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Previous Article | Next Article
The Journal of Neuroscience, December 1, 2000, 20(23):8736-8744
Localization and Enhanced Current Density of the Kv4.2 Potassium Channel by Interaction with the Actin-Binding Protein Filamin
Kevin Petrecca, David M. Miller, and Alvin Shrier Department of Physiology, McGill University, Montréal, Québec, Canada H3G 1Y6
Kv4.2 potassium channels play a critical role in postsynaptic excitability. Immunocytochemical studies reveal a somatodendritic Kv4.2 expression pattern, with the channels concentrated mainly at dendritic spines. The molecular mechanism that underlies the localization of Kv4.2 to this subcellular region is unknown. We used the yeast two-hybrid system to identify the Kv4.2-associated proteins that are involved in channel localization. Here we demonstrate a direct interaction between Kv4.2 and the actin-binding protein, filamin. We show that Kv4.2 and filamin can be coimmunoprecipitated both in vitro and in brain and that Kv4.2 and filamin share an overlapping expression pattern in the cerebellum and cultured hippocampal neurons. To examine the functional consequences of this interaction, we expressed Kv4.2 in filamin+ and filamin
cells and performed immunocytochemical and electrophysiological analyses. Our results indicate that Kv4.2 colocalizes with filamin at filopodial roots in filamin+ cells but shows a nonspecific expression pattern in filamin
Key words: Kv4.2; potassium channels; filamin; postsynaptic density; subcellular localization; actin-binding protein
Copyright © 2000 Society for Neuroscience 0270-6474/00/20238736-09$05.00/0
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