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.


Sci. STKE, 4 September 2001
Vol. 2001, Issue 98, p. pe1
[DOI: 10.1126/stke.2001.98.pe1]


Unzipping Ion Channels

Stacey Nee MacFarlane and Irwin B. Levitan

The authors are at the Department of Neuroscience, University of Pennsylvania School of Medicine, Philadelphia, PA 19104, USA. E-mail: levitani{at}

Abstract: The functions of ion channels can be regulated by their phosphorylation state. Protein kinases and protein phosphatases tightly control the activity of channels, thereby regulating the flow of ions across cell membranes. Channel proteins and kinases or phosphatases can associate directly or through intermediate adaptor proteins. An interaction domain termed the leucine zipper (LZ), once thought to be unique to some families of transcription factors, has been identified in channel proteins and their cognate binding proteins. MacFarlane and Levitan discuss what roles LZ-containing proteins might have in controlling channel function.

Citation: S. N. MacFarlane, I. B. Levitan, Unzipping Ion Channels. Sci. STKE 2001, pe1 (2001).

Read the Full Text

To Advertise     Find Products

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