Clustering of Shaker-type K+ channels by interaction with a family of membrane-associated guanylate kinases View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1995-11

AUTHORS

Eunjoon Kim, Martin Niethammer, Adam Rothschild, Yuh Nung Jan, Morgan Sheng

ABSTRACT

ANCHORING of ion channels at specific subcellular sites is critical for neuronal signalling, but the mechanisms underlying channel localization and clustering are largely unknown (reviewed in ref. 1). Voltage-gated K+ channels are concentrated in various neuronal domains, including presynaptic terminals, nodes of Ranvier and dendrites, where they regulate local membrane excitability. Here we present functional and biochemical evidence that cell-surface clustering of Shaker-subfamily K+ channels is mediated by the PSD-95 family of membrane-associated putative guanylate kinases, as a result of direct binding of the carboxy-terminal cyto-plasmic tails of the K+ channel subunits to two PDZ (also known as GLGF or DHR) domains in the PSD-95 protein2. The ability of PDZ domains to function as independent modules for protein–protein interaction, and their presence in other junction-associated molecules (such as ZO-1 (ref. 3) and syntrophin4), suggest that PDZ-domain-containing polypeptides may be widely involved in the organization of proteins at sites of membrane specialization. More... »

PAGES

85-88

Journal

TITLE

Nature

ISSUE

6552

VOLUME

378

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  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1038/378085a0

    DOI

    http://dx.doi.org/10.1038/378085a0

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1002590906

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/7477295


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