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dc.contributor.author | Lörinczi, Eva | |
dc.contributor.author | Napp, Joanna | |
dc.contributor.author | Contreras Jurado, Silvia Constanza![]() |
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dc.contributor.author | Pardo, Luis A. | |
dc.contributor.author | Stühmer, Walter | |
dc.date.accessioned | 2021-11-10T17:16:18Z | |
dc.date.available | 2021-11-10T17:16:18Z | |
dc.date.created | 2009 | |
dc.identifier.uri | https://hdl.handle.net/20.500.12080/26190 | |
dc.description.abstract | The ether-a`-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 cre ated, in which each single transmembrane domain of hEag1 was replaced by the corresponding segment of hEag2. The voltage-dependent properties of the chimaeras were ana lysed 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 (V50) to values inter mediate between the two wild types. Moreover, the presence of Mg2+ has strong effects on the voltage sensi tivity of hEag2 shifting V50 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. | es_ES |
dc.format | application/pdf | es_ES |
dc.language | eng | es_ES |
dc.rights | CC-BY | es_ES |
dc.rights.uri | http://creativecommons.org/licenses/by/4.0/deed.es | es_ES |
dc.title | The voltage dependence of hEag currents is not determined solely by membrane-spanning domains | es_ES |
dc.type | info:eu-repo/semantics/article | es_ES |
dc.rights.accessrights | info:eu-repo/semantics/openAccess | es_ES |
dc.identifier.location | N/A | es_ES |