ArticleThe Journal of biological chemistry2013
Identification of a novel site in the tail of dynein heavy chain important for dynein function in vivo.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 27 citations in OpenAlex.
- VezA/vezatin facilitates proper assembly of the dynactin complex in vivo.Cell reports · 2024Article
- VezA/vezatin facilitates proper assembly of the dynactin complex in vivo.bioRxiv : the preprint server for biology · 2024Article
- Muscle and bone characteristics of a Chinese family with spinal muscular atrophy, lower extremity predominant 1 (SMALED1) caused by a novel missense DYNC1H1 mutation.BMC medical genomics · 2023Article
- Dynein activation in vivo is regulated by the nucleotide states of its AAA3 domain.Current biology : CB · 2021Article
- The splicing-factor Prp40 affects dynein-dynactin function inMolecular biology of the cell · 2020Article
- Cargo-Mediated Activation of Cytoplasmic DyneinFrontiers in cell and developmental biology · 2020Review
- LIS1 regulates cargo-adapter-mediated activation of dynein by overcoming its autoinhibition in vivo.The Journal of cell biology · 2019Article
- Setting the dynein motor in motion: New insights from electron tomography.The Journal of biological chemistry · 2019Review
- p25 of the dynactin complex plays a dual role in cargo binding and dynactin regulation.The Journal of biological chemistry · 2018Article
- Nuclear movement in fungi.Seminars in cell & developmental biology · 2018Review
- The actin capping protein in Aspergillus nidulans enhances dynein function without significantly affecting Arp1 filament assembly.Scientific reports · 2018Article
- Transport of fungal RAB11 secretory vesicles involves myosin-5, dynein/dynactin/p25, and kinesin-1 and is independent of kinesin-3.Molecular biology of the cell · 2017Article
- DYNC1H1 mutations associated with neurological diseases compromise processivity of dynein-dynactin-cargo adaptor complexes.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Discovery of a vezatin-like protein for dynein-mediated early endosome transport.Molecular biology of the cell · 2015Article
- Cytoplasmic dynein and early endosome transport.Cellular and molecular life sciences : CMLS · 2015Review
- FHIP and FTS proteins are critical for dynein-mediated transport of early endosomes in Aspergillus.Molecular biology of the cell · 2014Article
- HookA is a novel dynein-early endosome linker critical for cargo movement in vivo.The Journal of cell biology · 2014Article
- Cytoplasmic dynein heavy chain: the servant of many masters.Trends in neurosciences · 2013Review
- The yeast dynein Dyn2-Pac11 complex is a dynein dimerization/processivity factor: structural and single-molecule characterization.Molecular biology of the cell · 2013Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The minus end-directed microtubule motor cytoplasmic dynein is responsible for the intracellular movements of many organelles, including nuclei and endosomes. The dynein heavy chain contains a C-terminal motor domain and an N-terminal tail domain. The tail binds other dynein subunits and the cargo-interacting dynactin complex but is dispensable for movement of single dynein molecules in vitro. Here, we identified a mutation in the Aspergillus nidulans heavy chain tail domain, nudA(F208V), which causes obvious defects in dynein-mediated nuclear positioning and early endosome movement. Astonishingly, the nudA(F208I) mutation in the same position does not cause the same defects, suggesting that a subtle difference in the size of the amino acid side chain at this position has a significant consequence. Importantly, our biochemical analyses indicate that the nudA(F208V) mutation does not affect dynein subunit interactions and the mutant dynein is also able to bind dynactin and another dynein regulator, NUDF/LIS1. The mutant dynein is able to physically interact with the early endosome cargo, but dynein-mediated early endosome movement away from the hyphal tip occurs at a significantly reduced frequency. Within the small group of early endosomes that move away from the hyphal tip in the mutant, the average speed of movement is lower than that in the wild type. Given the dispensability of the dynein tail in dynein motility in vitro, our results support the notion that the structural integrity of the dynein tail is critical in vivo for the coordination of dynein force production and movement when the motor is heavily loaded.
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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.