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

1
Instituto de Investigación, Desarrollo e Innovación en Biotecnología Sanitaria de Elche (IDiBE), and Instituto de Biología Molecular y Celular (IBMC), Universidad Miguel Hernández, Elche, E-03202 Alicante, Spain
2
iBB-Institute for Bioengineering and Bioscience, Instituto Superior Técnico, Universidade de Lisboa, 1049-001 Lisboa, Portugal
3
Departamento de Fisiología, Genética y Microbiología, Universidad de Alicante, E-03080 Alicante, Spain
*
Authors to whom correspondence should be addressed.
Int. J. Mol. Sci. 2020, 21(7), 2554; https://doi.org/10.3390/ijms21072554
Received: 5 March 2020 / Revised: 2 April 2020 / Accepted: 5 April 2020 / Published: 7 April 2020
(This article belongs to the Special Issue Lipid-Protein and Protein-Protein Interactions in Membranes)
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. View Full-Text
Keywords: lipid–protein interactions; C-type inactivation; membrane protein folding; ion channel clustering; ion binding; KcsA modulation lipid–protein interactions; C-type inactivation; membrane protein folding; ion channel clustering; ion binding; KcsA modulation
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MDPI and ACS Style

Renart, M.L.; Giudici, A.M.; Díaz-García, C.; Molina, M.L.; Morales, A.; González-Ros, J.M.; Poveda, J.A. Modulation of Function, Structure and Clustering of K+ Channels by Lipids: Lessons Learnt from KcsA. Int. J. Mol. Sci. 2020, 21, 2554. https://doi.org/10.3390/ijms21072554

AMA Style

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. https://doi.org/10.3390/ijms21072554

Chicago/Turabian Style

Renart, María L.; Giudici, Ana M.; Díaz-García, Clara; Molina, María L.; Morales, Andrés; González-Ros, José M.; Poveda, José A. 2020. "Modulation of Function, Structure and Clustering of K+ Channels by Lipids: Lessons Learnt from KcsA" Int. J. Mol. Sci. 21, no. 7: 2554. https://doi.org/10.3390/ijms21072554

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