期刊
ACS MACRO LETTERS
卷 10, 期 9, 页码 1151-1158出版社
AMER CHEMICAL SOC
DOI: 10.1021/acsmacrolett.1c00500
关键词
-
资金
- William M. Keck Foundation Research Grant
- National Institute of General Medical Sciences Award [R15GM123420]
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.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据