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Originally published In Press as doi:10.1074/jbc.M109412200 on March 28, 2002

J. Biol. Chem., Vol. 277, Issue 23, 20423-20430, June 7, 2002
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Cell Surface Targeting and Clustering Interactions between Heterologously Expressed PSD-95 and the Shal Voltage-gated Potassium Channel, Kv4.2*

Wei WongDagger §, Evan W. NewellDagger ||**, Denis G. M. JugloffDagger §, Owen T. JonesDagger §Dagger Dagger , and Lyanne C. SchlichterDagger §||§§

From the Dagger  Division of Cellular and Molecular Biology, Toronto Western Research Institute, University Health Network, Toronto, Ontario M5T 2S8, and the § Department of Pharmacology and the || Department of Physiology, University of Toronto, Toronto, Ontario M5S 1A8, Canada

Kv4.2 is a voltage-gated potassium channel that is critical in controlling the excitability of myocytes and neurons. Processes that influence trafficking and surface distribution patterns of Kv4.2 will affect its ability to contribute to cellular functions. The scaffolding/clustering protein PSD-95 regulates trafficking and distribution of several receptors and Shaker family Kv channels. We therefore investigated whether the C-terminal valine-serine-alanine-leucine (VSAL) of Kv4.2 is a novel binding motif for PSD-95. By using co-immunoprecipitation assays, we determined that full-length Kv4.2 and PSD-95 interact when co-expressed in mammalian cell lines. Mutation analysis in this heterologous expression system showed that the VSAL motif of Kv4.2 is necessary for PSD-95 binding. PSD-95 increased the surface expression of Kv4.2 protein and caused it to cluster, as shown by deconvolution microscopy and biotinylation assays. Deleting the C-terminal VSAL motif of Kv4.2 eliminated these effects, as did substituting a palmitoylation-deficient PSD-95 mutant. In addition to these effects of PSD-95 on Kv4.2 distribution, the channel itself promoted redistribution of PSD-95 to the cell surface in the heterologous expression system. This work represents the first evidence that a member of the Shal subfamily of Kv channels can bind to PSD-95, with functional consequences.

* This work was supported in part by Canadian Institutes of Health Grant MT13657, Heart and Stroke Foundation of Canada Grant T-3726 (to L. C. S.), and a Natural Sciences and Engineering Research Council grant (to O. T. J.). Parts of this work were previously published as abstracts (61, 62).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Supported by an Ontario Graduate Scholarship and a University of Toronto Connaught Scholarship.

** Supported by a National Science Foundation Graduate Student Fellowship.

Dagger Dagger Current address: Division of Neuroscience, School of Biological Sciences, University of Manchester, Manchester M13 9PT, UK.

§§ To whom correspondence should be addressed: MC9-415, Toronto Western Hospital, 399 Bathurst St., Toronto, Ontario M5T 2S8, Canada. Tel.: 416-603-5800, ext. 2052; Fax: 416-603-5745; E-mail: schlicht@uhnres.utoronto.ca.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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