ArticleNature communications2015
Control of cytoplasmic dynein force production and processivity by its C-terminal domain.
Article in Nature communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
47 citing papers in PubMed, 87 citations in OpenAlex.
- Adaptor-mediated recruitment of three dyneins to dynactin enhances force generation.Nature cell biology · 2026Article
- DNAHX: a novel, non-motile dynein heavy chain subfamily, identified by cryo-EM endogenously.bioRxiv : the preprint server for biology · 2025Article
- Single-Molecule Studies on the Motion and Force Generation of the Kinesin-3 Motor KIF1A.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Cytoplasmic factories for axonemal dynein assembly.Journal of cell science · 2021Article
- Flexible microtubule anchoring modulates the bi-directional motility of the kinesin-5 Cin8.Cellular and molecular life sciences : CMLS · 2021Article
- [Effect of dexamethasone on the expression of Dynein heavy chain and Dynactin in the cytoplasm of fetal rat cerebral cortical neurons culturedZhongguo dang dai er ke za zhi = Chinese journal of contemporary pediatrics · 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
- Aggresomal sequestration and STUB1-mediated ubiquitylation during mammalian proteaphagy of inhibited proteasomes.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Dynamic catch-bonding generates the large stall forces of cytoplasmic dynein.Physical biology · 2020Article
- Force production of human cytoplasmic dynein is limited by its processivity.Science advances · 2020Article
- The Generation of Dynein Networks by Multi-Layered Regulation and Their Implication in Cell Division.Frontiers in cell and developmental biology · 2020Review
- Cargo adaptors regulate stepping and force generation of mammalian dynein-dynactin.Nature chemical biology · 2019Article
- 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
- Review
- Load-dependent detachment kinetics plays a key role in bidirectional cargo transport by kinesin and dynein.Traffic (Copenhagen, Denmark) · 2019Article
- Force sharing and force generation by two teams of elastically coupled molecular motors.Scientific reports · 2019Article
- Application of the fluctuation theorem for noninvasive force measurement in living neuronal axons.Molecular biology of the cell · 2018Article
- A Unified Walking Model for Dimeric Motor Proteins.Biophysical journal · 2018Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Cytoplasmic dynein is a microtubule motor involved in cargo transport, nuclear migration and cell division. Despite structural conservation of the dynein motor domain from yeast to higher eukaryotes, the extensively studied S. cerevisiae dynein behaves distinctly from mammalian dyneins, which produce far less force and travel over shorter distances. However, isolated reports of yeast-like force production by mammalian dynein have called interspecies differences into question. We report that functional differences between yeast and mammalian dynein are real and attributable to a C-terminal motor element absent in yeast, which resembles a 'cap' over the central pore of the mammalian dynein motor domain. Removal of this cap increases the force generation of rat dynein from 1 pN to a yeast-like 6 pN and greatly increases its travel distance. Our findings identify the CT-cap as a novel regulator of dynein function.
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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.