ArticleThe EMBO journal2006
Processive movement of single kinesins on crowded microtubules visualized using quantum dots.
Article in The EMBO journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.
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Who cites it
50 citing papers in PubMed, 149 citations in OpenAlex.
- Nesprin-2 coordinates opposing microtubule motors during nuclear migration in neurons.The Journal of cell biology · 2024Article
- Microscopic interactions control a structural transition in active mixtures of microtubules and molecular motors.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Evaluating the effect of two-dimensional molecular layout on DNA origami-based transporters.Nanoscale advances · 2023Article
- Kinesin-1 transports morphologically distinct intracellular virions during vaccinia infection.Journal of cell science · 2023Article
- Myosin turnover controls actomyosin contractile instability.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Cargo surface fluidity can reduce inter-motor mechanical interference, promote load-sharing and enhance processivity in teams of molecular motors.PLoS computational biology · 2022Article
- Deformation of microtubules regulates translocation dynamics of kinesin.Science advances · 2021Article
- The crowding dynamics of the motor protein kinesin-II.PloS one · 2020Article
- Crowding and Pausing Strongly Affect Dynamics of Kinesin-1 Motors along Microtubules.Biophysical journal · 2018Article
- Secretory vesicle trafficking in awake and anaesthetized mice: differential speeds in axons versus synapses.The Journal of physiology · 2018Article
- Magnetic Cytoskeleton Affinity Purification of Microtubule Motors Conjugated to Quantum Dots.Bioconjugate chemistry · 2018Article
- Axonal neurofilaments exhibit frequent and complex folding behaviors.Cytoskeleton (Hoboken, N.J.) · 2018Article
- A fluid membrane enhances the velocity of cargo transport by small teams of kinesin-1.The Journal of chemical physics · 2018Article
- How the formation of amyloid plaques and neurofibrillary tangles may be related: a mathematical modelling study.Proceedings. Mathematical, physical, and engineering sciences · 2018Article
- Kymograph analysis with high temporal resolution reveals new features of neurofilament transport kinetics.Cytoskeleton (Hoboken, N.J.) · 2018Article
- aPKC Cycles between Functionally Distinct PAR Protein Assemblies to Drive Cell Polarity.Developmental cell · 2017Article
- Microtubule Defects Influence Kinesin-Based Transport In Vitro.Biophysical journal · 2016Article
- Effects of Obstacles on the Dynamics of Kinesins, Including Velocity and Run Length, Predicted by a Model of Two Dimensional Motion.PloS one · 2016Article
- Theoretical Analysis of Dynamic Processes for Interacting Molecular Motors.Journal of physics. A, Mathematical and theoretical · 2015Article
- Impact-Free Measurement of Microtubule Rotations on Kinesin and Cytoplasmic-Dynein Coated Surfaces.PloS one · 2015Article
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Kinesin-1 is a processive molecular motor transporting cargo along microtubules. Inside cells, several motors and microtubule-associated proteins compete for binding to microtubules. Therefore, the question arises how processive movement of kinesin-1 is affected by crowding on the microtubule. Here we use total internal reflection fluorescence microscopy to image in vitro the runs of single quantum dot-labelled kinesins on crowded microtubules under steady-state conditions and to measure the degree of crowding on a microtubule at steady-state. We find that the runs of kinesins are little affected by high kinesin densities on a microtubule. However, the presence of high densities of a mutant kinesin that is not able to step efficiently reduces the average speed of wild-type kinesin, while hardly changing its processivity. This indicates that kinesin waits in a strongly bound state on the microtubule when encountering an obstacle until the obstacle unbinds and frees the binding site for kinesin's next step. A simple kinetic model can explain quantitatively the behaviour of kinesin under both crowding conditions.
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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.