Competing Lipid-Protein and Protein-Protein Interactions Determine Clustering and Gating Patterns in the Potassium Channel from Streptomyces lividans (KcsA)

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Título: Competing Lipid-Protein and Protein-Protein Interactions Determine Clustering and Gating Patterns in the Potassium Channel from Streptomyces lividans (KcsA)
Autor/es: Molina, M. Luisa | Giudici, A. Marcela | Poveda, José A. | Fernández-Ballester, Gregorio | Montoya, Estefanía | Renart, M. Lourdes | Fernández, Asia M. | Encinar, José A. | Riquelme, Gloria | Morales, Andrés | González-Ros, José M.
Grupo/s de investigación o GITE: Fisiología de Membranas
Centro, Departamento o Servicio: Universidad de Alicante. Departamento de Fisiología, Genética y Microbiología
Palabras clave: Lipid-protein | Protein-protein interactions | Clustering | Gating | Potassium channel | Streptomyces lividans (KcsA)
Área/s de conocimiento: Fisiología
Fecha de publicación: 16-oct-2015
Editor: American Society for Biochemistry and Molecular Biology
Cita bibliográfica: The Journal of Biological Chemistry. 2015, 290(42): 25745-25755. doi:10.1074/jbc.M115.669598
Resumen: 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.
Patrocinador/es: 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.
URI: http://hdl.handle.net/10045/53254
ISSN: 0021-9258 (Print) | 1083-351X (Online)
DOI: 10.1074/jbc.M115.669598
Idioma: eng
Tipo: info:eu-repo/semantics/article
Derechos: © 2015 by The American Society for Biochemistry and Molecular Biology, Inc.
Revisión científica: si
Versión del editor: http://dx.doi.org/10.1074/jbc.M115.669598
Aparece en las colecciones:INV - Fisiología de Membranas - Artículos de Revistas

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