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Artículo
Collapse of conductance Is prevented by a Glutamate residue conserved in voltage-dependent K+ channels
dc.creator | Ortega Sáenz, Patricia | |
dc.creator | Pardal Redondo, Ricardo | |
dc.creator | Castellano Orozco, Antonio Gonzalo | |
dc.creator | López Barneo, José | |
dc.date.accessioned | 2015-01-15T10:46:37Z | |
dc.date.available | 2015-01-15T10:46:37Z | |
dc.date.issued | 2000 | |
dc.identifier.issn | 1540-7748 | es |
dc.identifier.issn | 0022-1295 | es |
dc.identifier.uri | http://hdl.handle.net/11441/17783 | |
dc.description.abstract | Voltage-dependent K 1 channel gating is influenced by the permeating ions. Extracellular K 1 determines the occupation of sites in the channels where the cation interferes with the motion of the gates. When external [K 1] decreases, some K 1 channels open too briefly to allow the conduction of measurable current. Given that extracellular K 1 is normally low, we have studied if negatively charged amino acids in the extracellular loops of Shaker K 1 channels contribute to increase the local [K 1]. Surprisingly, neutralization of the charge of most acidic residues has minor effects on gating. However, a glutamate residue (E418) located at the external end of the membrane spanning segment S5 is absolutely required for keeping channels active at the normal external [K 1]. E418 is conserved in all families of voltage-dependent K 1 channels. Although the channel mutant E418Q has kinetic properties resembling those produced by removal of K 1 from the pore, it seems that E418 is not simply concentrating cations near the channel mouth, but has a direct and critical role in gating. Our data suggest that E418 contributes to stabilize the S4 voltage sensor in the depolarized position, thus permitting maintenance of the channel open conformation. | es |
dc.language.iso | eng | es |
dc.relation.ispartof | The Journal of general physiology, 116 (2), 181-190. | es |
dc.rights | Atribución-NoComercial-SinDerivadas 4.0 España | * |
dc.rights.uri | http://creativecommons.org/licenses/by-nc-nd/4.0/ | * |
dc.subject | K+-channel gating | en |
dc.subject | extracellular K1 | en |
dc.subject | acidic residues | en |
dc.subject | open state stabilization | en |
dc.subject | glutamate mutation | en |
dc.title | Collapse of conductance Is prevented by a Glutamate residue conserved in voltage-dependent K+ channels | en |
dc.type | info:eu-repo/semantics/article | es |
dcterms.identifier | https://ror.org/03yxnpp24 | |
dc.rights.accessRights | info:eu-repo/semantics/openAccess | es |
dc.contributor.affiliation | Universidad de Sevilla. Departamento de Fisiología Médica y Biofísica | es |
dc.journaltitle | The Journal of general physiology | es |
dc.publication.volumen | 116 | es |
dc.publication.issue | 2 | es |
dc.publication.initialPage | 181 | es |
dc.publication.endPage | 190 | es |
dc.identifier.idus | https://idus.us.es/xmlui/handle/11441/17783 |
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