Rapid local compression in active gels is caused by nonlinear network response

D. Mizuno; C. Tardin; C. F. Schmidt

doi:10.1039/c9sm02362c

Rapid local compression in active gels is caused by nonlinear network response

D. Mizuno, C. Tardin, C. F. Schmidt

Condensed Matter Physics

Research output: Contribution to journal › Article › peer-review

2 Citations (Scopus)

Abstract

The actin cytoskeleton in living cells generates forces in conjunction with myosin motor proteins to directly and indirectly drive essential cellular processes. The semiflexible filaments of the cytoskeleton can respond nonlinearly to the collective action of motors. We here investigate mechanics and force generation in a model actin cytoskeleton, reconstituted in vitro, by observing the response and fluctuations of embedded micron-scale probe particles. Myosin mini-filaments can be modeled as force dipoles and give rise to deformations in the surrounding network of cross-linked actin. Anomalously correlated probe fluctuations indicate the presence of rapid local compression or draining of the network that emerges in addition to the ordinary linear shear elastic (incompressible) response to force dipoles. The anomalous propagation of compression can be attributed to the nonlinear response of actin filaments to the microscopic forces, and is quantitatively consistent with motor-generated large-scale stiffening of the gels.

Original language	English
Pages (from-to)	9369-9382
Number of pages	14
Journal	Soft Matter
Volume	16
Issue number	40
DOIs	https://doi.org/10.1039/c9sm02362c
Publication status	Published - Oct 28 2020

All Science Journal Classification (ASJC) codes

Chemistry(all)
Condensed Matter Physics

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title = "Rapid local compression in active gels is caused by nonlinear network response",

abstract = "The actin cytoskeleton in living cells generates forces in conjunction with myosin motor proteins to directly and indirectly drive essential cellular processes. The semiflexible filaments of the cytoskeleton can respond nonlinearly to the collective action of motors. We here investigate mechanics and force generation in a model actin cytoskeleton, reconstituted in vitro, by observing the response and fluctuations of embedded micron-scale probe particles. Myosin mini-filaments can be modeled as force dipoles and give rise to deformations in the surrounding network of cross-linked actin. Anomalously correlated probe fluctuations indicate the presence of rapid local compression or draining of the network that emerges in addition to the ordinary linear shear elastic (incompressible) response to force dipoles. The anomalous propagation of compression can be attributed to the nonlinear response of actin filaments to the microscopic forces, and is quantitatively consistent with motor-generated large-scale stiffening of the gels.",

author = "D. Mizuno and C. Tardin and Schmidt, {C. F.}",

note = "Funding Information: We acknowledge discussions with D. A. Head, and experimental supports by T. Toyota. This work was supported by JSPS KAKENHI Grant Number JP18H01189, JP25103011, JP15H03710 (to DM). This research was supported in part by the European Research Council under the European Union's Seventh Framework Programme (FP7/2007–2013)/ERC grant agreement no. 340528 (to CFS). Funding Information: We acknowledge discussions with D. A. Head, and experimental supports by T. Toyota. This work was supported by JSPS KAKENHI Grant Number JP18H01189, JP25103011, JP15H03710 (to DM). This research was supported in part by the European Research Council under the European Union{\textquoteright}s Seventh Framework Programme (FP7/2007–2013)/ERC grant agreement no. 340528 (to CFS). Publisher Copyright: {\textcopyright} The Royal Society of Chemistry.",

year = "2020",

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doi = "10.1039/c9sm02362c",

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AU - Mizuno, D.

AU - Tardin, C.

AU - Schmidt, C. F.

N1 - Funding Information: We acknowledge discussions with D. A. Head, and experimental supports by T. Toyota. This work was supported by JSPS KAKENHI Grant Number JP18H01189, JP25103011, JP15H03710 (to DM). This research was supported in part by the European Research Council under the European Union's Seventh Framework Programme (FP7/2007–2013)/ERC grant agreement no. 340528 (to CFS). Funding Information: We acknowledge discussions with D. A. Head, and experimental supports by T. Toyota. This work was supported by JSPS KAKENHI Grant Number JP18H01189, JP25103011, JP15H03710 (to DM). This research was supported in part by the European Research Council under the European Union’s Seventh Framework Programme (FP7/2007–2013)/ERC grant agreement no. 340528 (to CFS). Publisher Copyright: © The Royal Society of Chemistry.

PY - 2020/10/28

Y1 - 2020/10/28

N2 - The actin cytoskeleton in living cells generates forces in conjunction with myosin motor proteins to directly and indirectly drive essential cellular processes. The semiflexible filaments of the cytoskeleton can respond nonlinearly to the collective action of motors. We here investigate mechanics and force generation in a model actin cytoskeleton, reconstituted in vitro, by observing the response and fluctuations of embedded micron-scale probe particles. Myosin mini-filaments can be modeled as force dipoles and give rise to deformations in the surrounding network of cross-linked actin. Anomalously correlated probe fluctuations indicate the presence of rapid local compression or draining of the network that emerges in addition to the ordinary linear shear elastic (incompressible) response to force dipoles. The anomalous propagation of compression can be attributed to the nonlinear response of actin filaments to the microscopic forces, and is quantitatively consistent with motor-generated large-scale stiffening of the gels.

AB - The actin cytoskeleton in living cells generates forces in conjunction with myosin motor proteins to directly and indirectly drive essential cellular processes. The semiflexible filaments of the cytoskeleton can respond nonlinearly to the collective action of motors. We here investigate mechanics and force generation in a model actin cytoskeleton, reconstituted in vitro, by observing the response and fluctuations of embedded micron-scale probe particles. Myosin mini-filaments can be modeled as force dipoles and give rise to deformations in the surrounding network of cross-linked actin. Anomalously correlated probe fluctuations indicate the presence of rapid local compression or draining of the network that emerges in addition to the ordinary linear shear elastic (incompressible) response to force dipoles. The anomalous propagation of compression can be attributed to the nonlinear response of actin filaments to the microscopic forces, and is quantitatively consistent with motor-generated large-scale stiffening of the gels.

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Rapid local compression in active gels is caused by nonlinear network response

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