISSN 1937-9145 (online), 1945-0877 (print). Pre-2008: Science's STKE. ISSN 1525-8882