ArticleProceedings of the National Academy of Sciences of the United States of America2007
The coordination of cyclic microtubule association/dissociation and tail swing of cytoplasmic dynein.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.
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Who cites it
55 citing papers in PubMed, 95 citations in OpenAlex.
- Characterizing dynamics of productive dynein stepping by MINFLUX.Nature structural & molecular biology · 2026Article
- Multiple steps of dynein activation by Lis1 visualized by cryo-EM.Nature structural & molecular biology · 2025Article
- The mechanism and energetics of the dynein priming stroke.Structure (London, England : 1993) · 2024Article
- Microtubule-binding-induced allostery triggers LIS1 dissociation from dynein prior to cargo transport.Nature structural & molecular biology · 2023Article
- On and off controls within dynein-dynactin on native cargoes.Proceedings of the National Academy of Sciences of the United States of America · 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
- How Cytoplasmic Dynein Couples ATP Hydrolysis Cycle to Diverse Stepping Motions: Kinetic Modeling.Biophysical journal · 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
- Coupling of ATPase activity, microtubule binding, and mechanics in the dynein motor domain.The EMBO journal · 2019Article
- Step Sizes and Rate Constants of Single-headed Cytoplasmic Dynein Measured with Optical Tweezers.Scientific reports · 2018Article
- Motor Proteins.Cold Spring Harbor perspectives in biology · 2018Review
- She1 affects dynein through direct interactions with the microtubule and the dynein microtubule-binding domain.Nature communications · 2017Article
- Alpha-synuclein facilitates to form short unconventional microtubules that have a unique function in the axonal transport.Scientific reports · 2017Article
- Peptides mediating DNA transport on microtubules and their impact on non-viral gene transfer efficiency.Bioscience reports · 2017Review
- Allosteric conformational change cascade in cytoplasmic dynein revealed by structure-based molecular simulations.PLoS computational biology · 2017Article
- Angular measurements of the dynein ring reveal a stepping mechanism dependent on a flexible stalk.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The dynein motor domain is composed of a tail, head, and stalk and is thought to generate a force to microtubules by swinging the tail against the head during its ATPase cycle. For this "power stroke," dynein has to coordinate the tail swing with microtubule association/dissociation at the tip of the stalk. Although a detailed picture of the former process is emerging, the latter process remains to be elucidated. By using the single-headed recombinant motor domain of Dictyostelium cytoplasmic dynein, we address the questions of how the interaction of the motor domain with a microtubule is modulated by ATPase steps, how the two mechanical cycles (the microtubule association/dissociation and tail swing) are coordinated, and which ATPase site among the multiple sites in the motor domain regulates the coordination. Based on steady-state and pre-steady-state measurements, we demonstrate that the two mechanical cycles proceed synchronously at most of the intermediate states in the ATPase cycle: the motor domain in the poststroke state binds strongly to the microtubule with a K(d) of approximately 0.2 microM, whereas most of the motor domains in the prestroke state bind weakly to the microtubule with a K(d) of >10 microM. However, our results suggest that the timings of the microtubule affinity change and tail swing are staggered at the recovery stroke step in which the tail swings from the poststroke to the prestroke position. The ATPase site in the AAA1 module of the motor domain was found to be responsible for the coordination of these two mechanical processes.
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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.