ArticleProceedings of the National Academy of Sciences of the United States of America2017
Parsing the roles of neck-linker docking and tethered head diffusion in the stepping dynamics of kinesin.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed.
- Neck region-microtubule interactions direct counterclockwise stepping of kinesin-1.Biophysical journal · 2026Article
- Competition between physical search and a weak-to-strong transition rate-limits kinesin binding times.PLoS computational biology · 2024Article
- ADP release can explain spatially-dependent kinesin binding times.bioRxiv : the preprint server for biology · 2023Article
- Regulatory mechanisms of the dynein-2 motility by post-translational modification revealed by MD simulation.Scientific reports · 2023Article
- Road-blocker HSP disease mutation disrupts pre-organization for ATP hydrolysis in kinesin through a second sphere control.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Plus and minus ends of microtubules respond asymmetrically to kinesin binding by a long-range directionally driven allosteric mechanism.Science advances · 2022Article
- Theory and simulations of condensin mediated loop extrusion in DNA.Nature communications · 2021Article
- Mechanistic basis of propofol-induced disruption of kinesin processivity.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Protein Diffusion on Charged Biopolymers: DNA versus Microtubule.Biophysical journal · 2020Article
- Tubulin tails and their modifications regulate protein diffusion on microtubules.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Influenza as a molecular walker.Chemical science · 2020Review
- Molecular dynamics simulation of the nanosecond pulsed electric field effect on kinesin nanomotor.Scientific reports · 2019Article
- How kinesin waits for ATP affects the nucleotide and load dependence of the stepping kinetics.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Mouse embryo geometry drives formation of robust signaling gradients through receptor localization.Nature communications · 2019Article
- Structural basis for power stroke vs. Brownian ratchet mechanisms of motor proteins.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Insights into Kinesin-1 Stepping from Simulations and Tracking of Gold Nanoparticle-Labeled Motors.Biophysical journal · 2019Article
- Interface Residues That Drive Allosteric Transitions Also Control the Assembly of l-Lactate Dehydrogenase.The journal of physical chemistry. B · 2018Article
- Structural consequences of hereditary spastic paraplegia disease-related mutations in kinesin.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Directionally biased sidestepping of Kip3/kinesin-8 is regulated by ATP waiting time and motor-microtubule interaction strength.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
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Authors and funding
3 authors.
Funding
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Abstract
Kinesin walks processively on microtubules (MTs) in an asymmetric hand-over-hand manner consuming one ATP molecule per 16-nm step. The individual contributions due to docking of the approximately 13-residue neck linker to the leading head (deemed to be the power stroke) and diffusion of the trailing head (TH) that contributes in propelling the motor by 16 nm have not been quantified. We use molecular simulations by creating a coarse-grained model of the MT-kinesin complex, which reproduces the measured stall force as well as the force required to dislodge the motor head from the MT, to show that nearly three-quarters of the step occurs by bidirectional stochastic motion of the TH. However, docking of the neck linker to the leading head constrains the extent of diffusion and minimizes the probability that kinesin takes side steps, implying that both the events are necessary in the motility of kinesin and for the maintenance of processivity. Surprisingly, we find that during a single step, the TH stochastically hops multiple times between the geometrically accessible neighboring sites on the MT before forming a stable interaction with the target binding site with correct orientation between the motor head and the [Formula: see text] tubulin dimer.
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