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Probing membrane deformation energy by KcsA potassium channel gating under varied membrane thickness and tension.
- Source :
-
FEBS letters [FEBS Lett] 2024 Aug; Vol. 598 (16), pp. 1955-1966. Date of Electronic Publication: 2024 Jun 16. - Publication Year :
- 2024
-
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.<br /> (© 2024 The Author(s). FEBS Letters published by John Wiley & Sons Ltd on behalf of Federation of European Biochemical Societies.)
- Subjects :
- Lipid Bilayers metabolism
Lipid Bilayers chemistry
Cell Membrane metabolism
Cell Membrane chemistry
Hydrophobic and Hydrophilic Interactions
Protein Conformation
Potassium Channels metabolism
Potassium Channels chemistry
Ion Channel Gating
Bacterial Proteins metabolism
Bacterial Proteins chemistry
Bacterial Proteins genetics
Subjects
Details
- Language :
- English
- ISSN :
- 1873-3468
- Volume :
- 598
- Issue :
- 16
- Database :
- MEDLINE
- Journal :
- FEBS letters
- Publication Type :
- Academic Journal
- Accession number :
- 38880762
- Full Text :
- https://doi.org/10.1002/1873-3468.14956