| pubmed-article:18620005 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:18620005 | lifeskim:mentions | umls-concept:C0020792 | lld:lifeskim |
| pubmed-article:18620005 | lifeskim:mentions | umls-concept:C1332794 | lld:lifeskim |
| pubmed-article:18620005 | lifeskim:mentions | umls-concept:C0205245 | lld:lifeskim |
| pubmed-article:18620005 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
| pubmed-article:18620005 | lifeskim:mentions | umls-concept:C1416562 | lld:lifeskim |
| pubmed-article:18620005 | lifeskim:mentions | umls-concept:C0439799 | lld:lifeskim |
| pubmed-article:18620005 | pubmed:issue | 10 | lld:pubmed |
| pubmed-article:18620005 | pubmed:dateCreated | 2008-9-9 | lld:pubmed |
| pubmed-article:18620005 | pubmed:abstractText | Voltage-gated K(+) (Kv) channels are key determinants of cardiac and neuronal excitability. A substantial body of evidence has accumulated in support of a role for Src family tyrosine kinases in the regulation of Kv channels. In this study, we examined the possibility that c-Src tyrosine kinase participates in the modulation of the transient voltage-dependent K(+) channel Kv4.3. Supporting a mechanistic link between Kv4.3 and c-Src, confocal microscopy analysis of HEK293 cells stably transfected with Kv4.3 showed high degree of co-localization of the two proteins at the plasma membrane. Our results further demonstrate an association between Kv4.3 and c-Src by co-immunoprecipitation and GST pull-down assays, this interaction being mediated by the SH2 and SH3 domains of c-Src. Furthermore, we show that Kv4.3 is tyrosine phosphorylated under basal conditions. The functional relevance of the observed interaction between Kv4.3 and c-Src was established in patch-clamp experiments, where application of the Src inhibitor PP2 caused a decrease in Kv4.3 peak current amplitude, but not the inactive structural analogue PP3. Conversely, intracellular application of recombinant c-Src kinase or the protein tyrosine phosphatase inhibitor bpV(phen) increased Kv4.3 peak current amplitude. In conclusion, our findings provide evidence that c-Src-induced Kv4.3 channel activation involves their association in a macromolecular complex and suggest a role for c-Src-Kv4.3 pathway in regulating cardiac and neuronal excitability. | lld:pubmed |
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| pubmed-article:18620005 | pubmed:language | eng | lld:pubmed |
| pubmed-article:18620005 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18620005 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:18620005 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:18620005 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:18620005 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:18620005 | pubmed:issn | 0006-3002 | lld:pubmed |
| pubmed-article:18620005 | pubmed:author | pubmed-author:ToroLigiaL | lld:pubmed |
| pubmed-article:18620005 | pubmed:author | pubmed-author:StefaniEnrico... | lld:pubmed |
| pubmed-article:18620005 | pubmed:author | pubmed-author:GomesPedroP | lld:pubmed |
| pubmed-article:18620005 | pubmed:author | pubmed-author:AliouaAbderra... | lld:pubmed |
| pubmed-article:18620005 | pubmed:author | pubmed-author:SaitoTomoakiT | lld:pubmed |
| pubmed-article:18620005 | pubmed:author | pubmed-author:EghbaliMansou... | lld:pubmed |
| pubmed-article:18620005 | pubmed:author | pubmed-author:Del... | lld:pubmed |
| pubmed-article:18620005 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:18620005 | pubmed:volume | 1783 | lld:pubmed |
| pubmed-article:18620005 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:18620005 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:18620005 | pubmed:pagination | 1884-92 | lld:pubmed |
| pubmed-article:18620005 | pubmed:dateRevised | 2011-9-26 | lld:pubmed |
| pubmed-article:18620005 | pubmed:meshHeading | pubmed-meshheading:18620005... | lld:pubmed |
| pubmed-article:18620005 | pubmed:meshHeading | pubmed-meshheading:18620005... | lld:pubmed |
| pubmed-article:18620005 | pubmed:meshHeading | pubmed-meshheading:18620005... | lld:pubmed |
| pubmed-article:18620005 | pubmed:meshHeading | pubmed-meshheading:18620005... | lld:pubmed |
| pubmed-article:18620005 | pubmed:meshHeading | pubmed-meshheading:18620005... | lld:pubmed |
| pubmed-article:18620005 | pubmed:meshHeading | pubmed-meshheading:18620005... | lld:pubmed |
| pubmed-article:18620005 | pubmed:meshHeading | pubmed-meshheading:18620005... | lld:pubmed |
| pubmed-article:18620005 | pubmed:meshHeading | pubmed-meshheading:18620005... | lld:pubmed |
| pubmed-article:18620005 | pubmed:meshHeading | pubmed-meshheading:18620005... | lld:pubmed |
| pubmed-article:18620005 | pubmed:meshHeading | pubmed-meshheading:18620005... | lld:pubmed |
| pubmed-article:18620005 | pubmed:meshHeading | pubmed-meshheading:18620005... | lld:pubmed |
| pubmed-article:18620005 | pubmed:meshHeading | pubmed-meshheading:18620005... | lld:pubmed |
| pubmed-article:18620005 | pubmed:year | 2008 | lld:pubmed |
| pubmed-article:18620005 | pubmed:articleTitle | Identification of a functional interaction between Kv4.3 channels and c-Src tyrosine kinase. | lld:pubmed |
| pubmed-article:18620005 | pubmed:affiliation | Department of Anesthesiology, Division of Molecular Medicine, David Geffen School of Medicine at University of California Los Angeles, Los Angeles, CA 90095-1778, USA. pgomes@med.up.pt | lld:pubmed |
| pubmed-article:18620005 | pubmed:publicationType | Journal Article | lld:pubmed |
