Thick Filament Length and Isoform Composition Determine Self-Organized Contractile Units in Actomyosin Bundles

Todd Thoresen 1 Martin Lenz 2, 1, 3 Margaret Gardel 1, 3

Biophysical Journal, Biophysical Society, 2013, 104, pp.655-665. <10.1016/j.bpj.2012.12.042>

Diverse myosin II isoforms regulate contractility of actomyosin bundles in disparate physiological processes by variations in both motor mechanochemistry and the extent to which motors are clustered into thick filaments. Although the role of mechanochemistry is well appreciated, the extent to which thick filament length regulates actomyosin contractility is unknown. Here, we study the contractility of minimal actomyosin bundles formed in vitro by mixtures of F-actin and thick filaments of nonmuscle, smooth, and skeletal muscle myosin isoforms with varied length. Diverse myosin II isoforms guide the self-organization of distinct contractile units within in vitro bundles with shortening rates similar to those of in vivo myofibrils and stress fibers. The tendency to form contractile units increases with the thick filament length, resulting in a bundle shortening rate proportional to the length of constituent myosin thick filament. We develop a model that describes our data, providing a framework in which to understand how diverse myosin II isoforms regulate the contractile behaviors of disordered actomyosin bundles found in muscle and nonmuscle cells. These experiments provide insight into physiological processes that use dynamic regulation of thick filament length, such as smooth muscle contraction.

  • 1. The James Franck Institute, Institute Biophysical Dynamics
  • 2. LPTMS – Laboratoire de Physique Théorique et Modèles Statistiques
  • 3. Department of Physics – Department of Physics
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