| pubmed-article:18379771 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:18379771 | lifeskim:mentions | umls-concept:C0439857 | lld:lifeskim |
| pubmed-article:18379771 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:18379771 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
| pubmed-article:18379771 | lifeskim:mentions | umls-concept:C0598352 | lld:lifeskim |
| pubmed-article:18379771 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
| pubmed-article:18379771 | lifeskim:mentions | umls-concept:C0521116 | lld:lifeskim |
| pubmed-article:18379771 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
| pubmed-article:18379771 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:18379771 | pubmed:dateCreated | 2009-2-17 | lld:pubmed |
| pubmed-article:18379771 | pubmed:abstractText | The ether-à-go-go potassium channels hEag1 and hEag2 are highly homologous. Even though both possess identical voltage-sensing domain S4, the channels act differently in response to voltage. Therefore we asked whether transmembrane domains other than the voltage sensor could contribute to the voltage-dependent behaviour of these potassium channels. For this chimaeras were created, in which each single transmembrane domain of hEag1 was replaced by the corresponding segment of hEag2. The voltage-dependent properties of the chimaeras were analysed after expression in Xenopus laevis oocytes using the two-electrode voltage-clamp method. By this we found, that only the mutations in transmembrane domains S5 and S6 are able to change the voltage sensitivity of hEag1 by shifting the half-activation potential (V(50)) to values intermediate between the two wild types. Moreover, the presence of Mg2+ has strong effects on the voltage sensitivity of hEag2 shifting V(50) by more than 50 mV to more positive values. Interestingly, despite the identical binding site Mg2+ showed only little effects on hEag1 or the chimaeras. Altogether, our data suggest that not only transmembrane spanning regions, but also non-membrane spanning regions are responsible for differences in the behaviour of the hEag1 and hEag2 potassium channels. | lld:pubmed |
| pubmed-article:18379771 | pubmed:language | eng | lld:pubmed |
| pubmed-article:18379771 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18379771 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:18379771 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18379771 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18379771 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18379771 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18379771 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:18379771 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:18379771 | pubmed:issn | 1432-1017 | lld:pubmed |
| pubmed-article:18379771 | pubmed:author | pubmed-author:StühmerWalter... | lld:pubmed |
| pubmed-article:18379771 | pubmed:author | pubmed-author:PardoLuis ALA | lld:pubmed |
| pubmed-article:18379771 | pubmed:author | pubmed-author:Contreras-Jur... | lld:pubmed |
| pubmed-article:18379771 | pubmed:author | pubmed-author:NappJoannaJ | lld:pubmed |
| pubmed-article:18379771 | pubmed:author | pubmed-author:LörincziEvaE | lld:pubmed |
| pubmed-article:18379771 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:18379771 | pubmed:volume | 38 | lld:pubmed |
| pubmed-article:18379771 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:18379771 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:18379771 | pubmed:pagination | 279-84 | lld:pubmed |
| pubmed-article:18379771 | pubmed:meshHeading | pubmed-meshheading:18379771... | lld:pubmed |
| pubmed-article:18379771 | pubmed:meshHeading | pubmed-meshheading:18379771... | lld:pubmed |
| pubmed-article:18379771 | pubmed:meshHeading | pubmed-meshheading:18379771... | lld:pubmed |
| pubmed-article:18379771 | pubmed:meshHeading | pubmed-meshheading:18379771... | lld:pubmed |
| pubmed-article:18379771 | pubmed:meshHeading | pubmed-meshheading:18379771... | lld:pubmed |
| pubmed-article:18379771 | pubmed:meshHeading | pubmed-meshheading:18379771... | lld:pubmed |
| pubmed-article:18379771 | pubmed:meshHeading | pubmed-meshheading:18379771... | lld:pubmed |
| pubmed-article:18379771 | pubmed:meshHeading | pubmed-meshheading:18379771... | lld:pubmed |
| pubmed-article:18379771 | pubmed:meshHeading | pubmed-meshheading:18379771... | lld:pubmed |
| pubmed-article:18379771 | pubmed:meshHeading | pubmed-meshheading:18379771... | lld:pubmed |
| pubmed-article:18379771 | pubmed:meshHeading | pubmed-meshheading:18379771... | lld:pubmed |
| pubmed-article:18379771 | pubmed:year | 2009 | lld:pubmed |
| pubmed-article:18379771 | pubmed:articleTitle | The voltage dependence of hEag currents is not determined solely by membrane-spanning domains. | lld:pubmed |
| pubmed-article:18379771 | pubmed:affiliation | Max-Planck Institute of Experimental Medicine, Hermann-Rein Str. 3, 37075 Göttingen, Germany. | lld:pubmed |
| pubmed-article:18379771 | pubmed:publicationType | Journal Article | lld:pubmed |
