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Soft Matter. 2019 Aug 21;15(31):6300-6307. doi: 10.1039/c9sm01263j. Epub 2019 Jul 25.

Stress relaxation in F-actin solutions by severing.

Author information

1
Department of Chemical & Biomolecular Engineering, Rice University, Houston, TX 77005, USA. fcmack@gmail.com and Center for Theoretical Biological Physics, Rice University, Houston, TX 77030, USA.
2
Department of Physics, University of Chicago, Chicago, IL 60637, USA and James Franck Institute, University of Chicago, Chicago, IL 60637, USA and Max Planck Institute of Molecular Cell Biology and Genetics, Pfotenhauerstraße 108, 01307 Dresden, Germany and Max Planck Institute for the Physics of Complex Systems, Nöthnitzerstraße 38, 01187 Dresden, Germany and Center for Systems Biology Dresden, Pfotenhauerstraße 108, 01307, Dresden, Germany.
3
Center for Theoretical Biological Physics, Rice University, Houston, TX 77030, USA.
4
Department of Physics, University of Chicago, Chicago, IL 60637, USA and James Franck Institute, University of Chicago, Chicago, IL 60637, USA and Institute for Biophysical Dynamics, University of Chicago, IL 60637, USA.
5
Department of Chemical & Biomolecular Engineering, Rice University, Houston, TX 77005, USA. fcmack@gmail.com and Center for Theoretical Biological Physics, Rice University, Houston, TX 77030, USA and Department of Chemistry, Rice University, Houston, TX 77005, USA and Department of Physics & Astronomy, Rice University, Houston, TX 77005, USA.

Abstract

Networks of filamentous actin (F-actin) are important for the mechanics of most animal cells. These cytoskeletal networks are highly dynamic, with a variety of actin-associated proteins that control cross-linking, polymerization and force generation in the cytoskeleton. Inspired by recent rheological experiments on reconstituted solutions of dynamic actin filaments, we report a theoretical model that describes stress relaxation behavior of these solutions in the presence of severing proteins. We show that depending on the kinetic rates of assembly, disassembly, and severing, one can observe both length-dependent and length-independent relaxation behavior.

PMID:
31342050
DOI:
10.1039/c9sm01263j

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