ArticleMethods in molecular biology (Clifton, N.J.)2018
Combining Structure-Function and Single-Molecule Studies on Cytoplasmic Dynein.
Article in Methods in molecular biology (Clifton, N.J.), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 16 citations in OpenAlex.
- SLICK: A Sandwich-LIke Culturing Kit forbioRxiv : the preprint server for biology · 2025Article
- Measurements of the Force-Dependent Detachment Rates of Cytoplasmic Dynein from Microtubules.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Article
- ALS-linked KIF5A ΔExon27 mutant causes neuronal toxicity through gain-of-function.EMBO reports · 2022Article
- Single-Molecule Studies on the Motion and Force Generation of the Kinesin-3 Motor KIF1A.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Targeting allostery in the Dynein motor domain with small molecule inhibitors.Cell chemical biology · 2021Article
- Genotype and defects in microtubule-based motility correlate with clinical severity inHGG advances · 2021Article
- The regulatory function of the AAA4 ATPase domain of cytoplasmic dynein.Nature communications · 2020Article
- Self-organized networks: Darwinian evolution of dynein rings, stalks, and stalk heads.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Force production of human cytoplasmic dynein is limited by its processivity.Science advances · 2020Article
- Directional Stepping Model for Yeast Dynein: Longitudinal- and Side-Step Distributions.Biophysical journal · 2019Article
- Molecular mechanism of cytoplasmic dynein tension sensing.Nature communications · 2019Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Cytoplasmic dynein is the largest and most intricate cytoskeletal motor protein. It is responsible for a vast array of biological functions, ranging from the transport of organelles and mRNAs to the movement of nuclei during neuronal migration and the formation and positioning of the mitotic spindle during cell division. Despite its megadalton size and its complex design, recent success with the recombinant expression of the dynein heavy chain has advanced our understanding of dynein's molecular mechanism through the combination of structure-function and single-molecule studies. Single-molecule fluorescence assays have provided detailed insights into how dynein advances along its microtubule track in the absence of load, while optical tweezers have yielded insights into the force generation and stalling behavior of dynein. Here, using the S. cerevisiae expression system, we provide improved protocols for the generation of dynein mutants and for the expression and purification of the mutated and/or tagged proteins. To facilitate single-molecule fluorescence and optical trapping assays, we further describe updated, easy-to-use protocols for attaching microtubules to coverslip surfaces. The presented protocols together with the recently solved crystal structures of the dynein motor domain will further simplify and accelerate hypothesis-driven mutagenesis and structure-function studies on dynein.
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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.