ArticleBiophysical journal2018
A Unified Walking Model for Dimeric Motor Proteins.
Article in Biophysical journal, 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.
- Stall force measurement of the kinesin-3 motor KIF1A using a programmable DNA origami nanospring.eLife · 2026Article
- Extreme-value analysis in nano-biological systems: applications and implications.Biophysical reviews · 2024Review
- Modeling the motion of disease-associated KIF1A heterodimers.Biophysical journal · 2023Article
- Effect of varying load in moving period of a step on dynamics of molecular motors.The European physical journal. E, Soft matter · 2022Article
- Light-controlled micron-scale molecular motion.Nature chemistry · 2021Article
- A model of processive walking and slipping of kinesin-8 molecular motors.Scientific reports · 2021Article
- Backstepping Mechanism of Kinesin-1.Biophysical journal · 2020Article
- Dynamics of ATP-dependent and ATP-independent steppings of myosin-V on actin: catch-bond characteristics.Journal of the Royal Society, Interface · 2020Article
- A model for the chemomechanical coupling of the mammalian cytoplasmic dynein molecular motor.European biophysics journal : EBJ · 2019Article
- A model for the chemomechanical coupling of myosin-V molecular motors.RSC advances · 2019Article
- Physical parameters describing neuronal cargo transport by kinesin UNC-104.Biophysical reviews · 2019Review
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Authors and funding
3 authors.
Funding
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Abstract
Dimeric motor proteins, kinesin-1, cytoplasmic dynein-1, and myosin-V, move stepwise along microtubules and actin filaments with a regular step size. The motors take backward as well as forward steps. The step ratio r and dwell time τ, which are the ratio of the number of backward steps to the number of forward steps and the time between consecutive steps, respectively, were observed to change with the load. To understand the movement of motor proteins, we constructed a unified and simple mathematical model to explain the load dependencies of r and of τ measured for the above three types of motors quantitatively. Our model consists of three states, and the forward and backward steps are represented by the cycles of transitions visiting different pairs of states among the three, implying that a backward step is not the reversal of a forward step. Each of r and τ is given by a simple expression containing two exponential functions. The experimental data for r and τ for dynein available in the literature are not sufficient for a quantitative analysis, which is in contrast to those for kinesin and myosin-V. We reanalyze the data to obtain r and τ of native dynein to make up the insufficient data to fit them to the model. Our model successfully describes the behavior of r and τ for all of the motors in a wide range of loads from large assisting loads to superstall loads.
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