Journal
ACS MACRO LETTERS
Volume 10, Issue 9, Pages 1151-1158Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acsmacrolett.1c00500
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Funding
- William M. Keck Foundation Research Grant
- National Institute of General Medical Sciences Award [R15GM123420]
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In this study, light-activated myosin II motors were used to drive composites with varying actin-tubulin molar percentages, showing an increase in elastic plateau modulus and active restructuring of the cytoskeleton components. Nonlinear microrheology measurements demonstrated that motor-driven restructuring enhanced force response and stiffness while suppressing actin bending. The 50-50 composite exhibited the most dramatic mechanical response to motor activity due to a combination of added stiffness from microtubules and sufficient motor substrate.
The composite cytoskeleton, comprising interacting networks of semiflexible actin and rigid microtubules, generates forces and restructures by using motor proteins such as myosins to enable key processes including cell motility and mitosis. Yet, how motor-driven activity alters the mechanics of cytoskeleton composites remains an open challenge. Here, we perform optical tweezers microrheology and confocal imaging of composites with varying actin-tubulin molar percentages (25-75, 50-50, and 75-25), driven by light-activated myosin II motors, to show that motor activity increases the elastic plateau modulus by over 2 orders of magnitude by active restructuring of both actin and microtubules that persists for hours after motor activation has ceased. Nonlinear microrheology measurements show that motor-driven restructuring increases the force response and stiffness and suppresses actin bending. The 50-50 composite exhibits the most dramatic mechanical response to motor activity due to the synergistic effects of added stiffness from the microtubules and sufficient motor substrate for pronounced activity.
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