ArticleBiophysical journal2018
The Antiparallel Dimerization of Myosin X Imparts Bundle Selectivity for Processive Motility.
Article in Biophysical journal, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 14 citations in OpenAlex.
- Molecular features of myosin F adapted for driving actin flows in Toxoplasma gondii.Journal of cell science · 2026Article
- Molecular features of Myosin F adapted for driving actin flows inbioRxiv : the preprint server for biology · 2025Article
- Chiral growth of adherent filopodia.Biophysical journal · 2023Article
- The Antiparallel Coiled-Coil Domain Allows Multiple Forward Step Sizes of Myosin X.The journal of physical chemistry letters · 2023Article
- Comparative analysis of the MyTH4-FERM myosins reveals insights into the determinants of actin track selection in polarized epithelia.Molecular biology of the cell · 2021Article
- Processivity and Velocity for Motors Stepping on Periodic Tracks.Biophysical journal · 2020Article
- Straightening Out the Elasticity of Myosin Cross-Bridges.Biophysical journal · 2020Review
- Simultaneous tracking of two motor domains reveals near simultaneous steps and stutter steps of myosin 10 on actin filament bundles.Biochemical and biophysical research communications · 2020Article
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Myosin X is an unconventional actin-based molecular motor involved in filopodial formation, microtubule-actin filament interaction, and cell migration. Myosin X is an important component of filopodia regulation, localizing to tips of growing filopodia by an unclear targeting mechanism. The native α-helical dimerization domain of myosin X is thought to associate with antiparallel polarity of the two amino acid chains, making myosin X the only myosin that is currently considered to form antiparallel dimers. This study aims to determine if antiparallel dimerization of myosin X imparts selectivity toward actin bundles by comparing the motility of parallel and antiparallel dimers of myosin X on single and fascin-bundled actin filaments. Antiparallel myosin X dimers exhibit selective processivity on fascin-bundled actin and are only weakly processive on single actin filaments below saturating [ATP]. Artificial forced parallel dimers of myosin X are robustly processive on both single and bundled actin, exhibiting no selectivity. To determine the relationship between gating of the reaction steps and observed differences in motility, a mathematical model was developed to correlate the parameters of motility with the biochemical and mechanical kinetics of the dimer. Results from the model, constrained by experimental data, suggest that the probability of binding forward, toward the barbed end of the actin filament, is lower in antiparallel myosin X on single actin filaments compared to fascin-actin bundles and compared to constructs of myosin X with parallel dimerization.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.