ArticleThe Journal of cell biology2015
A flipped ion pair at the dynein-microtubule interface is critical for dynein motility and ATPase activation.
Article in The Journal of cell biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 48 citations in OpenAlex.
- 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
- Microtubule-binding-induced allostery triggers LIS1 dissociation from dynein prior to cargo transport.Nature structural & molecular biology · 2023Article
- MAPping tubulin mutations.Frontiers in cell and developmental biology · 2023Review
- Mutation of the H12-helix of α-tubulin/MEC-12 disrupts the localization of neuronal mitochondria.microPublication biology · 2022Article
- The microtubule-associated protein She1 coordinates directional spindle positioning by spatially restricting dynein activity.Journal of cell science · 2021Article
- Structure and Mechanics of Dynein Motors.Annual review of biophysics · 2021Review
- The regulatory function of the AAA4 ATPase domain of cytoplasmic dynein.Nature communications · 2020Article
- Structure of Microtubule-Trapped Human Kinesin-5 and Its Mechanism of Inhibition Revealed Using Cryoelectron Microscopy.Structure (London, England : 1993) · 2020Article
- The complex of outer-arm dynein light chain-1 and the microtubule-binding domain of the γ heavy chain shows how axonemal dynein tunes ciliary beating.The Journal of biological chemistry · 2020Article
- Structural basis for two-way communication between dynein and microtubules.Nature communications · 2020Article
- A model for the chemomechanical coupling of the mammalian cytoplasmic dynein molecular motor.European biophysics journal : EBJ · 2019Article
- Molecular mechanism of cytoplasmic dynein tension sensing.Nature communications · 2019Article
- TUBA1A mutations identified in lissencephaly patients dominantly disrupt neuronal migration and impair dynein activity.Human molecular genetics · 2019Article
- Overview of the mechanism of cytoskeletal motors based on structure.Biophysical reviews · 2018Review
- Structural atlas of dynein motors at atomic resolution.Biophysical reviews · 2018Review
Corrections and comments
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Authors and funding
12 authors at 6 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Dynein is a motor protein that moves on microtubules (MTs) using the energy of adenosine triphosphate (ATP) hydrolysis. To understand its motility mechanism, it is crucial to know how the signal of MT binding is transmitted to the ATPase domain to enhance ATP hydrolysis. However, the molecular basis of signal transmission at the dynein-MT interface remains unclear. Scanning mutagenesis of tubulin identified two residues in α-tubulin, R403 and E416, that are critical for ATPase activation and directional movement of dynein. Electron cryomicroscopy and biochemical analyses revealed that these residues form salt bridges with the residues in the dynein MT-binding domain (MTBD) that work in concert to induce registry change in the stalk coiled coil and activate the ATPase. The R403-E3390 salt bridge functions as a switch for this mechanism because of its reversed charge relative to other residues at the interface. This study unveils the structural basis for coupling between MT binding and ATPase activation and implicates the MTBD in the control of directional movement.
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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.