ArticleNano letters2026
Direct Observation of Nanometer-Sized Steps of Single Myosin VI Molecules in Living Cells.
Article in Nano letters, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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8 authors.
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Abstract
Living cells undergo dynamic biological processes. For example, motor proteins transport cargos by taking nanometer-sized steps. However, it is challenging to measure nanometer-sized steps in living cells. Using cell-permeable, extremely bright, and photostable deuterium congeners of tetramethyl(silicon)rhodamine (SiR-d12) connected chloroalkane linker to label single HaloTag-fused myosin VI in living cells and total internal reflection fluorescence microscopy (TIRFM), we measured nanometer-sized steps of single myosin VI in living cells. The measured step size of wild-type myosin VI was larger than that predicted from its short-lever arms. Furthermore, myosin VI harboring a mutation in the ATP-binding pocket exhibited longer dwell times between steps, reduced velocity, and shorter run lengths than wild-type myosin VI, underscoring the critical role of the ATP-binding pocket in motility. Therefore, our direct measurements of nanometer-sized steps of single motor proteins in living cells provide mechanistic insights into the dynamics and biological processes of motor proteins in living cells.
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