ArticleScientific reports2016
Cytoplasmic dynein binding, run length, and velocity are guided by long-range electrostatic interactions.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 43 citations in OpenAlex.
- The mechanochemical cycle of reactive full-length human dynein 1.Nature structural & molecular biology · 2025Article
- AMOEBA Force Field Predicts Accurate Hydrogen Bond Counts of Nitriles in SNase by Revealing Water-Protein Interaction in Vibrational Absorption Frequencies.The journal of physical chemistry. B · 2023Article
- Regulatory mechanisms of the dynein-2 motility by post-translational modification revealed by MD simulation.Scientific reports · 2023Article
- AMOEBA Force Field Trajectories Improve Predictions of Accurate pThe journal of physical chemistry. B · 2022Article
- Electrostatics in Computational Biophysics and Its Implications for Disease Effects.International journal of molecular sciences · 2022Review
- Long-range electrostatic interactions significantly modulate the affinity of dynein for microtubules.Biophysical journal · 2022Article
- HIT web server: A hybrid method to improve electrostatic calculations for biomolecules.Computational and structural biotechnology journal · 2022Article
- Nano-Particles Carried by Multiple Dynein Motors Self-Regulate Their Number of Actively Participating Motors.International journal of molecular sciences · 2021Article
- Computational Study on DNA Repair: The Roles of Electrostatic Interactions Between Uracil-DNA Glycosylase (UDG) and DNA.Frontiers in molecular biosciences · 2021Article
- Hybrid method for representing ions in implicit solvation calculations.Computational and structural biotechnology journal · 2021Article
- A computational model of ESAT-6 complex in membrane.Journal of theoretical & computational chemistry · 2020Article
- Spike Proteins of SARS-CoV and SARS-CoV-2 Utilize Different Mechanisms to Bind With Human ACE2.Frontiers in molecular biosciences · 2020Article
- StructureMan: A Structure Manipulation Tool to Study Large Scale Biomolecular Interactions.Frontiers in molecular biosciences · 2020Article
- Directional Stepping Model for Yeast Dynein: Longitudinal- and Side-Step Distributions.Biophysical journal · 2019Article
- Processivity vs. Beating: Comparing Cytoplasmic and Axonemal Dynein Microtubule Binding Domain Association with Microtubule.International journal of molecular sciences · 2019Article
- Modeling Electrostatic Force in Protein-Protein Recognition.Frontiers in molecular biosciences · 2019Article
- E-hooks provide guidance and a soft landing for the microtubule binding domain of dynein.Scientific reports · 2018Article
- Allosteric conformational change cascade in cytoplasmic dynein revealed by structure-based molecular simulations.PLoS computational biology · 2017Article
- Forces and Disease: Electrostatic force differences caused by mutations in kinesin motor domains can distinguish between disease-causing and non-disease-causing mutations.Scientific reports · 2017Article
- DelPhiForce, a tool for electrostatic force calculations: Applications to macromolecular binding.Journal of computational chemistry · 2017Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Dyneins are important molecular motors involved in many essential biological processes, including cargo transport along microtubules, mitosis, and in cilia. Dynein motility involves the coupling of microtubule binding and unbinding to a change in the configuration of the linker domain induced by ATP hydrolysis, which occur some 25 nm apart. This leaves the accuracy of dynein stepping relatively inaccurate and susceptible to thermal noise. Using multi-scale modeling with a computational focusing technique, we demonstrate that the microtubule forms an electrostatic funnel that guides the dynein's microtubule binding domain (MTBD) as it finally docks to the precise, keyed binding location on the microtubule. Furthermore, we demonstrate that electrostatic component of the MTBD's binding free energy is linearly correlated with the velocity and run length of dynein, and we use this linearity to predict the effect of mutating each glutamic and aspartic acid located in MTBD domain to alanine. Lastly, we show that the binding of dynein to the microtubule is associated with conformational changes involving several helices, and we localize flexible hinge points within the stalk helices. Taken all together, we demonstrate that long range electrostatic interactions bring a level of precision to an otherwise noisy dynein stepping process.
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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.