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- W2912706226 abstract "Myosin X is an unconventional motor that can move along actin bundles. It is involved in the formation of filopodia in cells, which play important roles in migration and cell adhesion. It was found that myosin X monomers dimerize via an anti-parallel coiled coil. How anti-parallel myosin X moves along actin bundle has not been clearly understood yet. In particular, the stepping mechanism of single full-length myosin X remains enigmatic. Here, we investigated the stepping mechanism of myosin X along actin bundles by tracking labeled motor domain of myosin X with the total internal reflection microscopy. We observed clear stepping patterns under 2 μM ATP. The step size distributions of full-length myosin X were broad and had multiple peaks, which suggests several possible inter-motor configurations of myosin X. To further understand the stepping mechanism of myosin X, we labeled two motor domains of myosin X using different fluorescent molecules and tracked the motility of myosin X on actin bundles. We found that the distributions of stepping in two motors were broad and had multiple peaks. We also found that the distributions of inter-motor distance were broad. The broad distributions of steps with multiple peaks and inter-motor distances suggest that myosin X is optimized for moving along actin bundles." @default.
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- W2912706226 date "2019-02-01" @default.
- W2912706226 modified "2023-09-30" @default.
- W2912706226 title "Tracking of Labeled Motor Domains of Single Full-Length Myosin X on Actin Bundles" @default.
- W2912706226 doi "https://doi.org/10.1016/j.bpj.2018.11.1411" @default.
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