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DOI10.1073/pnas.1708625114
Filament rigidity and connectivity tune the deformation modes of active biopolymer networks
Stam S.; Freedman S.L.; Banerjee S.; Weirich K.L.; Dinner A.R.; Gardel M.L.
发表日期2017
ISSN0027-8424
起始页码E10037
结束页码E10045
卷号114期号:47
英文摘要Molecular motors embedded within collections of actin and microtubule filaments underlie the dynamics of cytoskeletal assemblies. Understanding the physics of such motor-filament materials is critical to developing a physical model of the cytoskeleton and designing biomimetic active materials. Here, we demonstrate through experiments and simulations that the rigidity and connectivity of filaments in active biopolymer networks regulates the anisotropy and the length scale of the underlying deformations, yielding materials with variable contractility. We find that semiflexible filaments can be compressed and bent by motor stresses, yielding materials that undergo predominantly biaxial deformations. By contrast, rigid filament bundles slide without bending under motor stress, yielding materials that undergo predominantly uniaxial deformations. Networks dominated by biaxial deformations are robustly contractile over a wide range of connectivities, while networks dominated by uniaxial deformations can be tuned from extensile to contractile through cross-linking. These results identify physical parameters that control the forces generated within motor-filament arrays and provide insight into the self-organization and mechanics of cytoskeletal assemblies. © 2017, National Academy of Sciences. All rights reserved.
英文关键词Actin; Active matter; Agent-based simulation; Mechanics; Myosin
语种英语
scopus关键词actin; biopolymer; molecular motor; actin; actin binding protein; carrier protein; fascin; filamin; myosin; actin filament; Article; biopolymer structure; compression; connectome; controlled study; cross linking; cytoskeleton; force; molecular mechanics; muscle contractility; physical parameters; polymerization; priority journal; protein assembly; rigidity; simulation; stress; actin filament; animal; biological model; biomechanics; chemistry; chicken; computer simulation; Leporidae; metabolism; microtubule; ultrastructure; Actin Cytoskeleton; Actins; Animals; Biomechanical Phenomena; Carrier Proteins; Chickens; Computer Simulation; Cytoskeleton; Filamins; Microfilament Proteins; Microtubules; Models, Biological; Myosins; Rabbits
来源期刊Proceedings of the National Academy of Sciences of the United States of America
文献类型期刊论文
条目标识符http://gcip.llas.ac.cn/handle/2XKMVOVA/160573
作者单位Stam, S., Biophysical Sciences Graduate Program, University of Chicago, Chicago, IL 60637, United States, Institute for Biophysical Dynamics, University of Chicago, Chicago, IL 60637, United States; Freedman, S.L., James Franck Institute, University of Chicago, Chicago, IL 60637, United States, Department of Physics, University of Chicago, Chicago, IL 60637, United States; Banerjee, S., James Franck Institute, University of Chicago, Chicago, IL 60637, United States, Department of Physics and Astronomy, University College London, London, WC1E 6BT, United Kingdom, Institute for Physics of Living Systems, University College London, London, WC1E 6BT, United Kingdom; Weirich, K.L., James Franck Institute, University of Chicago, Chicago, IL 60637, United States; Dinner, A.R., Institute for Biophysical Dynamics, University of Chicago, Chicago, IL 60637, United States, James Franck Institute, University of Chicago, Chicago, IL 60637, United States, Department of Chemistry, University of Chicago, Chicago, ...
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Stam S.,Freedman S.L.,Banerjee S.,et al. Filament rigidity and connectivity tune the deformation modes of active biopolymer networks[J],2017,114(47).
APA Stam S.,Freedman S.L.,Banerjee S.,Weirich K.L.,Dinner A.R.,&Gardel M.L..(2017).Filament rigidity and connectivity tune the deformation modes of active biopolymer networks.Proceedings of the National Academy of Sciences of the United States of America,114(47).
MLA Stam S.,et al."Filament rigidity and connectivity tune the deformation modes of active biopolymer networks".Proceedings of the National Academy of Sciences of the United States of America 114.47(2017).
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