DC Field | Value | Language |
---|---|---|
dc.contributor.author | Kim, Eunjoon | ko |
dc.contributor.author | Niethammer, M | ko |
dc.contributor.author | Rothshild, A | ko |
dc.contributor.author | Jan, YN | ko |
dc.contributor.author | Sheng, M | ko |
dc.date.accessioned | 2013-03-03T06:17:03Z | - |
dc.date.available | 2013-03-03T06:17:03Z | - |
dc.date.created | 2012-02-06 | - |
dc.date.created | 2012-02-06 | - |
dc.date.issued | 1995-11 | - |
dc.identifier.citation | NATURE, v.378, no.6552, pp.85 - 88 | - |
dc.identifier.issn | 0028-0836 | - |
dc.identifier.uri | http://hdl.handle.net/10203/77591 | - |
dc.description.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 cytoplasmic tails of the K+ channel subunits to two PDZ (also known as GLGF or DHR) domains in the PSD-95 protein(2). 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 syntrophin(4)), suggest that PDZ-domain-containing polypeptides may be widely involved in the organization of proteins at sites of membrane specialization. | - |
dc.language | English | - |
dc.publisher | MACMILLAN MAGAZINES LTD | - |
dc.subject | TUMOR-SUPPRESSOR PROTEIN | - |
dc.subject | SEPTATE JUNCTIONS | - |
dc.subject | POTASSIUM CHANNEL | - |
dc.subject | NMDA RECEPTOR | - |
dc.subject | NEURONS | - |
dc.subject | DIVERSITY | - |
dc.subject | HOMOLOG | - |
dc.subject | BRAIN | - |
dc.subject | GENE | - |
dc.title | Clustering of Shaker-type K+ channels by interaction with a family of membrane-associated guanylate kinases | - |
dc.type | Article | - |
dc.identifier.wosid | A1995TC46900056 | - |
dc.identifier.scopusid | 2-s2.0-0028882810 | - |
dc.type.rims | ART | - |
dc.citation.volume | 378 | - |
dc.citation.issue | 6552 | - |
dc.citation.beginningpage | 85 | - |
dc.citation.endingpage | 88 | - |
dc.citation.publicationname | NATURE | - |
dc.identifier.doi | 10.1038/378085a0 | - |
dc.contributor.localauthor | Kim, Eunjoon | - |
dc.contributor.nonIdAuthor | Niethammer, M | - |
dc.contributor.nonIdAuthor | Rothshild, A | - |
dc.contributor.nonIdAuthor | Jan, YN | - |
dc.contributor.nonIdAuthor | Sheng, M | - |
dc.type.journalArticle | Article | - |
dc.subject.keywordPlus | TUMOR-SUPPRESSOR PROTEIN | - |
dc.subject.keywordPlus | SEPTATE JUNCTIONS | - |
dc.subject.keywordPlus | POTASSIUM CHANNEL | - |
dc.subject.keywordPlus | NMDA RECEPTOR | - |
dc.subject.keywordPlus | NEURONS | - |
dc.subject.keywordPlus | DIVERSITY | - |
dc.subject.keywordPlus | HOMOLOG | - |
dc.subject.keywordPlus | BRAIN | - |
dc.subject.keywordPlus | GENE | - |
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.