# Mechanosensitive Self-Assembly of Myosin II Minifilaments

Source: [Mechanosensitive Self-Assembly of Myosin II Minifilaments](<https://www.sota2.com/research/paper/68fa3b7f1e209131ce8d3264>)

Collection index: [llms.txt](<https://www.sota2.com/research/llms.txt>)

Data updated: 2025-10-25T00:37:52.438Z

Authors: Justin Grewe, Ulrich S. Schwarz

Published: 2019-10-18T14:58:17.000Z

## Abstract

Self-assembly and force generation are two central processes in biological systems that usually are considered in separation. However, the signals that activate non-muscle myosin II molecular motors simultaneously lead to self-assembly into myosin II minifilaments as well as progression of the motor heads through the crossbridge cycle. Here we investigate theoretically the possible effects of coupling these two processes. Our assembly model, which builds upon a consensus architecture of the minifilament, predicts a critical aggregation concentration at which the assembly kinetics slows down dramatically. The combined model predicts that increasing actin filament concentration and force both lead to a decrease in the critical aggregation concentration. We suggest that due to these effects, myosin II minifilaments in a filamentous context might be in a critical state that reacts faster to varying conditions than in solution. We finally compare our model to experiments by simulating fluorescence recovery after photobleaching.

## Recorded benchmark results

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## Original sources and implementation

[Original paper](<https://arxiv.org/abs/1910.08453>)

[PDF](<https://arxiv.org/pdf/1910.08453.pdf>)