ArticleThe Journal of cell biology1992
Directional instability of microtubule transport in the presence of kinesin and dynein, two opposite polarity motor proteins.
Article in The Journal of cell biology, 1992. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.
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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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Who cites it
53 citing papers in PubMed, 131 citations in OpenAlex.
- MINFLUX reveals dynein stepping in live neurons.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Radial contractility of actomyosin rings facilitates axonal trafficking and structural stability.The Journal of cell biology · 2020Article
- Single Molecule Studies Enabled by Model-Based Controller Design.IEEE/ASME transactions on mechatronics : a joint publication of the IEEE Industrial Electronics Society and the ASME Dynamic Systems and Control Division · 2018Article
- Motor Reattachment Kinetics Play a Dominant Role in Multimotor-Driven Cargo Transport.Biophysical journal · 2018Article
- Modeling microtubule-based transport and anchoring of mRNA.SIAM journal on applied dynamical systems · 2018Article
- A Versatile Framework for Simulating the Dynamic Mechanical Structure of Cytoskeletal Networks.Biophysical journal · 2017Article
- Metaphase Spindle Assembly.Biology · 2017Review
- Back to the tubule: microtubule dynamics in Parkinson's disease.Cellular and molecular life sciences : CMLS · 2017Review
- Collective dynamics of processive cytoskeletal motors.Soft matter · 2016Review
- Emergent Properties of the Metaphase Spindle.Cold Spring Harbor perspectives in biology · 2015Review
- Bidirectional cargo transport: moving beyond tug of war.Nature reviews. Molecular cell biology · 2014Review
- Tug-of-war of microtubule filaments at the boundary of a kinesin- and dynein-patterned surface.Scientific reports · 2014Article
- Single-molecule fluorescence and in vivo optical traps: how multiple dyneins and kinesins interact.Chemical reviews · 2014Review
- In vivo optical trapping indicates kinesin's stall force is reduced by dynein during intracellular transport.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Building complexity: insights into self-organized assembly of microtubule-based architectures.Developmental cell · 2012Review
- Tug-of-war in motor protein ensembles revealed with a programmable DNA origami scaffold.Science (New York, N.Y.) · 2012Article
- Plus-end directed myosins accelerate actin filament sliding by single-headed myosin VI.Cytoskeleton (Hoboken, N.J.) · 2012Article
- Hybrid four-headed myosin motor engineered with antagonistic motor domains.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Adaptive braking by Ase1 prevents overlapping microtubules from sliding completely apart.Nature cell biology · 2011Article
- Force-velocity relationship for multiple kinesin motors pulling a magnetic bead.European biophysics journal : EBJ · 2011Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Kinesin and dynein are motor proteins that move in opposite directions along microtubules. In this study, we examine the consequences of having kinesin and dynein (ciliary outer arm or cytoplasmic) bound to glass surfaces interacting with the same microtubule in vitro. Although one might expect a balance of opposing forces to produce little or no net movement, we find instead that microtubules move unidirectionally for several microns (corresponding to hundreds of ATPase cycles by a motor) but continually switch between kinesin-directed and dynein-directed transport. The velocities in the plus-end (0.2-0.3 microns/s) and minus-end (3.5-4 microns/s) directions were approximately half those produced by kinesin (0.5 microns/s) and ciliary dynein (6.7 microns/s) alone, indicating that the motors not contributing to movement can interact with and impose a drag upon the microtubule. By comparing two dyneins with different duty ratios (percentage of time spent in a strongly bound state during the ATPase cycle) and varying the nucleotide conditions, we show that the microtubule attachment times of the two opposing motors as well as their relative numbers determine which motor predominates in this assay. Together, these findings are consistent with a model in which kinesin-induced movement of a microtubule induces a negative strain in attached dyneins which causes them to dissociate before entering a force-generating state (and vice versa); reversals in the direction of transport may require the temporary dissociation of the transporting motor from the microtubule. The bidirectional movements described here are also remarkably similar to the back-and-forth movements of chromosomes during mitosis and membrane vesicles in fibroblasts. These results suggest that the underlying mechanical properties of motor proteins, at least in part, may be responsible for reversals in microtubule-based transport observed 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.