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Papers In Press, published online ahead of print March 28, 2002
Cellular and Molecular Biology, Toronto Western Research Institute, Toronto, Ontario M5T2S8
Corresponding Author: schlicht{at}uhnres.utoronto.ca
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. Using co-immunoprecipitation assays, we determined that full-length Kv4.2 and PSD-95 interact when co-expressed in a mammalian cell line, tsA201. 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 in a physiologically relevant interaction.
J. Biol. Chem, 10.1074/jbc.M109412200
Submitted on September 28, 2001
Revised on March 28, 2002
Accepted on March 28, 2002
Cell-surface targeting and clustering interactions between heterologously expressed PSD-95 and the Shal voltage-gated potassium channel, Kv4.2
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