Key result
During ATP depletion, actin networks containing heavy meromyosin undergo a sol-gel transition accompanied by a sudden onset of directed filament motion, likely due to a zipping mechanism.
Demonstrates a sol-gel transition and directed filament motion in actin-myosin networks during ATP depletion, suggesting a 'zipping' mechanism for cooperativity.
Hypothesis-generating for cytoskeletal dynamics in energy-stressed cells; leaves open relevance to cardiomyocyte ischemia.
We present a study on filamentous actin solutions containing heavy meromyosin subfragments of myosin II motor molecules. We focus on the viscoelastic phase behavior and internal dynamics of such networks during adenosine-triphosphate depletion. By combining microrheology and fluorescence microscopy, we observed a sol-gel transition accompanied by a sudden onset of directed filament motion. We interpret the sol-gel transition in terms of myosin II enzymology, and suggest a ``zipping'' mechanism to explain the filament motion in the vicinity of the sol-gel transition.
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Uhde et al. (2004) studied In vitro actin-myosin networks. Heavy meromyosin (HMM) was evaluated on Viscoelastic phase behavior and internal dynamics during ATP depletion. During ATP depletion, actin networks containing heavy meromyosin undergo a sol-gel transition accompanied by a sudden onset of directed filament motion, likely due to a zipping mechanism.
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