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