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

Sci. STKE, 3 July 2007
Vol. 2007, Issue 393, p. pe37
[DOI: 10.1126/stke.3932007pe37]

PERSPECTIVES

The Surprising Catch of a Voltage-Gated Potassium Channel in a Neuronal SNARE

Durga P. Mohapatra, Helene Vacher, and James S. Trimmer*

Department of Pharmacology, School of Medicine, University of California, Davis, CA 95616, USA.

Abstract: Among ion channels, voltage-gated calcium channels have been considered unique in their ability to mediate signaling events independent of the flow of ions through their pore. A voltage-gated potassium channel termed Kv2.1 has been identified as playing a role remarkably similar to one ion-independent function of calcium channels, facilitating regulated exocytosis through a direct interaction with a t-SNARE [soluble NSF (N-ethylmaleimide–sensitive factor) attachment protein receptor] component of the vesicle release machinery. Kv2.1 overexpression enhances depolarization-induced secretion from the neuroendocrine-like PC12 cell line, and a nonconducting Kv2.1 mutant can accomplish the same feat. Kv2.1 interacts directly with syntaxin 1A, a plasma membrane t-SNARE component of the vesicle docking and fusion apparatus. Deletion of the syntaxin 1A–binding segment from Kv2.1 abolishes its ability to promote vesicle release, supporting a mechanism whereby Kv2.1 presumably transfers voltage-dependent conformational changes induced by membrane depolarization to interacting t-SNAREs to affect exocytosis. Kv2.1, a major mediator of electrical events in central neurons, cardiac and smooth muscle, and pancreatic beta cells, must now also be recognized as a physical mediator of secretion. That Kv2.1 is phosphorylated at numerous sites within the syntaxin 1A binding segment raises the possibility that its role in secretion may be dynamically regulated by diverse signaling events.

*Corresponding author. Department of Pharmacology, School of Medicine, University of California, Davis, CA 95616, USA. Telephone, 530-754-6075; fax, 530-754-6079; e-mail, jtrimmer{at}ucdavis.edu

Citation: D. P. Mohapatra, H. Vacher, J. S. Trimmer, The Surprising Catch of a Voltage-Gated Potassium Channel in a Neuronal SNARE. Sci. STKE 2007, pe37 (2007).

Read the Full Text


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Signal integration at the level of ion channel and exocytotic function in pancreatic {beta}-cells.
P. E. MacDonald (2011)
Am J Physiol Endocrinol Metab 301, E1065-E1069
   Abstract »    Full Text »    PDF »
Non-conducting function of the Kv2.1 channel enables it to recruit vesicles for release in neuroendocrine and nerve cells.
L. Feinshreiber, D. Singer-Lahat, R. Friedrich, U. Matti, A. Sheinin, O. Yizhar, R. Nachman, D. Chikvashvili, J. Rettig, U. Ashery, et al. (2010)
J. Cell Sci. 123, 1940-1947
   Abstract »    Full Text »    PDF »

To Advertise     Find Products


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