期刊
SCIENCE
卷 321, 期 5885, 页码 133-136出版社
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1159419
关键词
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资金
- NIAMS NIH HHS [P01 AR051174-050003, AR051174, P01 AR051174] Funding Source: Medline
- NIGMS NIH HHS [GM057247, R01 GM057247-10, R01 GM057247] Funding Source: Medline
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.
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