Journal
SOFT MATTER
Volume 14, Issue 37, Pages 7740-7747Publisher
ROYAL SOC CHEMISTRY
DOI: 10.1039/c8sm00741a
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Funding
- University of Chicago Materials Research Science and Engineering Center - National Science Foundation [DMR-1420709]
- DoD through the NDSEG Program
- NIH Ruth L. Kirschstein NRSA award [1F32GM113415-01]
- UCL Strategic Fellowship
- National Institutes of Health (NIH) [5 R01 GM109455-02]
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM109455, F32GM113415] Funding Source: NIH RePORTER
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Living cells dynamically modulate the local morphologies of their actin networks to perform biological functions, including force transduction, intracellular transport, and cell division. A major challenge is to understand how diverse structures of the actin cytoskeleton are assembled from a limited set of molecular building blocks. Here we study the spontaneous self-assembly of a minimal model of cytoskeletal materials, consisting of semiflexible actin filaments, crosslinkers, and molecular motors. Using coarse-grained simulations, we demonstrate that by changing concentrations and kinetics of crosslinkers and motors, as well as filament lengths, we can generate three distinct structural phases of actomyosin assemblies: bundled, polarity-sorted, and contracted. We introduce new metrics to distinguish these structural phases and demonstrate their functional roles. We find that the binding kinetics of motors and crosslinkers can be tuned to optimize contractile force generation, motor transport, and mechanical response. By quantitatively characterizing the relationships between the modes of cytoskeletal self-assembly, the resulting structures, and their functional consequences, our work suggests new principles for the design of active materials.
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