A model of processive walking and slipping of kinesin-8 molecular motors

Xie, Ping

doi:10.1038/s41598-021-87532-0

Cited by 8 publications

(3 citation statements)

References 49 publications

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“…In time t r , the binding energy of the ADP-head to the local α/β-tubulin changes from E w1 to E w2 . As shown elsewhere, based on the above deduction, the proposed Brownian dynamics model for the chemomechanical coupling of kinesin dimers can explain well various experimental data on dynamics of different families of N-terminal kinesin motors such as kinesin-1, kinesin-3, kinesin-5, kinesin-8, and orphan kinesin PAKRP2 [28][29][30][31][32][33]. In particular, to fit the available single molecule data on load dependences of velocity, dissociation rate, run length, etc., for the kinesin motors, using the proposed Brownian dynamics model, it was estimated that E w1 ≤ 25 k B T and E w2 ≥ 35 k B T [30,[33][34][35][36][37][38], which are consistent with the values of E w1 = 17.7 k B T and E w2 = 35 k B T calculated here using all-atom MD simulations.…”

Section: Discussionsupporting

confidence: 55%

Studies of Conformational Changes of Tubulin Induced by Interaction with Kinesin Using Atomistic Molecular Dynamics Simulations

Shi

Wang

Chen

et al. 2021

IJMS

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The transition between strong and weak interactions of the kinesin head with the microtubule, which is regulated by the change of the nucleotide state of the head, is indispensable for the processive motion of the kinesin molecular motor on the microtubule. Here, using all-atom molecular dynamics simulations, the interactions between the kinesin head and tubulin are studied on the basis of the available high-resolution structural data. We found that the strong interaction can induce rapid large conformational changes of the tubulin, whereas the weak interaction cannot. Furthermore, we found that the large conformational changes of the tubulin have a significant effect on the interaction of the tubulin with the head in the weak-microtubule-binding ADP state. The calculated binding energy of the ADP-bound head to the tubulin with the large conformational changes is only about half that of the tubulin without the conformational changes.

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Section: Discussionsupporting

confidence: 55%

Studies of Conformational Changes of Tubulin Induced by Interaction with Kinesin Using Atomistic Molecular Dynamics Simulations

Shi

Wang

Chen

et al. 2021

IJMS

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“…Mechanical analysis indicates that as kinesin walks on the microtubule surface, it can carry a load of up to 6–8 pN. 35 In mechanical separation experiments of DNA, it was found that the force required to pull apart the double helix of a DNA molecule is ∼100 pN. 36 However, the electric forces generated by TTFields on MT, KT plate, and kinesin heads are notably smaller than the intrinsic typical values, indeed, smaller by an order of magnitude.…”

Section: Discussionmentioning

confidence: 99%

Electrodynamic interaction between tumor treating fields and microtubule electrophysiological activities

Li,

Liu,

Fang

et al. 2024

APL Bioengineering

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Tumor treating fields (TTFields) are a type of sinusoidal alternating current electric field that has proven effective in inhibiting the reproduction of dividing tumor cells. Despite their recognized impact, the precise biophysical mechanisms underlying the unique effects of TTFields remain unknown. Many of the previous studies predominantly attribute the inhibitory effects of TTFields to mitotic disruption, with intracellular microtubules identified as crucial targets. However, this conceptual framework lacks substantiation at the mesoscopic level. This study addresses the existing gap by constructing force models for tubulin and other key subcellular structures involved in microtubule electrophysiological activities under TTFields exposure. The primary objective is to explore whether the electric force or torque exerted by TTFields significantly influences the normal structure and activities of microtubules. Initially, we examine the potential effect on the dynamic stability of microtubule structures by calculating the electric field torque on the tubulin dimer orientation. Furthermore, given the importance of electrostatics in microtubule-associated activities, such as chromosome segregation and substance transport of kinesin during mitosis, we investigate the interaction between TTFields and these electrostatic processes. Our data show that the electrodynamic effects of TTFields are most likely too weak to disrupt normal microtubule electrophysiological activities significantly. Consequently, we posit that the observed cytoskeleton destruction in mitosis is more likely attributable to non-mechanical mechanisms.

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“…This is consistent with the previous argument for the potential form of the kinesin-1 head interacting with MT in the theoretical and numerical studies. [63,64]…”

Section: Dissociation Along the Forward Directionmentioning

confidence: 99%

Investigation of the structural and dynamic basis of kinesin dissociation from microtubule by atomistic molecular dynamics simulations

Wang¹,

Shi²,

Liu³

et al. 2022

Chinese Phys. B

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Kinesin is a molecular motor that can step processively on microtubules via the hydrolysis of ATP molecules. An important factor characterizing the processivity of the kinesin motor is its dissociation from the microtubule. Here, using all-atom molecular dynamics simulations, we studied the dissociation process of the kinesin head in weak-microtubule-binding or ADP state from tubulin on the basis of the available high-resolution structural data for the head and tubulin. By analyzing the simulated snapshots of the structure of the head-tubulin complex we provided detailed structural and dynamic information for the dissociation process. We found that the dissociation of the head along different directions relative to the tubulin exhibits very different dynamic behaviors. Moreover, the potential forms or energy landscapes of the interaction between the head and tubulin along different directions were determined. The studies have important implications for the detailed molecular mechanism of the dissociation of the kinesin motor and thus are critical to the mechanism of its processivity.

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A model of processive walking and slipping of kinesin-8 molecular motors

Cited by 8 publications

References 49 publications

Studies of Conformational Changes of Tubulin Induced by Interaction with Kinesin Using Atomistic Molecular Dynamics Simulations

Studies of Conformational Changes of Tubulin Induced by Interaction with Kinesin Using Atomistic Molecular Dynamics Simulations

Electrodynamic interaction between tumor treating fields and microtubule electrophysiological activities

Investigation of the structural and dynamic basis of kinesin dissociation from microtubule by atomistic molecular dynamics simulations

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