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https://doi.org/10.1074/jbc.M115.669598
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Campo DC | Valor | Lengua/Idioma |
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dc.contributor.author | Molina Gallego, María Luisa | - |
dc.contributor.author | Giudici Besseghini, Ana Marcela | - |
dc.contributor.author | Poveda Larrosa, José Antonio | - |
dc.contributor.author | Fernández Ballester, Gregorio | - |
dc.contributor.author | Montoya Díaz, Estefanía | - |
dc.contributor.author | Renart Pérez, María Lourdes | - |
dc.contributor.author | Fernández Carvajal, Asia María | - |
dc.contributor.author | Encinar Hidalgo, José Antonio | - |
dc.contributor.author | Riquelme Pino, Gloria | - |
dc.contributor.author | Morales Calderón, Andrés | - |
dc.contributor.author | González Ros, José Manuel | - |
dc.contributor.other | Facultades, Departamentos, Servicios y Escuelas::Departamentos de la UMU::Bioquímica y Biología Molecular "B" e Inmunología | - |
dc.date.accessioned | 2024-07-03T11:42:59Z | - |
dc.date.available | 2024-07-03T11:42:59Z | - |
dc.date.issued | 2015-09-02 | - |
dc.identifier.citation | Journal of Biological Chemistry, 2015. Vol. 290, issue 42, pp.25745-25755. | es |
dc.identifier.issn | Print: 0021-9258 | - |
dc.identifier.issn | Electronic: 1083-351X | - |
dc.identifier.uri | http://hdl.handle.net/10201/142833 | - |
dc.description | © 2015 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.M115.669598 | - |
dc.description.abstract | There is increasing evidence to support the notion that membrane proteins, instead of being isolated components floating in a fluid lipid environment, can be assembled into supramolecular complexes that take part in a variety of cooperative cellular functions. The interplay between lipid-protein and protein-protein interactions is expected to be a determinant factor in the assembly and dynamics of such membrane complexes. Here we report on a role of anionic phospholipids in determining the extent of clustering of KcsA, a model potassium channel. Assembly/disassembly of channel clusters occurs, at least partly, as a consequence of competing lipid-protein and protein-protein interactions at nonannular lipid binding sites on the channel surface and brings about profound changes in the gating properties of the channel. Our results suggest that these latter effects of anionic lipids are mediated via the Trp67–Glu71–Asp80 inactivation triad within the channel structure and its bearing on the selectivity filter. | es |
dc.format | application/pdf | es |
dc.format.extent | 11 | es |
dc.language | eng | es |
dc.publisher | American Society for Biochemistry and Molecular Biology | - |
dc.relation | This work was supported in part by grants from the Spanish Ministerio de Ciencia e Innovación Grants BFU2011-25920 and BFU2012-31359 and Consolider-Ingenio 2010 Grant CSD2-2008-00005 | es |
dc.rights | info:eu-repo/semantics/openAccess | es |
dc.rights | Atribución 4.0 Internacional | * |
dc.rights.uri | http://creativecommons.org/licenses/by/4.0/ | * |
dc.subject | Gating | es |
dc.subject | Lipid-protein interaction | es |
dc.subject | Molecular modeling | es |
dc.subject | Potassium channel | es |
dc.subject | Protein-protein interaction | es |
dc.subject | Coupled channel gating | es |
dc.subject | Ion channel inactivation | es |
dc.title | Competing lipid-protein and protein-protein interactions determine clustering and gating patterns in KcsA | es |
dc.type | info:eu-repo/semantics/article | es |
dc.relation.publisherversion | https://www.sciencedirect.com/science/article/pii/S0021925820445879?via%3Dihub | - |
dc.identifier.doi | https://doi.org/10.1074/jbc.M115.669598 | - |
Aparece en las colecciones: | Artículos: Bioquímica y Biología Molecular "B" e Inmunología |
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PIIS0021925820445879.pdf | 1,68 MB | Adobe PDF | ![]() Visualizar/Abrir |
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