ArticleProceedings of the National Academy of Sciences of the United States of America2021
Three-color single-molecule imaging reveals conformational dynamics of dynein undergoing motility.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Characterizing dynamics of productive dynein stepping by MINFLUX.Nature structural & molecular biology · 2026Article
- Traction Force Microscopy with DNA FluoroCubes.Langmuir : the ACS journal of surfaces and colloids · 2026Article
- Nanometer-resolution tracking of single cargo reveals dynein motor mechanisms.Nature chemical biology · 2025Article
- Multicolor Tracking of Molecular Motors at Nanometer Resolution.Methods in molecular biology (Clifton, N.J.) · 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
- Multicolor Long-Term Single-Particle Tracking Using 10 nm Upconverting Nanoparticles.Nano letters · 2024Article
- Choosing the Probe for Single-Molecule Fluorescence Microscopy.International journal of molecular sciences · 2022Review
- Article
- Ultra-photostable DNA FluoroCubes: Mechanism of Photostability and Compatibility with FRET and Dark Quenching.Nano letters · 2022Article
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Authors and funding
4 authors.
Funding
Abstract
The motor protein dynein undergoes coordinated conformational changes of its domains during motility along microtubules. Previous single-molecule studies analyzed the motion of the AAA rings of the dynein homodimer, but not the distal microtubule-binding domains (MTBDs) that step along the track. Here, we simultaneously tracked with nanometer precision two MTBDs and one AAA ring of a single dynein as it underwent hundreds of steps using three-color imaging. We show that the AAA ring and the MTBDs do not always step simultaneously and can take differently sized steps. This variability in the movement between the AAA ring and MTBDs results in an unexpectedly large number of conformational states of dynein during motility. Extracting data on conformational transition biases, we could accurately model dynein stepping in silico. Our results reveal that the flexibility between major dynein domains is critical for dynein motility.
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