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Nat Commun. 2016 Aug 25;7:12615. doi: 10.1038/ncomms12615.

Disordered actomyosin networks are sufficient to produce cooperative and telescopic contractility.

Author information

1
Department of Biomedical Engineering, Yale University, 55 Prospect Street, New Haven, Connecticut 06520, USA.
2
Systems Biology Institute, Yale University, 850 West Campus Drive, West Haven, Connecticut 06516, USA.
3
James Franck Institute, University of Chicago, Chicago, Illinois 60637, USA.
4
School of Mechanical Engineering, 585 Purdue Mall, Purdue University, West Lafayette, Indiana 47907, USA.
5
Weldon School of Biomedical Engineering, 206 S Martin Jischke Drive, Purdue University, West Lafayette, Indiana 47907, USA.

Abstract

While the molecular interactions between individual myosin motors and F-actin are well established, the relationship between F-actin organization and actomyosin forces remains poorly understood. Here we explore the accumulation of myosin-induced stresses within a two-dimensional biomimetic model of the disordered actomyosin cytoskeleton, where myosin activity is controlled spatiotemporally using light. By controlling the geometry and the duration of myosin activation, we show that contraction of disordered actin networks is highly cooperative, telescopic with the activation size, and capable of generating non-uniform patterns of mechanical stress. We quantitatively reproduce these collective biomimetic properties using an isotropic active gel model of the actomyosin cytoskeleton, and explore the physical origins of telescopic contractility in disordered networks using agent-based simulations.

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