Modulation of Function, Structure and Clustering of K+ Channels by Lipids: Lessons Learnt from KcsA

Please use this identifier to cite or link to this item:
Información del item - Informació de l'item - Item information
Title: Modulation of Function, Structure and Clustering of K+ Channels by Lipids: Lessons Learnt from KcsA
Authors: Renart, M. Lourdes | Giudici, A. Marcela | Díaz-García, Clara | Molina, M. Luisa | Morales, Andrés | González-Ros, José M. | Poveda, José A.
Research Group/s: Fisiología de Membranas
Center, Department or Service: Universidad de Alicante. Departamento de Fisiología, Genética y Microbiología
Keywords: Lipid–protein interactions | C-type inactivation | Membrane protein folding | Ion channel clustering | Ion binding | KcsA modulation
Knowledge Area: Fisiología
Issue Date: 7-Apr-2020
Publisher: MDPI
Citation: 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
Abstract: 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.
Sponsor: 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).
ISSN: 1661-6596 (Print) | 1422-0067 (Online)
DOI: 10.3390/ijms21072554
Language: eng
Type: info:eu-repo/semantics/article
Rights: © 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 (
Peer Review: si
Publisher version:
Appears in Collections:INV - Fisiología de Membranas - Artículos de Revistas

Files in This Item:
Files in This Item:
File Description SizeFormat 
ThumbnailRenart_etal_2020_IntJMolSci.pdf2,34 MBAdobe PDFOpen Preview

Items in RUA are protected by copyright, with all rights reserved, unless otherwise indicated.