Abstract
Myo1c, a widely expressed single-headed myosin, has been proposed to act in a variety of cellular processes, including insulin-stimulated transport of GLUT4 and mechanosensing in sensory hair cells; however, the mechanical and kinetic properties of a transporter and a tension sensor are very different. To better understand the adaptations of myo1c for its molecular roles in the cell, we examined its biochemical and mechanical properties using ensemble kinetic and single molecule techniques. Consistent with previous reports, we found that the myo1c working stroke is comprised of two substeps, which are likely associated with phosphate and ADP release.
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