Microscopic origin of macroscopic contractility in actin-myosin active gel models
Artur Alexandre, Nicola Dietler, Simone Cicolini, Andrew Callan-Jones, Dennis W\"orthm\"uller, Serge Dmitrieff

TL;DR
This paper uses numerical simulations to connect microscopic motor properties with macroscopic contractile behavior in actin-myosin networks, validating active gel models with concrete predictions.
Contribution
It demonstrates that active gel models can accurately describe microscopic actin-myosin interactions and predict contractile stress based on microscopic parameters.
Findings
Contractile stress scales linearly with actin density.
Predictions of stress dependence on motor speed and stall force are accurate.
Active gel models are validated against microscopic simulations.
Abstract
Actin filaments, crosslinkers and myosin molecular motors form contractile networks. For instance, the cell cortex is a thin network below the cell membrane ; contraction of the cell cortex allows cells to round up during cell division. Contractile actin-myosin networks are often represented at large scale by continuous theories such as active gel models. However, experimental perturbations are microscopic while parameters in continuous models are macroscopic, thus making those models hard to falsify experimentally. Here we use numerical simulations, in which we can access both microscopic and macroscopic quantities, to show that active gel models can indeed be applied to describe contractile actin. We predict that contractile stress should scale linearly with actin density, which is confirmed by numerical simulations. Moreover, we can accurately predict how the contractile stress…
Peer Reviews
No public reviews on file for this paper yet. If you reviewed it on a platform where reviews are public (OpenReview, ICLR, NeurIPS, ICML), you can paste yours below so the community can read it here.
Videos
No videos yet. Explain this paper in a talk, walkthrough, or lecture? Add one.
Taxonomy
TopicsMicro and Nano Robotics · Cellular Mechanics and Interactions · Cardiomyopathy and Myosin Studies
