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Myosin Clusters of Finite Size Develop Contractile Stress in 1D Random Actin Arrays.
Rubinstein, Boris Y; Mogilner, Alex.
Affiliation
  • Rubinstein BY; Stowers Institute, Kansas City, Missouri, New York University, New York, New York.
  • Mogilner A; Courant Institute of Mathematical Sciences, New York University, New York, New York; Department of Biology, New York University, New York, New York. Electronic address: mogilner@cims.nyu.edu.
Biophys J ; 113(4): 937-947, 2017 Aug 22.
Article in En | MEDLINE | ID: mdl-28834729
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.
Subject(s)

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Stress, Mechanical / Actins / Myosins / Models, Biological / Muscle Contraction Type of study: Clinical_trials Language: En Journal: Biophys J Year: 2017 Document type: Article

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Stress, Mechanical / Actins / Myosins / Models, Biological / Muscle Contraction Type of study: Clinical_trials Language: En Journal: Biophys J Year: 2017 Document type: Article
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