ArticleScientific reports2020
Small stepping motion of processive dynein revealed by load-free high-speed single-particle tracking.
Article in Scientific reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 20 citations in OpenAlex.
- Mapping Nanoscale Forces and Potentials in Live Cells with Microsecond 3D Single-Particle Tracking.Chemical & biomedical imaging · 2026Article
- Metallic nanoparticles: from biosynthesis to biomedical applications, current scenarios and prospects.Nanoscale advances · 2026Review
- Engineered Chitosan-Derived Nanocarrier for Efficient siRNA Delivery to Peripheral and Central Neurons.Advanced healthcare materials · 2025Article
- Rational engineering of DNA-nanoparticle motor with high speed and processivity comparable to motor proteins.Nature communications · 2025Article
- Regulatory mechanisms of the dynein-2 motility by post-translational modification revealed by MD simulation.Scientific reports · 2023Article
- Morphological Evidence for Novel Roles of Microtubules in Macrophage Phagocytosis.International journal of molecular sciences · 2023Article
- Direct observation of stepping rotation of V-ATPase reveals rigid component in coupling between VProceedings of the National Academy of Sciences of the United States of America · 2022Article
- Scattering-based Light Microscopy: From Metal Nanoparticles to Single Proteins.Chemical reviews · 2021Review
- Nano-Particles Carried by Multiple Dynein Motors Self-Regulate Their Number of Actively Participating Motors.International journal of molecular sciences · 2021Article
- Crystalline chitin hydrolase is a burnt-bridge Brownian motor.Biophysics and physicobiology · 2020Article
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Authors and funding
8 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cytoplasmic dynein is a dimeric motor protein which processively moves along microtubule. Its motor domain (head) hydrolyzes ATP and induces conformational changes of linker, stalk, and microtubule binding domain (MTBD) to trigger stepping motion. Here we applied scattering imaging of gold nanoparticle (AuNP) to visualize load-free stepping motion of processive dynein. We observed artificially-dimerized chimeric dynein, which has the head, linker, and stalk from Dictyostelium discoideum cytoplasmic dynein and the MTBD from human axonemal dynein, whose structure has been well-studied by cryo-electron microscopy. One head of a dimer was labeled with 30 nm AuNP, and stepping motions were observed with 100 μs time resolution and sub-nanometer localization precision at physiologically-relevant 1 mM ATP. We found 8 nm forward and backward steps and 5 nm side steps, consistent with on- and off-axes pitches of binding cleft between αβ-tubulin dimers on the microtubule. Probability of the forward step was 1.8 times higher than that of the backward step, and similar to those of the side steps. One-head bound states were not clearly observed, and the steps were limited by a single rate constant. Our results indicate dynein mainly moves with biased small stepping motion in which only backward steps are slightly suppressed.
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