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- W2069314092 abstract "The ability to sense molecular tension is crucial for a wide array of cellular processes, including the detection of auditory stimuli, control of cell shape, and internalization and transport of membranes. We show that myosin I, a motor protein that has been implicated in powering key steps in these processes, dramatically alters its motile properties in response to tension. We measured the displacement generated by single myosin I molecules, and we determined the actin-attachment kinetics with varying tensions using an optical trap. The rate of myosin I detachment from actin decreases >75-fold under tension of 2 piconewtons or less, resulting in myosin I transitioning from a low (<0.2) to a high (>0.9) duty-ratio motor. This impressive tension sensitivity supports a role for myosin I as a molecular force sensor." @default.
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- W2069314092 date "2008-07-04" @default.
- W2069314092 modified "2023-10-10" @default.
- W2069314092 title "Myosin I Can Act As a Molecular Force Sensor" @default.
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- W2069314092 doi "https://doi.org/10.1126/science.1159419" @default.
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