ArticleThe journal of physical chemistry letters2023
The Antiparallel Coiled-Coil Domain Allows Multiple Forward Step Sizes of Myosin X.
Article in The journal of physical chemistry letters, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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3 citing papers in PubMed.
- Regulation and function of specialized membrane protrusions in intercellular communication.Nature reviews. Molecular cell biology · 2026Review
- Direct Observation of Nanometer-Sized Steps of Single Myosin VI Molecules in Living Cells.Nano letters · 2026Article
- Identification and analysis of pyroptosis-related key genes in heart failure.Journal of cardiothoracic surgery · 2025Article
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Authors and funding
8 authors.
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Abstract
Myosin X forms an antiparallel dimer and moves processively on actin bundles. How the antiparallel dimer affects the stepping mechanism of myosin X remains elusive. Here, we generated several chimeras using domains of myosin V and X and performed single-molecule motility assays. We found that the chimera containing the motor domain from myosin V and the lever arm and antiparallel coiled-coil domain from myosin X has multiple forward step sizes and moves processively, similar to full-length myosin X. The chimera containing the motor domain and lever arm from myosin X and the parallel coiled-coil from myosin V takes steps of ∼40 nm at lower ATP concentrations but was nonprocessive at higher ATP concentrations. Furthermore, mutant myosin X with four mutations in the antiparallel coiled-coil domain failed to dimerize and was nonprocessive. These results imply that the antiparallel coiled-coil domain is necessary for multiple forward step sizes of myosin X.
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