Insights from graph theory on the morphologies of actomyosin networks with multilinkers
Insights from graph theory on the morphologies of actomyosin networks with multilinkers
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DOI：
10.1103/physreve.102.062420
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发表时间：
2020-12-23
影响因子：
2.4
通讯作者：
Cheung, Margaret S.
中科院分区：
文献类型：
--
作者：
Eliaz, Yossi;Nedelec, Francois;Cheung, Margaret S.
量化微观细节对丝状网络整体结构发展动态的影响在许多生物学相关的背景下是重要的，但不清楚什么样的序参数可以用来充分描述这个复杂的过程。在本文中，我们研究的作用，多价肌动蛋白结合蛋白（ABPs）重组肌动蛋白丝成高阶复杂网络通过半柔性丝的计算机模型。我们的特点肌动蛋白丝之间的局部连接的重要性，以及肌动球蛋白网络的全球功能。我们首先将网络映射到局部图表示中，然后使用网络理论序参数的原理，联合收割机结合这些表示的属性，以深入了解全球层面肌动球蛋白网络的异质形态。我们发现，ABPs的化合价大于2促进丝束和大的细丝簇在更大程度上比二价多接头。我们还表明，积极的肌球蛋白样马达蛋白促进形成树突状分支从一柄肌动蛋白束。我们的工作激励未来的研究拥抱网络理论作为一种工具，以表征复杂的形态学的肌动球蛋白检测实验，导致定量了解的作用，ABP在操纵肌动蛋白丝的自组装成独特的架构，基础的结构支架的细胞有关其流动性和形状。
Quantifying the influence of microscopic details on the dynamics of development of the overall structure of a filamentous network is important in a number of biologically relevant contexts, but it is not obvious what order parameters can be used to adequately describe this complex process. In this paper we investigated the role of multivalent actin-binding proteins (ABPs) in reorganizing actin filaments into higher-order complex networks via a computer model of semiflexible filaments. We characterize the importance of local connectivity among actin filaments, as well as the global features of actomyosin networks. We first map the networks into local graph representations and then, using principles from network-theory order parameters, combine properties from these representations to gain insight into the heterogeneous morphologies of actomyosin networks at a global level. We find that ABPs with a valency greater than 2 promote filament bundles and large filament clusters to a much greater extent than bivalent multilinkers. We also show that active myosinlike motor proteins promote the formation of dendritic branches from a stalk of actin bundles. Our work motivates future studies to embrace network theory as a tool to characterize complex morphologies of actomyosin detected by experiments, leading to a quantitative understanding of the role of ABPs in manipulating the self-assembly of actin filaments into unique architectures that underlie the structural scaffold of a cell relating to its mobility and shape.