Friction patterns guide actin network contraction

肌球蛋白 收缩(语法) 肌动蛋白 材料科学 微图形化 生物物理学 机械 纳米技术 化学 物理 生物 生物化学 内分泌学
作者
Alexandra Colin,Magali Orhant‐Prioux,Christophe Guérin,Mariya Savinov,Wenxiang Cao,Benoît Vianay,Ilaria Scarfone,Aurélien Roux,Enrique M. De La Cruz,Alex Mogilner,Manuel Théry,Laurent Blanchoin
出处
期刊:Proceedings of the National Academy of Sciences of the United States of America [Proceedings of the National Academy of Sciences]
卷期号:120 (39) 被引量:6
标识
DOI:10.1073/pnas.2300416120
摘要

The shape of cells is the outcome of the balance of inner forces produced by the actomyosin network and the resistive forces produced by cell adhesion to their environment. The specific contributions of contractile, anchoring and friction forces to network deformation rate and orientation are difficult to disentangle in living cells where they influence each other. Here, we reconstituted contractile actomyosin networks in vitro to study specifically the role of the friction forces between the network and its anchoring substrate. To modulate the magnitude and spatial distribution of friction forces, we used glass or lipids surface micropatterning to control the initial shape of the network. We adapted the concentration of Nucleating Promoting Factor on each surface to induce the assembly of actin networks of similar densities and compare the deformation of the network toward the centroid of the pattern shape upon myosin-induced contraction. We found that actin network deformation was faster and more coordinated on lipid bilayers than on glass, showing the resistance of friction to network contraction. To further study the role of the spatial distribution of these friction forces, we designed heterogeneous micropatterns made of glass and lipids. The deformation upon contraction was no longer symmetric but biased toward the region of higher friction. Furthermore, we showed that the pattern of friction could robustly drive network contraction and dominate the contribution of asymmetric distributions of myosins. Therefore, we demonstrate that during contraction, both the active and resistive forces are essential to direct the actin network deformation.

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