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Título: | Clustering and coupled gating modulate the activity in KcsA, a potassium channel model |
Fecha de publicación: | 7-jul-2006 |
Editorial: | Elsevier |
Cita bibliográfica: | Journal of Biological Chemistry, 2006, Vol. 281, Issue 27, pp.18837-18848 |
ISSN: | Print: 0021-9258 Electronic: 1083-351X |
Resumen: | Different patterns of channel activity have been detected by patch clamping excised membrane patches from reconstituted giant liposomes containing purified KcsA, a potassium channel from prokaryotes. The more frequent pattern has a characteristic low channel opening probability and exhibits many other features reported for KcsA reconstituted into planar lipid bilayers, including a moderate voltage dependence, blockade by Na+, and a strict dependence on acidic pH for channel opening. The predominant gating event in this low channel opening probability pattern corresponds to the positive coupling of two KcsA channels. However, other activity patterns have been detected as well, which are characterized by a high channel opening probability (HOP patterns), positive coupling of mostly five concerted channels, and profound changes in other KcsA features, including a different voltage dependence, channel opening at neutral pH, and lack of Na+ blockade. The above functional diversity occurs correlatively to the heterogeneous supramolecular assembly of KcsA into clusters. Clustering of KcsA depends on protein concentration and occurs both in detergent solution and more markedly in reconstituted membranes, including giant liposomes, where some of the clusters are large enough (up to micrometer size) to be observed by confocal microscopy. As in the allosteric conformational spread responses observed in receptor clustering (Bray, D. and Duke, T. (2004) Annu. Rev. Biophys. Biomol. Struct. 33, 53-73) our tenet is that physical clustering of KcsA channels is behind the observed multiple coupled gating and diverse functional responses. |
Autor/es principal/es: | Molina Gallego, María Luisa Barrera Olivares, Francisco Nicolás Fernández Carvajal, Asia María Poveda Larrosa, José Antonio Renart Pérez, María Lourdes Encinar Hidalgo, José Antonio Riquelme Pino, Gloria González Ros, José Manuel |
Facultad/Departamentos/Servicios: | Facultades, Departamentos, Servicios y Escuelas::Departamentos de la UMU::Bioquímica y Biología Molecular "B" e Inmunología |
Versión del editor: | https://www.sciencedirect.com/science/article/pii/S0021925820576473#ceack10 |
URI: | http://hdl.handle.net/10201/142854 |
DOI: | https://doi.org/10.1074/jbc.M600342200 |
Tipo de documento: | info:eu-repo/semantics/article |
Número páginas / Extensión: | 12 |
Derechos: | info:eu-repo/semantics/openAccess Atribución 4.0 Internacional |
Descripción: | © 2006 by The American Society for Biochemistry and Molecular Biology, Inc. This manuscript version is made available under the CC-BY 4.0 license http://creativecommons.org/licenses/by/4.0/ This document is the Published version of a Published Work that appeared in final form in Journal of Biological Chemistry. To access the final edited and published work see https://doi.org/10.1074/jbc.M600342200 |
Aparece en las colecciones: | Artículos: Bioquímica y Biología Molecular "B" e Inmunología |
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