Key result
Multiple-paths myosin V model matches experimental data for velocity, movement length, and randomness under load.
Why the study?
The study aimed to model the independent hydrolysis processes at the two heads of myosin V to better understand its stepping mechanism.
A proposed multiple-paths model accurately describes the biomechanical transition process and movement of myosin V under varying ATP concentrations and external loads.
Answers are grounded in this paper and cite their sources.
Supports multiple-paths model of myosin V; leaves open validation in cardiac myosins and clinical translation.
Myosin V, a two-headed motor protein, moves along actin filaments toward the positive end. Similar to other molecular motors, myosin V hydrolyzes Adenosine tri-phosphate (ATP) and releases its product to produce movement. This study proposes a multiple-paths model that considers the hydrolysis processes of catalytic sites at the two heads of myosin V as independent. The proposed model describes the myosin V transition process by seven states, with one load-dependent transition rate among these states. This model demonstrates how myosin V steps forward at different chemical reaction paths. This study also uses the enzyme kinetics to calculate the mean velocity. Stochastic processes are used to analyze the randomness as well. Analytical results reveal that the theoretical mean velocities, mean movement lengths, and randomness with various ATP concentrations under external load agree with the experimental data.
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Hsu et al. (2009) studied this question. Multiple-paths model was evaluated on Mean velocity, mean movement lengths, and randomness. A multiple-paths model of myosin V demonstrated that theoretical mean velocities, movement lengths, and randomness under external load agree with experimental data.
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