ArticleProceedings of the National Academy of Sciences of the United States of America2012
Two independent switches regulate cytoplasmic dynein's processivity and directionality.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 49 citations in OpenAlex.
- Adaptor-mediated recruitment of three dyneins to dynactin enhances force generation.Nature cell biology · 2026Article
- Structural and ensemble-based mechanistic insights into cytoplasmic dynein-1.Frontiers in molecular biosciences · 2026Review
- Microtubule Dumbbells to Assess the Effect of Force Geometry on Single Kinesin Motors.Methods in molecular biology (Clifton, N.J.) · 2022Article
- TheInternational journal of molecular sciences · 2021Article
- Computational Tool for Ensemble Averaging of Single-Molecule Data.Biophysical journal · 2021Article
- These motors were made for walking.Protein science : a publication of the Protein Society · 2020Review
- How Cytoplasmic Dynein Couples ATP Hydrolysis Cycle to Diverse Stepping Motions: Kinetic Modeling.Biophysical journal · 2020Article
- Modulation of Kinesin's Load-Bearing Capacity by Force Geometry and the Microtubule Track.Biophysical journal · 2020Article
- A Tug-of-War Model Explains the Saltatory Sperm Cell Movement inFrontiers in plant science · 2020Article
- From isolated structures to continuous networks: A categorization of cytoskeleton-based motile engineered biological microstructures.Wiley interdisciplinary reviews. Nanomedicine and nanobiotechnology · 2019Review
- E-hooks provide guidance and a soft landing for the microtubule binding domain of dynein.Scientific reports · 2018Article
- Combining Structure-Function and Single-Molecule Studies on Cytoplasmic Dynein.Methods in molecular biology (Clifton, N.J.) · 2018Article
- Candida albicans Kinesin Kar3 Depends on a Cik1-Like Regulatory Partner Protein for Its Roles in Mating, Cell Morphogenesis, and Bipolar Spindle Formation.Eukaryotic cell · 2015Article
- Control of cytoplasmic dynein force production and processivity by its C-terminal domain.Nature communications · 2015Article
- Impact-Free Measurement of Microtubule Rotations on Kinesin and Cytoplasmic-Dynein Coated Surfaces.PloS one · 2015Article
- Ensemble velocity of non-processive molecular motors with multiple chemical states.Interface focus · 2014Article
- Increased spinal cord Na⁺-K⁺-2Cl⁻ cotransporter-1 (NKCC1) activity contributes to impairment of synaptic inhibition in paclitaxel-induced neuropathic pain.The Journal of biological chemistry · 2014Article
- Autoinhibition and cooperative activation mechanisms of cytoplasmic dynein.Nature cell biology · 2014Article
- The winch model can explain both coordinated and uncoordinated stepping of cytoplasmic dynein.Biophysical journal · 2014Article
- Article
Corrections and comments
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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
Cytoplasmic dynein is a microtubule-based molecular motor that participates in a multitude of cell activities, from cell division to organelle transport. Unlike kinesin and myosin, where different tasks are performed by highly specialized members of these superfamilies, a single form of the dynein heavy chain is utilized for different functions. This versatility demands an extensive regulation of motor function. Using an improved application of an optical trap, we were now able to demonstrate that cytoplasmic dynein can generate a discrete power stroke as well as a processive walk in either direction; i.e., towards the plus- or towards the minus-end of a microtubule. Thus, dynein's motor functions can be described by four basic modes of motion: processive and nonprocessive movement, and movement in the forward and reverse directions. Importantly, these four modes of movement can be controlled by two switches. One switch, based on phosphate, determines the directionality of movement. The second switch, depending on magnesium, converts cytoplasmic dynein from a nonprocessive to a processive motor. The two switches can be triggered separately or jointly by changing concentrations of phosphate and magnesium in the local environment. The control of four modes of movement by two switches has major implications for our understanding of the cellular functions and regulation of cytoplasmic dynein. Based on recent studies of dynein's structure we are able to draw new conclusions on cytoplasmic dynein's stepping mechanism.
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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.