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      Impact of branching on the elasticity of actin networks.

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          Abstract

          Actin filaments play a fundamental role in cell mechanics: assembled into networks by a large number of partners, they ensure cell integrity, deformability, and migration. Here we focus on the mechanics of the dense branched network found at the leading edge of a crawling cell. We develop a new technique based on the dipolar attraction between magnetic colloids to measure mechanical properties of branched actin gels assembled around the colloids. This technique allows us to probe a large number of gels and, through the study of different networks, to access fundamental relationships between their microscopic structure and their mechanical properties. We show that the architecture does regulate the elasticity of the network: increasing both capping and branching concentrations strongly stiffens the networks. These effects occur at protein concentrations that can be regulated by the cell. In addition, the dependence of the elastic modulus on the filaments' flexibility and on increasing internal stress has been studied. Our overall results point toward an elastic regime dominated by enthalpic rather than entropic deformations. This result strongly differs from the elasticity of diluted cross-linked actin networks and can be explained by the dense dendritic structure of lamellipodium-like networks.

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          Author and article information

          Journal
          Proc. Natl. Acad. Sci. U.S.A.
          Proceedings of the National Academy of Sciences of the United States of America
          Proceedings of the National Academy of Sciences
          1091-6490
          0027-8424
          Jun 26 2012
          : 109
          : 26
          Affiliations
          [1 ] Physique et Mécanique des Milieux Hétérogènes, École Supérieure de Physique et Chimie Industrielle de la ville de Paris, Centre National de la Recherche Scientifique Unité Mixte de Recherche 7636, Université Pierre et Marie Curie, Université Paris Diderot, 10 rue Vauquelin, 75005 Paris, France.
          Article
          1121238109
          10.1073/pnas.1121238109
          3387051
          22689953
          9645909a-c0f6-4316-80c7-7ceafaae6125
          History

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