ArticleFEBS open bio2018
Processivity of dimeric kinesin-1 molecular motors.
Article in FEBS open bio, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- A Model for Chemomechanical Coupling of Kinesin-3 Motor.Cellular and molecular bioengineering · 2024Article
- Magic-angle-spinning NMR structure of the kinesin-1 motor domain assembled with microtubules reveals the elusive neck linker orientation.Nature communications · 2022Article
- Modeling processive motion of kinesin-13 MCAK and kinesin-14 Cik1-Kar3 molecular motors.Protein science : a publication of the Protein Society · 2021Article
- Effect of Kinesin-5 Tail Domain on Motor Dynamics for Antiparallel Microtubule Sliding.International journal of molecular sciences · 2021Article
- Studies of Conformational Changes of Tubulin Induced by Interaction with Kinesin Using Atomistic Molecular Dynamics Simulations.International journal of molecular sciences · 2021Article
- A model of processive walking and slipping of kinesin-8 molecular motors.Scientific reports · 2021Article
- Theoretical Analysis of Dynamics of Kinesin Molecular Motors.ACS omega · 2020Article
- Run length distribution of dimerized kinesin-3 molecular motors: comparison with dimeric kinesin-1.Scientific reports · 2019Article
- Dynamics of cooperative cargo transport by two elastically coupled kinesin motors.The European physical journal. E, Soft matter · 2019Article
- Force Dependence of Velocity and Run Length of Kinesin-1, Kinesin-2 and Kinesin-5 Family Molecular Motors.Molecules (Basel, Switzerland) · 2019Article
- Epistatic Analysis of the Contribution of Rabs and Kifs to CATCHR Family Dependent Golgi Organization.Frontiers in cell and developmental biology · 2019Article
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Kinesin-1 is a homodimeric motor protein that can move along microtubule filaments by hydrolyzing ATP with a high processivity. How the two motor domains are coordinated to achieve such high processivity is not clear. To address this issue, we computationally studied the run length of the dimer with our proposed model. The computational data quantitatively reproduced the puzzling experimental data, including the dramatically asymmetric character of the run length with respect to the direction of external load acting on the coiled-coil stalk, the enhancement of the run length by addition of phosphate, and the contrary features of the run length for different types of kinesin-1 with extensions of their neck linkers compared with those without extension of the neck linker. The computational data on other aspects of the movement dynamics such as velocity and durations of one-head-bound and two-head-bound states in a mechanochemical coupling cycle were also in quantitative agreement with the available experimental data. Moreover, predicted results are provided on dependence of the run length upon external load acting on one head of the dimer, which can be easily tested in the future using single-molecule optical trapping assays.
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