抄録
Actomyosin contractility is a major force-generating mechanism that drives rearrangement of actomyosin networks; it is fundamental to cellular functions, such as cellular reshaping and movements. Thus, to clarify the mechanochemical foundation of the emergence of cellular functions, understanding the relationship between actomyosin contractility and rearrangement of actomyosin networks is crucial. For this purpose, in this study, we present a new particulate-base model for simulating the motions of actin, non-muscle myosin II, and α-actinin. We simulated the dynamic rearrangement of actomyosin networks. Our simulation results indicate that an increase in the density fraction of myosin induces a higher-order structural transition of actomyosin filaments from networks to bundles, in addition to developing the force generated by actomyosin filaments in the network. On the basis of our results, we describe the mechanical and biochemical roles of a-actinin in sustaining the network and a positive feedback loop observed in the formation of actomyosin bundles.
