Abstract
Myosin VI is an ATP driven molecular motor that functions as both a vesicle transporter and a cytoskeletal anchor. Recently, we reported that myosin VI generates three types of steps by taking either a distant binding or adjacent binding state. The adjacent binding state is unique to myosin VI and therefore may help explain some of myosin VI's distinct features including its dual functions. To better understand this state, we performed simultaneous observations of the head and tail domains and of the two head domains during motility. We found that the lever arms tilt forward in the adjacent binding state and that the nucleotide binding affinities are similar to that of the rear head domain in the distant binding state. From these results, we propose a model for how the adjacent binding state leads to myosin VI dual function.
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