ArticleNature structural & molecular biology2015
The AAA3 domain of cytoplasmic dynein acts as a switch to facilitate microtubule release.
Article in Nature structural & molecular biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.
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Who cites it
56 citing papers in PubMed, 94 citations in OpenAlex.
- Characterizing dynamics of productive dynein stepping by MINFLUX.Nature structural & molecular biology · 2026Article
- A nucleotide code governs Lis1's ability to relieve dynein autoinhibition.Nature chemical biology · 2026Article
- Structural and ensemble-based mechanistic insights into cytoplasmic dynein-1.Frontiers in molecular biosciences · 2026Review
- The mechanochemical cycle of reactive full-length human dynein 1.Nature structural & molecular biology · 2025Article
- Multiple steps of dynein activation by Lis1 visualized by cryo-EM.Nature structural & molecular biology · 2025Article
- Cryo-EM captures early intermediate steps in dynein activation by LIS1.Nature communications · 2025Article
- Nanometer-resolution tracking of single cargo reveals dynein motor mechanisms.Nature chemical biology · 2025Article
- MINFLUX reveals dynein stepping in live neurons.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Stepping dynamics of dynein characterized by MINFLUX.bioRxiv : the preprint server for biology · 2024Article
- Review
- Conventional and Unconventional Protein Secretion in Yeast and Animal Cells.Methods in molecular biology (Clifton, N.J.) · 2024Review
- Article
- Measurements of the Force-Dependent Detachment Rates of Cytoplasmic Dynein from Microtubules.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Article
- Vesicle trafficking and vesicle fusion: mechanisms, biological functions, and their implications for potential disease therapy.Molecular biomedicine · 2022Review
- Dynein activation in vivo is regulated by the nucleotide states of its AAA3 domain.Current biology : CB · 2021Article
- Targeting allostery in the Dynein motor domain with small molecule inhibitors.Cell chemical biology · 2021Article
- Dynein Heavy Chain 64C Differentially Regulates Cell Survival and Proliferation of Wingless-Producing Cells inJournal of developmental biology · 2021Article
- Three-color single-molecule imaging reveals conformational dynamics of dynein undergoing motility.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Cytoplasmic factories for axonemal dynein assembly.Journal of cell science · 2021Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Cytoplasmic dynein is an AAA+ motor responsible for intracellular cargo transport and force generation along microtubules (MTs). Unlike kinesin and myosin, dynein contains multiple ATPase subunits, with AAA1 serving as the primary catalytic site. ATPase activity at AAA3 is also essential for robust motility, but its role in dynein's mechanochemical cycle remains unclear. Here, we introduced transient pauses in Saccharomyces cerevisiae dynein motility by using a slowly hydrolyzing ATP analog. Analysis of pausing behavior revealed that AAA3 hydrolyzes nucleotide an order of magnitude more slowly than AAA1, and the two sites do not coordinate. ATPase mutations to AAA3 abolish the ability of dynein to modulate MT release. Nucleotide hydrolysis at AAA3 lifts this 'MT gate' to allow fast motility. These results suggest that AAA3 acts as a switch that repurposes cytoplasmic dynein for fast cargo transport and MT-anchoring tasks in cells.
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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.