Unbinding of Kinesin from Microtubule in the Strongly Bound States Enhances under Assisting Forces

Khataee, H, Naseri, S, Zhong, Y and Liew, A 2018, 'Unbinding of Kinesin from Microtubule in the Strongly Bound States Enhances under Assisting Forces', Molecular Informatics, vol. 37, no. 4, pp. 1-7.


Document type: Journal Article
Collection: Journal Articles

Title Unbinding of Kinesin from Microtubule in the Strongly Bound States Enhances under Assisting Forces
Author(s) Khataee, H
Naseri, S
Zhong, Y
Liew, A
Year 2018
Journal name Molecular Informatics
Volume number 37
Issue number 4
Start page 1
End page 7
Total pages 7
Publisher Wiley - V C H Verlag GmbH & Co. KGaA
Abstract The ability to predict the cellular dynamics of intracellular transport has enormous potential to impact human health. A key transporter is kinesin-1, an ATP-driven molecular motor that shuttles cellular cargos along microtubules (MTs). The dynamics of kinesins depends critically on their unbinding rate from MT, which varies depending on the force direction applied on the motor, i.e. the force-unbinding rate relation is asymmetric. However, it remains unclear how changing the force direction from resisting (applied against the motion direction) to assisting (applied in the motion direction) alters the kinesin's unbinding and stepping. Here, we propose a theoretical model for the influence of the force direction on the stepping dynamics of a single kinesin. The model shows that the asymmetry of the force-unbinding rate relation is independent of ATP concentration. It also reveals that the synthesis of ATP from backward stepping under assisting forces is less likely than under resisting forces. It then finds that the unbinding of kinesin in the strongly MT-bound kinetic states enhances under assisting forces.
Subject Automation and Control Engineering
Keyword(s) assisting force
Kinesin
microtubule
unbinding rate
DOI - identifier 10.1002/minf.201700092
Copyright notice © 2018 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim
ISSN 1868-1743
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