Publication: Modulation of function, structure and clustering of K+ channels by lipids: lessons learnt from KcsA
Authors
Renart Pérez, María Lourdes ; Guidici Besseghini, Ana Marcela ; Díaz García, Clara ; Molina Gallego, María Luisa ; Morales, Andrés ; González Ros, José Manuel ; Poveda Larrosa, José Antonio
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Publisher
MDPI
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DOI
https://doi.org/10.3390/ijms21072554
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info:eu-repo/semantics/article
Description
©2020 by the authors. 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 International Journal of Molecular Sciences. To access the final edited and published work see https://doi.org/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.
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Citation
Int. J. Mol. Sci. 2020, 21, 2554
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