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Assembly Kinetics Determine the Architecture of α-actinin Crosslinked F-actin Networks
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Details:
  • Pubmed ID:
    22643888
  • Pubmed Central ID:
    PMC3563296
  • Description:
    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.

  • Document Type:
  • Collection(s):
  • Funding:
    DP10D00354/DP/NCCDPHP CDC HHS/United States
    R01 GM079265/GM/NIGMS NIH HHS/United States
    R01GM079265/GM/NIGMS NIH HHS/United States
    T32 EB009412/EB/NIBIB NIH HHS/United States
    T32 GM007183/GM/NIGMS NIH HHS/United States
    Howard Hughes Medical Institute/United States
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