ArticleNature communications2016
The myosin X motor is optimized for movement on actin bundles.
Article in Nature communications, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.
What it found
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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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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
55 citing papers in PubMed, 96 citations in OpenAlex.
- Myosin II-independent contraction of actin filaments in membrane nanotubes.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Exosomal miR-20a-5p derived from renal tubular epithelial cells regulates podocyte cytoskeletal remodeling via targeting myosin X in diabetic kidney disease.Diabetology & metabolic syndrome · 2026Article
- AAV2 Crosslinks Actin Filaments: Implications for AAV Gene Therapy Vector Design.bioRxiv : the preprint server for biology · 2026Article
- Building the bridges: molecular mechanisms of tunneling nanotube formation.Cellular and molecular life sciences : CMLS · 2026Review
- Molecular features of myosin F adapted for driving actin flows in Toxoplasma gondii.Journal of cell science · 2026Article
- Direct Observation of Nanometer-Sized Steps of Single Myosin VI Molecules in Living Cells.Nano letters · 2026Article
- Molecular features of Myosin F adapted for driving actin flows inbioRxiv : the preprint server for biology · 2025Article
- Modulation of Filopodial Myosin Function.bioRxiv : the preprint server for biology · 2025Article
- The filopodial myosin DdMyo7 is a slow, calcium-regulated motor.The Journal of biological chemistry · 2025Article
- Select autosomal dominant DFNA11 deafness variants activate Myo7A targeting in epithelial cells.Journal of cell science · 2025Article
- Vimentin undergoes liquid-liquid phase separation to form droplets which wet and stabilize actin fibers.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Myosin-based nucleation of actin filaments contributes to stereocilia development critical for hearing.Nature communications · 2025Article
- Hundreds of myosin 10s are pushed to the tips of filopodia and could cause traffic jams on actin.eLife · 2024Article
- Pushing boundaries: mechanisms enabling bacterial pathogens to spread between cells.Infection and immunity · 2024Review
- Hundreds of myosin 10s are pushed to the tips of filopodia and could cause traffic jams on actin.bioRxiv : the preprint server for biology · 2024Article
- Sequence Alignment-Based Prediction of Myosin 7A: Structural Implications and Protein Interactions.International journal of molecular sciences · 2024Article
- Cell-particles interaction - selective uptake and transport of microdiamonds.Communications biology · 2024Article
- Toward physics-based precision medicine: Exploiting protein dynamics to design new therapeutics and interpret variants.Protein science : a publication of the Protein Society · 2024Review
- filoVision - using deep learning and tip markers to automate filopodia analysis.Journal of cell science · 2024Article
- Mechanisms underlying Myosin 10's contribution to the maintenance of mitotic spindle bipolarity.Molecular biology of the cell · 2024Article
Corrections and comments
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Authors and funding
17 authors at 4 institutions in 3 countries.
Funding
Abstract
Myosin X has features not found in other myosins. Its structure must underlie its unique ability to generate filopodia, which are essential for neuritogenesis, wound healing, cancer metastasis and some pathogenic infections. By determining high-resolution structures of key components of this motor, and characterizing the in vitro behaviour of the native dimer, we identify the features that explain the myosin X dimer behaviour. Single-molecule studies demonstrate that a native myosin X dimer moves on actin bundles with higher velocities and takes larger steps than on single actin filaments. The largest steps on actin bundles are larger than previously reported for artificially dimerized myosin X constructs or any other myosin. Our model and kinetic data explain why these large steps and high velocities can only occur on bundled filaments. Thus, myosin X functions as an antiparallel dimer in cells with a unique geometry optimized for movement on actin bundles.
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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.