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Hysteresis of a Tension-Sensitive K(+) Channel Revealed by Time-Lapse Tension Measurements

[Image: see text] Various types of channels vary their function by membrane tension changes upon cellular activities, and lipid bilayer methods allow elucidation of direct interaction between channels and the lipid bilayer. However, the dynamic responsiveness of the channel to the membrane tension r...

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Autores principales: Iwamoto, Masayuki, Oiki, Shigetoshi
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Chemical Society 2021
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8395652/
https://www.ncbi.nlm.nih.gov/pubmed/34467309
http://dx.doi.org/10.1021/jacsau.0c00098
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author Iwamoto, Masayuki
Oiki, Shigetoshi
author_facet Iwamoto, Masayuki
Oiki, Shigetoshi
author_sort Iwamoto, Masayuki
collection PubMed
description [Image: see text] Various types of channels vary their function by membrane tension changes upon cellular activities, and lipid bilayer methods allow elucidation of direct interaction between channels and the lipid bilayer. However, the dynamic responsiveness of the channel to the membrane tension remains elusive. Here, we established a time-lapse tension measurement system. A bilayer is formed by docking two monolayer-lined water bubbles, and tension is evaluated via measuring intrabubble pressure as low as <100 Pa (Young–Laplace principle). The prototypical KcsA potassium channel is tension-sensitive, and single-channel current recordings showed that the activation gate exhibited distinct tension sensitivity upon stretching and relaxing. The mechanism underlying the hysteresis is discussed in the mode shift regime, in which the channel protein bears short “memory” in their conformational changes.
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spelling pubmed-83956522021-08-30 Hysteresis of a Tension-Sensitive K(+) Channel Revealed by Time-Lapse Tension Measurements Iwamoto, Masayuki Oiki, Shigetoshi JACS Au [Image: see text] Various types of channels vary their function by membrane tension changes upon cellular activities, and lipid bilayer methods allow elucidation of direct interaction between channels and the lipid bilayer. However, the dynamic responsiveness of the channel to the membrane tension remains elusive. Here, we established a time-lapse tension measurement system. A bilayer is formed by docking two monolayer-lined water bubbles, and tension is evaluated via measuring intrabubble pressure as low as <100 Pa (Young–Laplace principle). The prototypical KcsA potassium channel is tension-sensitive, and single-channel current recordings showed that the activation gate exhibited distinct tension sensitivity upon stretching and relaxing. The mechanism underlying the hysteresis is discussed in the mode shift regime, in which the channel protein bears short “memory” in their conformational changes. American Chemical Society 2021-03-22 /pmc/articles/PMC8395652/ /pubmed/34467309 http://dx.doi.org/10.1021/jacsau.0c00098 Text en © 2021 The Authors. Published by American Chemical Society https://creativecommons.org/licenses/by-nc-nd/4.0/Permits non-commercial access and re-use, provided that author attribution and integrity are maintained; but does not permit creation of adaptations or other derivative works (https://creativecommons.org/licenses/by-nc-nd/4.0/).
spellingShingle Iwamoto, Masayuki
Oiki, Shigetoshi
Hysteresis of a Tension-Sensitive K(+) Channel Revealed by Time-Lapse Tension Measurements
title Hysteresis of a Tension-Sensitive K(+) Channel Revealed by Time-Lapse Tension Measurements
title_full Hysteresis of a Tension-Sensitive K(+) Channel Revealed by Time-Lapse Tension Measurements
title_fullStr Hysteresis of a Tension-Sensitive K(+) Channel Revealed by Time-Lapse Tension Measurements
title_full_unstemmed Hysteresis of a Tension-Sensitive K(+) Channel Revealed by Time-Lapse Tension Measurements
title_short Hysteresis of a Tension-Sensitive K(+) Channel Revealed by Time-Lapse Tension Measurements
title_sort hysteresis of a tension-sensitive k(+) channel revealed by time-lapse tension measurements
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8395652/
https://www.ncbi.nlm.nih.gov/pubmed/34467309
http://dx.doi.org/10.1021/jacsau.0c00098
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