ArticleScience (New York, N.Y.)2012
Structural basis for microtubule binding and release by dynein.
Article in Science (New York, N.Y.), 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 100 papers.
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Who cites it
100 citing papers in PubMed.
- Investigating the Function of C‑Terminal Tails of Human Tubulin Isotypes in the Motility Regulation of Cytoplasmic Dynein.ACS omega · 2026Article
- Structural and ensemble-based mechanistic insights into cytoplasmic dynein-1.Frontiers in molecular biosciences · 2026Review
- Cryo-ET and MD simulations reveal that dynein-2 is tuned for binding to the A-tubule of the ciliary doublet.The EMBO journal · 2025Article
- The mechanochemical cycle of reactive full-length human dynein 1.Nature structural & molecular biology · 2025Article
- Application of temperature replica exchange molecular dynamics: Structure of mitotic spindle-associated protein SHE1 and its binding to dynein.Computational and structural biotechnology journal · 2025Article
- Review
- Bi-allelic variants inHuman reproduction open · 2024Article
- ATP-induced conformational change of axonemal outer dynein arms revealed by cryo-electron tomography.The EMBO journal · 2023Article
- Article
- Regulatory mechanisms of the dynein-2 motility by post-translational modification revealed by MD simulation.Scientific reports · 2023Article
- Article
- The tubulin database: Linking mutations, modifications, ligands and local interactions.PloS one · 2023Article
- Regulation of motor activity of ciliary outer-arm dynein by the light chain 1; Implications from the structure of the light chain bound to the microtubule-binding domain of the heavy chain.Biophysics and physicobiology · 2023Article
- MAPping tubulin mutations.Frontiers in cell and developmental biology · 2023Review
- Article
- Article
- The force required to remove tubulin from the microtubule lattice by pulling on its α-tubulin C-terminal tail.Nature communications · 2022Article
- Long-range electrostatic interactions significantly modulate the affinity of dynein for microtubules.Biophysical journal · 2022Article
- Radical pairs may play a role in microtubule reorganization.Scientific reports · 2022Article
- Article
40 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
Cytoplasmic dynein is a microtubule-based motor required for intracellular transport and cell division. Its movement involves coupling cycles of track binding and release with cycles of force-generating nucleotide hydrolysis. How this is accomplished given the ~25 nanometers separating dynein's track- and nucleotide-binding sites is not understood. Here, we present a subnanometer-resolution structure of dynein's microtubule-binding domain bound to microtubules by cryo-electron microscopy that was used to generate a pseudo-atomic model of the complex with molecular dynamics. We identified large rearrangements triggered by track binding and specific interactions, confirmed by mutagenesis and single-molecule motility assays, which tune dynein's affinity for microtubules. Our results provide a molecular model for how dynein's binding to microtubules is communicated to the rest of the motor.
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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.