Literature DB >> 28834729

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

Boris Y Rubinstein1, Alex Mogilner2.   

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.
Copyright © 2017 Biophysical Society. Published by Elsevier Inc. All rights reserved.

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Year:  2017        PMID: 28834729      PMCID: PMC5567592          DOI: 10.1016/j.bpj.2017.07.003

Source DB:  PubMed          Journal:  Biophys J        ISSN: 0006-3495            Impact factor:   4.033


  2 in total

1.  Protein friction and filament bending facilitate contraction of disordered actomyosin networks.

Authors:  Alexander K Y Tam; Alex Mogilner; Dietmar B Oelz
Journal:  Biophys J       Date:  2021-08-12       Impact factor: 3.699

2.  Feedback inhibition of actin on Rho mediates content release from large secretory vesicles.

Authors:  Dagan Segal; Assaf Zaritsky; Eyal D Schejter; Ben-Zion Shilo
Journal:  J Cell Biol       Date:  2018-03-01       Impact factor: 10.539

  2 in total

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