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Probing membrane deformation energy by KcsA potassium channel gating under varied membrane thickness and tension.
Matsuki, Yuka; Takashima, Masako; Ueki, Misuzu; Iwamoto, Masayuki; Oiki, Shigetoshi.
Afiliación
  • Matsuki Y; Department of Anesthesiology and Reanimatology, Faculty of Medical Sciences, University of Fukui, Yoshida-gun, Japan.
  • Takashima M; Life Science Innovation Center, University of Fukui, Yoshida-gun, Japan.
  • Ueki M; Department of Molecular Neuroscience, Faculty of Medical Sciences, University of Fukui, Yoshida-gun, Japan.
  • Iwamoto M; Life Science Innovation Center, University of Fukui, Yoshida-gun, Japan.
  • Oiki S; Department of Molecular Neuroscience, Faculty of Medical Sciences, University of Fukui, Yoshida-gun, Japan.
FEBS Lett ; 598(16): 1955-1966, 2024 Aug.
Article en En | MEDLINE | ID: mdl-38880762
ABSTRACT
This study investigated how membrane thickness and tension modify the gating of KcsA potassium channels when simultaneously varied. The KcsA channel undergoes global conformational changes upon gating expansion of the cross-sectional area and longitudinal shortening upon opening. Thus, membranes impose differential effects on the open and closed conformations, such as hydrophobic mismatches. Here, the single-channel open probability was recorded in the contact bubble bilayer, by which variable thickness membranes under a defined tension were applied. A fully open channel in thin membranes turned to sporadic openings in thick membranes, where the channel responded moderately to tension increase. Quantitative gating analysis prompted the hypothesis that tension augmented the membrane deformation energy when hydrophobic mismatch was enhanced in thick membranes.
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Texto completo: 1 Colección: 01-internacional Banco de datos: MEDLINE Asunto principal: Proteínas Bacterianas / Canales de Potasio / Activación del Canal Iónico Idioma: En Revista: FEBS Lett Año: 2024 Tipo del documento: Article País de afiliación: Japón

Texto completo: 1 Colección: 01-internacional Banco de datos: MEDLINE Asunto principal: Proteínas Bacterianas / Canales de Potasio / Activación del Canal Iónico Idioma: En Revista: FEBS Lett Año: 2024 Tipo del documento: Article País de afiliación: Japón