DSpace Repository

The voltage dependence of hEag currents is not determined solely by membrane-spanning domains

Show simple item record

APA

Lörinczi, Eva & Napp, Joanna & Contreras Jurado, Silvia Constanza & Pardo, Luis A. & Stühmer, Walter .The voltage dependence of hEag currents is not determined solely by membrane-spanning domains.

ISO 690

Lörinczi, Eva & Napp, Joanna & Contreras Jurado, Silvia Constanza & Pardo, Luis A. & Stühmer, Walter. The voltage dependence of hEag currents is not determined solely by membrane-spanning domains.

https://hdl.handle.net/20.500.12080/26190
dc.contributor.author Lörinczi, Eva
dc.contributor.author Napp, Joanna
dc.contributor.author Contreras Jurado, Silvia Constanza
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


Files in this item

This item appears in the following Collection(s)

Show simple item record

CC-BY Except where otherwise noted, this item's license is described as CC-BY

Search DSpace


Browse

My Account

Social Media