PMID: 8938729Jan 1, 1996Paper

Differential K+ channel clustering activity of PSD-95 and SAP97, two related membrane-associated putative guanylate kinases

Neuropharmacology
E Kim, M Sheng

Abstract

The molecular mechanisms underlying the clustering and localization of K+ channels in specific microdomains on the neuronal surface are largely unknown. The Shaker subclass of voltage-gated K+ channel alpha-subunits interact through their cytoplasmic C-terminus with a family of membrane-associated putative guanylate kinases, including PSD-95 and SAP97. We show here that heterologous coexpression of either sap97 or PSD-95 with various Shaker-type subunits results in the coclustering of these proteins with the K+ channels. Mutation of the C-terminal sequence (-ETDV) of the Shaker subunit Kv1.4 abolishes its binding to, and prevents its clustering with, SAP97 and PSD-95. Whereas PSD-95 induces plaque-like clusters of K+ channels at the cell surface; however, SAP97 coexpression results in the formation of large round intracellular aggregates into which both SAP97 and the K+ channel proteins are colocalized. The efficiency of surface clustering by PSD-95 varies with different Shaker subunits: striking Kv1.4 clustering occurs in > 60% of cotransfected cells, whereas Kv1.1 and Kv1.2 form convincing clusters with PSD-95 only in approximately 10% of cells.

References

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Citations

Apr 5, 2013·Pflügers Archiv : European journal of physiology·Orsolya SzilágyiPéter Hajdu
Oct 12, 2007·Journal of Computational Neuroscience·Anna Y Kuznetsova, Richard C Deth
Aug 12, 2003·Cell Calcium·Mark Arundine, Michael Tymianski
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Jun 6, 1998·Proceedings of the National Academy of Sciences of the United States of America·J ReinhardtA Schwab
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Feb 5, 2002·Annual Review of Physiology·Carol Deutsch
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Nov 24, 2004·Molecular and Cellular Neurosciences·Henry H JerngManuel Covarrubias

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