Myosin Clusters of Finite Size Develop Contractile Stress in 1D Random Actin Arrays

Boris Y. Rubinstein, Alex Mogilner

Research output: Contribution to journalArticle

3 Scopus citations

Abstract

Myosin-powered force generation and contraction in nonmuscle cells underlies many cell biological processes and is based on contractility of random actin arrays. This contractility must rely on a microscopic asymmetry, the precise mechanism of which is not completely clear. A number of models of mechanical and structural asymmetries in actomyosin contraction have been posited. Here, we examine a contraction mechanism based on a finite size of myosin clusters and anisotropy of force generation by myosin heads at the ends of the myosin clusters. We use agent-based numerical simulations to demonstrate that if average lengths of actin filaments and myosin clusters are similar, then the proposed microscopic asymmetry leads to effective contraction of random 1D actomyosin arrays. We discuss the model's implication for mechanics of contractile rings and stress fibers.

Original languageEnglish (US)
Pages (from-to)937-947
Number of pages11
JournalBiophysical Journal
Volume113
Issue number4
DOIs
StatePublished - Aug 22 2017
Externally publishedYes

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ASJC Scopus subject areas

  • Biophysics

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