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Assembly kinetics determine the architecture of α-actinin crosslinked F-actin networks

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  • Tobias T. Falzone

    (Biophysics Graduate Program, University of Chicago
    Institute for Biophysical Dynamics, University of Chicago)

  • Martin Lenz

    (University of Chicago)

  • David R. Kovar

    (University of Chicago
    University of Chicago)

  • Margaret L. Gardel

    (Institute for Biophysical Dynamics, University of Chicago
    University of Chicago)

Abstract

The actin cytoskeleton is organized into diverse meshworks and bundles that support many aspects of cell physiology. Understanding the self-assembly of these actin-based structures is essential for developing predictive models of cytoskeletal organization. Here we show that the competing kinetics of bundle formation with the onset of dynamic arrest arising from filament entanglements and crosslinking determine the architecture of reconstituted actin networks formed with α-actinin crosslinks. Crosslink-mediated bundle formation only occurs in dilute solutions of highly mobile actin filaments. As actin polymerization proceeds, filament mobility and bundle formation are arrested concomitantly. By controlling the onset of dynamic arrest, perturbations to actin assembly kinetics dramatically alter the architecture of biochemically identical samples. Thus, the morphology of reconstituted F-actin networks is a kinetically determined structure similar to those formed by physical gels and glasses. These results establish mechanisms controlling the structure and mechanics in diverse semiflexible biopolymer networks.

Suggested Citation

  • Tobias T. Falzone & Martin Lenz & David R. Kovar & Margaret L. Gardel, 2012. "Assembly kinetics determine the architecture of α-actinin crosslinked F-actin networks," Nature Communications, Nature, vol. 3(1), pages 1-9, January.
    • Handle: RePEc:nat:natcom:v:3:y:2012:i:1:d:10.1038_ncomms1862
    DOI: 10.1038/ncomms1862
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