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Updated: Nov 3, 2025

Examining the Conformational Dynamics of Membrane Proteins in situ with Site-directed Fluorescence Labeling
Published on: May 29, 2011
Fluorescent labeling in size-controlled liposomes reveals membrane curvature-induced structural changes in the KcsA
Misuzu Ueki1, Masayuki Iwamoto1
1Department of Molecular Neuroscience, Faculty of Medical Sciences, University of Fukui, Japan.
Abstract:
Biological structures with highly curved membranes, such as caveolae and transport vesicles, are essential for signal transduction and membrane trafficking. Although membrane proteins in these structures are subjected to physical stress due to the curvature of the lipid bilayers, the effect of this membrane curvature on protein structure and function remains unclear. In this study, we established an experimental procedure to evaluate membrane curvature-induced structural changes in the prototypical potassium channel KcsA. The effect of a large membrane curvature was estimated using fluorescently labeled KcsA by incorporating it into liposomes with a small diameter (< 30 nm). We found that a large membrane curvature significantly affects the activation gate conformation of the KcsA channel.
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