ArticleProceedings of the National Academy of Sciences of the United States of America2013
In vivo optical trapping indicates kinesin's stall force is reduced by dynein during intracellular transport.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 51 papers.
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Who cites it
51 citing papers in PubMed.
- Article
- Many dynein teams collectively generate high forces during the transport of large organelles.Biophysical journal · 2026Article
- DNA tensiometer reveals catch-bond detachment kinetics of kinesin-1, -2 and -3.bioRxiv : the preprint server for biology · 2025Article
- Measuring molecular forces inside living cells using magnetic tweezers.Biophysical reviews · 2025Review
- Kinesin-1-transported liposomes prefer to go straight in 3D microtubule intersections by a mechanism shared by other molecular motors.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Huntingtin S421 phosphorylation increases kinesin and dynein engagement on early endosomes and lysosomes.Biophysical journal · 2023Article
- On the use of thermal forces to probe kinesin's response to force.Frontiers in molecular biosciences · 2023Article
- Article
- High-throughput force measurement of individual kinesin-1 motors during multi-motor transport.Nanoscale · 2022Article
- Shear relaxation governs fusion dynamics of biomolecular condensates.Nature communications · 2021Article
- Multiscale mechanics and temporal evolution of vimentin intermediate filament networks.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Vimentin intermediate filaments stabilize dynamic microtubules by direct interactions.Nature communications · 2021Article
- On and off controls within dynein-dynactin on native cargoes.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Structure and Mechanics of Dynein Motors.Annual review of biophysics · 2021Review
- Optical tweezers in single-molecule biophysics.Nature reviews. Methods primers · 2021Article
- Dynamic actin cross-linking governs the cytoplasm's transition to fluid-like behavior.Molecular biology of the cell · 2020Article
- Article
- Probing force in living cells with optical tweezers: from single-molecule mechanics to cell mechanotransduction.Biophysical reviews · 2019Review
- Article
- Force sharing and force generation by two teams of elastically coupled molecular motors.Scientific reports · 2019Article
Corrections and comments
- Erratum issued
Authors and funding
5 authors.
Funding
Abstract
Kinesin and dynein are fundamental components of intracellular transport, but their interactions when simultaneously present on cargos are unknown. We built an optical trap that can be calibrated in vivo during data acquisition for each individual cargo to measure forces in living cells. Comparing directional stall forces in vivo and in vitro, we found evidence that cytoplasmic dynein is active during minus- and plus-end directed motion, whereas kinesin is only active in the plus direction. In vivo, we found outward (∼plus-end) stall forces range from 2 to 7 pN, which is significantly less than the 5- to 7-pN stall force measured in vitro for single kinesin molecules. In vitro measurements on beads with kinesin-1 and dynein bound revealed a similar distribution, implying that an interaction between opposite polarity motors causes this difference. Finally, inward (∼minus-end) stalls in vivo were 2-3 pN, which is higher than the 1.1-pN stall force of a single dynein, implying multiple active dynein.
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