Modulation of Function, Structure and Clustering of K+ Channels by Lipids: Lessons Learnt from KcsA
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http://hdl.handle.net/10045/105387
Títol: | Modulation of Function, Structure and Clustering of K+ Channels by Lipids: Lessons Learnt from KcsA |
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Autors: | Renart, M. Lourdes | Giudici, A. Marcela | Díaz-García, Clara | Molina, M. Luisa | Morales, Andrés | González-Ros, José M. | Poveda, José A. |
Grups d'investigació o GITE: | Fisiología de Membranas |
Centre, Departament o Servei: | Universidad de Alicante. Departamento de Fisiología, Genética y Microbiología |
Paraules clau: | Lipid–protein interactions | C-type inactivation | Membrane protein folding | Ion channel clustering | Ion binding | KcsA modulation |
Àrees de coneixement: | Fisiología |
Data de publicació: | 7-d’abril-2020 |
Editor: | MDPI |
Citació bibliogràfica: | Renart ML, Giudici AM, Díaz-García C, Molina ML, Morales A, González-Ros JM, Poveda JA. Modulation of Function, Structure and Clustering of K+ Channels by Lipids: Lessons Learnt from KcsA. International Journal of Molecular Sciences. 2020; 21(7):2554. doi:10.3390/ijms21072554 |
Resum: | KcsA, a prokaryote tetrameric potassium channel, was the first ion channel ever to be structurally solved at high resolution. This, along with the ease of its expression and purification, made KcsA an experimental system of choice to study structure–function relationships in ion channels. In fact, much of our current understanding on how the different channel families operate arises from earlier KcsA information. Being an integral membrane protein, KcsA is also an excellent model to study how lipid–protein and protein–protein interactions within membranes, modulate its activity and structure. In regard to the later, a variety of equilibrium and non-equilibrium methods have been used in a truly multidisciplinary effort to study the effects of lipids on the KcsA channel. Remarkably, both experimental and “in silico” data point to the relevance of specific lipid binding to two key arginine residues. These residues are at non-annular lipid binding sites on the protein and act as a common element to trigger many of the lipid effects on this channel. Thus, processes as different as the inactivation of channel currents or the assembly of clusters from individual KcsA channels, depend upon such lipid binding. |
Patrocinadors: | This work was partly supported by the grant PGC2018-093505-B-I00 from the Spanish “Ministerio de Ciencia, Innovación y Universidades”/FEDER, UE. CD-G acknowledges support from Medical Biochemistry and Biophysics Doctoral Programme (M2B-PhD) and FCT Portugal (SFRH/PD/BD/135154/2017). |
URI: | http://hdl.handle.net/10045/105387 |
ISSN: | 1661-6596 (Print) | 1422-0067 (Online) |
DOI: | 10.3390/ijms21072554 |
Idioma: | eng |
Tipus: | info:eu-repo/semantics/article |
Drets: | © 2020 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/). |
Revisió científica: | si |
Versió de l'editor: | https://doi.org/10.3390/ijms21072554 |
Apareix a la col·lecció: | INV - Fisiología de Membranas - Artículos de Revistas |
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Renart_etal_2020_IntJMolSci.pdf | 2,34 MB | Adobe PDF | Obrir Vista prèvia | |
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