| pubmed-article:16914520 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:16914520 | lifeskim:mentions | umls-concept:C0597357 | lld:lifeskim |
| pubmed-article:16914520 | lifeskim:mentions | umls-concept:C0090388 | lld:lifeskim |
| pubmed-article:16914520 | lifeskim:mentions | umls-concept:C1416572 | lld:lifeskim |
| pubmed-article:16914520 | lifeskim:mentions | umls-concept:C1426343 | lld:lifeskim |
| pubmed-article:16914520 | lifeskim:mentions | umls-concept:C0004083 | lld:lifeskim |
| pubmed-article:16914520 | lifeskim:mentions | umls-concept:C1153410 | lld:lifeskim |
| pubmed-article:16914520 | pubmed:issue | 11 | lld:pubmed |
| pubmed-article:16914520 | pubmed:dateCreated | 2006-10-31 | lld:pubmed |
| pubmed-article:16914520 | pubmed:abstractText | We identify a new mechanism for the beta(1)-adrenergic receptor (beta(1)AR)-mediated regulation of human ether-a-go-go-related gene (HERG) potassium channel (Kv11.1). We find that the previously reported modulatory interaction between Kv11.1 channels and 14-3-3epsilon proteins is competed by wild type beta(1)AR by means of a novel interaction between this receptor and 14-3-3epsilon. The association between beta(1)AR and 14-3-3epsilon is increased by agonist stimulation in both transfected cells and heart tissue and requires cAMP-dependent protein kinase (PKA) activity. The beta(1)AR/14-3-3epsilon association is direct, since it can be recapitulated using purified 14-3-3epsilon and beta(1)AR fusion proteins and is abolished in cells expressing beta(1)AR phosphorylation-deficient mutants. Biochemical and electrophysiological studies of the effects of isoproterenol on Kv11.1 currents recorded using the whole-cell patch clamp demonstrated that beta(1)AR phosphorylation-deficient mutants do not recruit 14-3-3epsilon away from Kv11.1 and display a markedly altered agonist-mediated modulation of Kv11.1 currents compared with wild-type beta(1)AR, increasing instead of inhibiting current amplitudes. Interestingly, such differential modulation is not observed in the presence of 14-3-3 inhibitors. Our results suggest that the dynamic association of 14-3-3 proteins to both beta(1)AR and Kv11.1 channels is involved in the adrenergic modulation of this critical regulator of cardiac repolarization and refractoriness. | lld:pubmed |
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| pubmed-article:16914520 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:16914520 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:16914520 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:16914520 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:16914520 | pubmed:issn | 1059-1524 | lld:pubmed |
| pubmed-article:16914520 | pubmed:author | pubmed-author:DelpónEvaE | lld:pubmed |
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| pubmed-article:16914520 | pubmed:author | pubmed-author:VaqueroMiguel... | lld:pubmed |
| pubmed-article:16914520 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:16914520 | pubmed:volume | 17 | lld:pubmed |
| pubmed-article:16914520 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16914520 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:16914520 | pubmed:pagination | 4666-74 | lld:pubmed |
| pubmed-article:16914520 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:16914520 | pubmed:year | 2006 | lld:pubmed |
| pubmed-article:16914520 | pubmed:articleTitle | Association of 14-3-3 proteins to beta1-adrenergic receptors modulates Kv11.1 K+ channel activity in recombinant systems. | lld:pubmed |
| pubmed-article:16914520 | pubmed:affiliation | Departamento de Biología Molecular and Centro de Biología Molecular "Severo Ochoa," Universidad Autónoma de Madrid, 28049 Madrid, Spain. | lld:pubmed |
| pubmed-article:16914520 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:16914520 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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