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Published online 18 November 2002. doi:10.1083/jcb.200206024
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© The Rockefeller University Press, 0021-9525/2002/11/663 $5.00
The Journal of Cell Biology, Volume 159, Number 4, 663-672

Article

 Clustering of neuronal potassium channels is independent of their interaction with PSD-95

Matthew N. Rasband1, Eunice W. Park1, Dongkai Zhen1, Margaret I. Arbuckle2, Sebastian Poliak3, Elior Peles3, Seth G.N. Grant2 and James S. Trimmer1

1 Department of Biochemistry and Cell Biology, State University of New York at Stony Brook, Stony Brook, NY 11794
2 Center for Genome Research and Center for Neuroscience, University of Edinburgh, Edinburgh EH9 3JQ, UK
3 The Weizmann Institute of Science, Rehovot, Israel 76100

Address correspondence to James S. Trimmer, Dept. of Biochemistry and Cell Biology, 044 Life Sciences Building, SUNY at Stony Brook, Stony Brook, NY 11794-5215. Tel.: (631) 632-9171. Fax (631) 632-9714. E-mail: james.trimmer{at}sunysb.edu

Voltage-dependent potassium channels regulate membrane excitability and cell–cell communication in the mammalian nervous system, and are found highly localized at distinct neuronal subcellular sites. Kv1 (mammalian Shaker family) potassium channels and the neurexin Caspr2, both of which contain COOH-terminal PDZ domain binding peptide motifs, are found colocalized at high density at juxtaparanodes flanking nodes of Ranvier of myelinated axons. The PDZ domain–containing protein PSD-95, which clusters Kv1 potassium channels in heterologous cells, has been proposed to play a major role in potassium channel clustering in mammalian neurons. Here, we show that PSD-95 colocalizes precisely with Kv1 potassium channels and Caspr2 at juxtaparanodes, and that a macromolecular complex of Kv1 channels and PSD-95 can be immunopurified from mammalian brain and spinal cord. Surprisingly, we find that the high density clustering of Kv1 channels and Caspr2 at juxtaparanodes is normal in a mutant mouse lacking juxtaparanodal PSD-95, and that the indirect interaction between Kv1 channels and Caspr2 is maintained in these mutant mice. These data suggest that the primary function of PSD-95 at juxtaparanodes lies outside of its accepted role in mediating the high density clustering of Kv1 potassium channels at these sites.

Key Words: juxtaparanode; myelin; ion channel; MAGUK; node of Ranvier


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