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• W2000242989 abstract "In a quantitative manner, we investigated the mechanism of switching ezrin from the dormant to the active, F-actin binding state by recognition of PIP2. For this purpose, we established a novel in vitro model mimicking ezrin-mediated membrane−cytoskeleton attachment and compared the F-actin binding capability of ezrin that either had been coupled via a His tag to a lipid bilayer displaying Ni-NTA or had been bound to supported membranes containing PIP2. Epifluorescence and colloidal probe microscopy (CPM) were employed to demonstrate ezrin’s conformational switch into an active conformation capable of binding F-actin. Epifluorescence images revealed attachment of fluorescently labeled F-actin solely to PIP2-bound ezrin. For the first time, colloidal spheres equipped with an artificial cytoskeleton composed of firmly attached F-actin filaments were used to measure quantitatively the maximal adhesion forces and the work of adhesion of the ezrin−F-actin interface. We found that the work of adhesion between PIP2-bound ezrin and F-actin is substantially larger than that measured between F-actin and ezrin bound to the membrane via the His tag. Collectively, these data indicate that activation of ezrin can occur as a consequence of PIP2 binding and does not require additional cofactors." @default.
• W2000242989 created "2016-06-24" @default.
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• W2000242989 date "2008-02-27" @default.
• W2000242989 modified "2023-09-23" @default.
• W2000242989 title "Actin Binding of Ezrin Is Activated by Specific Recognition of PIP₂-Functionalized Lipid Bilayers" @default.
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• W2000242989 doi "https://doi.org/10.1021/bi702542s" @default.
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