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The membrane-actin linker ezrin acts as a sliding anchor

View ORCID ProfileElgin Korkmazhan, Alexander R. Dunn
doi: https://doi.org/10.1101/2021.11.28.470228
Elgin Korkmazhan
1Department of Chemical Engineering, Stanford University; Stanford, CA 94305 USA
2Graduate Program in Biophysics, Stanford University; Stanford, CA 94305 USA
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  • ORCID record for Elgin Korkmazhan
Alexander R. Dunn
1Department of Chemical Engineering, Stanford University; Stanford, CA 94305 USA
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  • For correspondence: alex.dunn@stanford.edu
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ABSTRACT

Protein linkages to filamentous (F)-actin provide the cell membrane with mechanical resiliency and give rise to intricate membrane architectures. However, the actin cytoskeleton is highly dynamic, and undergoes rapid changes in shape during cell motility and other processes. The molecular mechanisms that underlie the mechanically robust yet fluid connection between the membrane and actin cytoskeleton remain poorly understood. Here, we used a single-molecule optical trap assay to examine how the prototypical membrane-actin linker ezrin acts to anchor F-actin to the cell membrane. Remarkably, we find that ezrin forms a complex that slides along F-actin over micron distances while resisting mechanical detachment. The ubiquity of ezrin and analogous proteins suggests that sliding anchors such as ezrin may constitute an important but overlooked element in the construction of the actin cytoskeleton.

Competing Interest Statement

The authors have declared no competing interest.

Copyright 
The copyright holder for this preprint is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under a CC-BY-NC-ND 4.0 International license.
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Posted November 28, 2021.
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The membrane-actin linker ezrin acts as a sliding anchor
Elgin Korkmazhan, Alexander R. Dunn
bioRxiv 2021.11.28.470228; doi: https://doi.org/10.1101/2021.11.28.470228
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The membrane-actin linker ezrin acts as a sliding anchor
Elgin Korkmazhan, Alexander R. Dunn
bioRxiv 2021.11.28.470228; doi: https://doi.org/10.1101/2021.11.28.470228

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