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Modulation of Voltage-Gating and Hysteresis of Lysenin Channels by Cu(2+) Ions
The intricate voltage regulation presented by lysenin channels reconstituted in artificial lipid membranes leads to a strong hysteresis in conductance, bistability, and memory. Prior investigations on lysenin channels indicate that the hysteresis is modulated by multivalent cations which are also ca...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2023
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10455686/ https://www.ncbi.nlm.nih.gov/pubmed/37629177 http://dx.doi.org/10.3390/ijms241612996 |
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author | Bogard, Andrew Finn, Pangaea W. Smith, Aviana R. Flacau, Ilinca M. Whiting, Rose Fologea, Daniel |
author_facet | Bogard, Andrew Finn, Pangaea W. Smith, Aviana R. Flacau, Ilinca M. Whiting, Rose Fologea, Daniel |
author_sort | Bogard, Andrew |
collection | PubMed |
description | The intricate voltage regulation presented by lysenin channels reconstituted in artificial lipid membranes leads to a strong hysteresis in conductance, bistability, and memory. Prior investigations on lysenin channels indicate that the hysteresis is modulated by multivalent cations which are also capable of eliciting single-step conformational changes and transitions to stable closed or sub-conducting states. However, the influence on voltage regulation of Cu(2+) ions, capable of completely closing the lysenin channels in a two-step process, was not sufficiently addressed. In this respect, we employed electrophysiology approaches to investigate the response of lysenin channels to variable voltage stimuli in the presence of small concentrations of Cu(2+) ions. Our experimental results showed that the hysteretic behavior, recorded in response to variable voltage ramps, is accentuated in the presence of Cu(2+) ions. Using simultaneous AC/DC stimulation, we were able to determine that Cu(2+) prevents the reopening of channels previously closed by depolarizing potentials and the channels remain in the closed state even in the absence of a transmembrane voltage. In addition, we showed that Cu(2+) addition reinstates the voltage gating and hysteretic behavior of lysenin channels reconstituted in neutral lipid membranes in which lysenin channels lose their voltage-regulating properties. In the presence of Cu(2+) ions, lysenin not only regained the voltage gating but also behaved like a long-term molecular memory controlled by electrical potentials. |
format | Online Article Text |
id | pubmed-10455686 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-104556862023-08-26 Modulation of Voltage-Gating and Hysteresis of Lysenin Channels by Cu(2+) Ions Bogard, Andrew Finn, Pangaea W. Smith, Aviana R. Flacau, Ilinca M. Whiting, Rose Fologea, Daniel Int J Mol Sci Article The intricate voltage regulation presented by lysenin channels reconstituted in artificial lipid membranes leads to a strong hysteresis in conductance, bistability, and memory. Prior investigations on lysenin channels indicate that the hysteresis is modulated by multivalent cations which are also capable of eliciting single-step conformational changes and transitions to stable closed or sub-conducting states. However, the influence on voltage regulation of Cu(2+) ions, capable of completely closing the lysenin channels in a two-step process, was not sufficiently addressed. In this respect, we employed electrophysiology approaches to investigate the response of lysenin channels to variable voltage stimuli in the presence of small concentrations of Cu(2+) ions. Our experimental results showed that the hysteretic behavior, recorded in response to variable voltage ramps, is accentuated in the presence of Cu(2+) ions. Using simultaneous AC/DC stimulation, we were able to determine that Cu(2+) prevents the reopening of channels previously closed by depolarizing potentials and the channels remain in the closed state even in the absence of a transmembrane voltage. In addition, we showed that Cu(2+) addition reinstates the voltage gating and hysteretic behavior of lysenin channels reconstituted in neutral lipid membranes in which lysenin channels lose their voltage-regulating properties. In the presence of Cu(2+) ions, lysenin not only regained the voltage gating but also behaved like a long-term molecular memory controlled by electrical potentials. MDPI 2023-08-20 /pmc/articles/PMC10455686/ /pubmed/37629177 http://dx.doi.org/10.3390/ijms241612996 Text en © 2023 by the authors. https://creativecommons.org/licenses/by/4.0/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 (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Bogard, Andrew Finn, Pangaea W. Smith, Aviana R. Flacau, Ilinca M. Whiting, Rose Fologea, Daniel Modulation of Voltage-Gating and Hysteresis of Lysenin Channels by Cu(2+) Ions |
title | Modulation of Voltage-Gating and Hysteresis of Lysenin Channels by Cu(2+) Ions |
title_full | Modulation of Voltage-Gating and Hysteresis of Lysenin Channels by Cu(2+) Ions |
title_fullStr | Modulation of Voltage-Gating and Hysteresis of Lysenin Channels by Cu(2+) Ions |
title_full_unstemmed | Modulation of Voltage-Gating and Hysteresis of Lysenin Channels by Cu(2+) Ions |
title_short | Modulation of Voltage-Gating and Hysteresis of Lysenin Channels by Cu(2+) Ions |
title_sort | modulation of voltage-gating and hysteresis of lysenin channels by cu(2+) ions |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10455686/ https://www.ncbi.nlm.nih.gov/pubmed/37629177 http://dx.doi.org/10.3390/ijms241612996 |
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