We study the role of multivalent actin-binding proteins in remodeling actomyosin networks , using a numerical model of semiflexible filaments. We find that the valency of actin-binding proteins greatly affects URLanization of actomyosin networks. The rich variety of emergent architectures and morphologies inspired us to develop order parametersbased on network theory, to quantitatively characterize the URLanization in the simulated network. First, actin-binding proteins with a valency greater than two promote filament bundles and large filament clusters to a much greater extent than bivalent multilinkers. Second, active myosin-like motor proteins promote rich phases of actomyosin, as characterized by network theory. Lastly, we find that both high content of multilinkers and active motors are necessary to the reduction of node degree correlation in the network of filaments . Our work provides a framework to describe the dendritic structures of actomyosin networks mediated by ABP with the ability of binding multiple filaments, such as Ca2+/Calmodulin-dependent Kinase II (CaMKII). We expect this work to motivate future directions to embrace network theory as a tool to analyze experimentsas well as to establish a quantitative understanding of the role of dendritic spine growth in synaptic plasticity .
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 URLanizing 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 on the heterogeneous morphologies of actomyosin networks at a global level. We find that ABPs with a valency greater than two promote filament bundles and large filament clusters to a much greater extent than bivalent multilinkers. We also show that active myosin-like 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 .
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We study the
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
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in remodeling actomyosin networks , using a numerical
(ABPs) in URLanizing actin filaments into higher-order complex networks via a computer
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find that the valency of actin-binding proteins greatly affects URLanization
characterize the importance of local connectivity among actin filaments as well as the global features
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The rich variety of emergent architectures and morphologies inspired us to develop order parametersbased on network theory, to quantitatively characterize the URLanization in the simulated network. First, actin-binding proteins
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 on the heterogeneous morphologies of actomyosin networks at a global level. We find that ABPs
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Second,
We also show that
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rich phases of actomyosin, as characterized by network theory. Lastly, we find that both high content of multilinkers and active motors are necessary to the reduction of node degree correlation in the network of filaments
the formation of dendritic branches from a stalk of actin bundles
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provides a framework to describe the dendritic structures of actomyosin networks mediated by ABP with the ability of binding multiple filaments, such as Ca2+/Calmodulin-dependent Kinase II (CaMKII). We expect this work to motivate future directions
motivates future studies
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analyze experimentsas well as to establish
characterize complex morphologies of actomyosin detected by experiments, leading to
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dendritic spine growth in synaptic plasticity
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