ArticleThe Journal of cell biology2005
Long-range cooperative binding of kinesin to a microtubule in the presence of ATP.
Article in The Journal of cell biology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed.
- Article
- An Overview of Contrasting Experimental Results on Dynamics of Kinesin-1 Molecular Motors: Insight into the Underlying Mechanism.Biomolecules · 2025Review
- Structural switching of tubulin in the microtubule lattice.Biochemical Society transactions · 2025Review
- Tubulin CFEOM mutations both inhibit or activate kinesin motor activity.Molecular biology of the cell · 2024Article
- Cooperative ligand binding to a double-stranded Ising lattice-Application to cofilin binding to actin filaments.PNAS nexus · 2023Article
- Causes, costs and consequences of kinesin motors communicating through the microtubule lattice.Journal of cell science · 2023Article
- Article
- Motor guidance by long-range communication on the microtubule highway.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- A kinesin-1 variant reveals motor-induced microtubule damage in cells.Current biology : CB · 2022Article
- Plus and minus ends of microtubules respond asymmetrically to kinesin binding by a long-range directionally driven allosteric mechanism.Science advances · 2022Article
- Modeling spatiotemporally varying protein-protein interactions in CyLaKS, the Cytoskeleton Lattice-based Kinetic Simulator.The European physical journal. E, Soft matter · 2021Article
- Micron-scale geometrical features of microtubules as regulators of microtubule organization.eLife · 2021Review
- Long-Range and Directional Allostery of Actin Filaments Plays Important Roles in Various Cellular Activities.International journal of molecular sciences · 2020Review
- The model of local axon homeostasis - explaining the role and regulation of microtubule bundles in axon maintenance and pathology.Neural development · 2019Review
- Kinesin-binding-triggered conformation switching of microtubules contributes to polarized transport.The Journal of cell biology · 2018Article
- Crowding and Pausing Strongly Affect Dynamics of Kinesin-1 Motors along Microtubules.Biophysical journal · 2018Article
- Processive Kinesin-14 HSET Exhibits Directional Flexibility Depending on Motor Traffic.Current biology : CB · 2018Article
- Kinesin expands and stabilizes the GDP-microtubule lattice.Nature nanotechnology · 2018Article
- Mechanical Model of Nuclei Ordering in Drosophila Embryos Reveals Dilution of Stochastic Forces.Biophysical journal · 2018Article
- Review
Corrections and comments
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Interaction of kinesin-coated latex beads with a single microtubule (MT) was directly observed by fluorescence microscopy. In the presence of ATP, binding of a kinesin bead to the MT facilitated the subsequent binding of other kinesin beads to an adjacent region on the MT that extended for micrometers in length. This cooperative binding was not observed in the presence of ADP or 5'-adenylylimidodiphosphate (AMP-PNP), where binding along the MT was random. Cooperative binding also was induced by an engineered, heterodimeric kinesin, WT/E236A, that could hydrolyze ATP, yet remained fixed on the MT in the presence of ATP. Relative to the stationary WT/E236A kinesin on a MT, wild-type kinesin bound preferentially in close proximity, but was biased to the plus-end direction. These results suggest that kinesin binding and ATP hydrolysis may cause a long-range state transition in the MT, increasing its affinity for kinesin toward its plus end. Thus, our study highlights the active involvement of MTs in kinesin motility.
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