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- Marina Soares e Silva
- Foundation for Fundamental Research on Matter Institute for Atomic and Molecular Physics (FOM Institute AMOLF), 1009 DB, Amsterdam, The Netherlands; and
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- Martin Depken
- Vrije Universiteit Amsterdam, 1081 HV, Amsterdam, The Netherlands
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- Björn Stuhrmann
- Foundation for Fundamental Research on Matter Institute for Atomic and Molecular Physics (FOM Institute AMOLF), 1009 DB, Amsterdam, The Netherlands; and
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- Marijn Korsten
- Foundation for Fundamental Research on Matter Institute for Atomic and Molecular Physics (FOM Institute AMOLF), 1009 DB, Amsterdam, The Netherlands; and
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- Fred C. MacKintosh
- Vrije Universiteit Amsterdam, 1081 HV, Amsterdam, The Netherlands
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- Gijsje H. Koenderink
- Foundation for Fundamental Research on Matter Institute for Atomic and Molecular Physics (FOM Institute AMOLF), 1009 DB, Amsterdam, The Netherlands; and
書誌事項
- 公開日
- 2011-05-18
- DOI
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- 10.1073/pnas.1016616108
- 公開者
- Proceedings of the National Academy of Sciences
この論文をさがす
説明
<jats:p>In cells, many vital processes involve myosin-driven motility that actively remodels the actin cytoskeleton and changes cell shape. Here we study how the collective action of myosin motors organizes actin filaments into contractile structures in a simplified model system devoid of biochemical regulation. We show that this self-organization occurs through an active multistage coarsening process. First, motors form dense foci by moving along the actin network structure followed by coalescence. Then the foci accumulate actin filaments in a shell around them. These actomyosin condensates eventually cluster due to motor-driven coalescence. We propose that the physical origin of this multistage aggregation is the highly asymmetric load response of actin filaments: they can support large tensions but buckle easily under piconewton compressive loads. Because the motor-generated forces well exceed this threshold, buckling is induced on the connected actin network that resists motor-driven filament sliding. We show how this buckling can give rise to the accumulation of actin shells around myosin foci and subsequent coalescence of foci into superaggregates. This new physical mechanism provides an explanation for the formation and contractile dynamics of disordered condensed actomyosin states observed in vivo.</jats:p>
収録刊行物
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- Proceedings of the National Academy of Sciences
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Proceedings of the National Academy of Sciences 108 (23), 9408-9413, 2011-05-18
Proceedings of the National Academy of Sciences