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Quantitative Biology > Biomolecules

arXiv:1910.08453 (q-bio)
[Submitted on 18 Oct 2019 ]

Title: Mechanosensitive Self-Assembly of Myosin II Minifilaments

Title: 肌球蛋白II微型丝的机械敏感自组装

Authors:Justin Grewe, Ulrich S. Schwarz (Heidelberg University)
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.
Abstract: 自组装和力生成是生物系统中的两个核心过程,通常被分别考虑。 然而,激活非肌性肌球蛋白II分子马达的信号同时导致肌球蛋白II微型丝的自组装以及马达头部通过横桥循环的进展。 在这里,我们从理论上研究了耦合这两个过程的可能影响。 我们的组装模型基于微型丝的共识结构,预测了一个临界聚集浓度,在该浓度下,组装动力学会显著减慢。 组合模型预测,增加肌动蛋白丝浓度和力都会导致临界聚集浓度的降低。 我们认为,由于这些效应,纤维状环境中肌球蛋白II微型丝可能处于一个临界状态,其对变化条件的反应速度比在溶液中更快。 最后,我们通过模拟光漂白后的荧光恢复来将我们的模型与实验进行比较。
Comments: 15 pages, 6 figures, 4 supplemental figures
Subjects: Biomolecules (q-bio.BM) ; Soft Condensed Matter (cond-mat.soft); Biological Physics (physics.bio-ph)
Cite as: arXiv:1910.08453 [q-bio.BM]
  (or arXiv:1910.08453v1 [q-bio.BM] for this version)
  https://doi.org/10.48550/arXiv.1910.08453
arXiv-issued DOI via DataCite
Journal reference: Phys. Rev. E 101, 022402 (2020)
Related DOI: https://doi.org/10.1103/PhysRevE.101.022402
DOI(s) linking to related resources

Submission history

From: Ulrich S. Schwarz [view email]
[v1] Fri, 18 Oct 2019 14:58:17 UTC (3,593 KB)
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