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

Abstract Kinesin-8 molecular motor can move with superprocessivity on microtubules towards the plus end by hydrolyzing ATP molecules, depolymerizing microtubules. The available single molecule data for yeast kinesin-8 (Kip3) motor showed that its superprocessive movement is frequently interrupted by...

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Autor principal:	Ping Xie
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/68027f252c5549bf94e615b5806b255b
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spelling	oai:doaj.org-article:68027f252c5549bf94e615b5806b255b2021-12-02T18:03:15ZA model of processive walking and slipping of kinesin-8 molecular motors10.1038/s41598-021-87532-02045-2322https://doaj.org/article/68027f252c5549bf94e615b5806b255b2021-04-01T00:00:00Zhttps://doi.org/10.1038/s41598-021-87532-0https://doaj.org/toc/2045-2322Abstract Kinesin-8 molecular motor can move with superprocessivity on microtubules towards the plus end by hydrolyzing ATP molecules, depolymerizing microtubules. The available single molecule data for yeast kinesin-8 (Kip3) motor showed that its superprocessive movement is frequently interrupted by brief stick–slip motion. Here, a model is presented for the chemomechanical coupling of the kinesin-8 motor. On the basis of the model, the dynamics of Kip3 motor is studied analytically. The analytical results reproduce quantitatively the available single molecule data on velocity without including the slip and that with including the slip versus external load at saturating ATP as well as slipping velocity versus external load at saturating ADP and no ATP. Predicted results on load dependence of stepping ratio at saturating ATP and load dependence of velocity at non-saturating ATP are provided. Similarities and differences between dynamics of kinesin-8 and that of kinesin-1 are discussed.Ping XieNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 11, Iss 1, Pp 1-12 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Ping Xie A model of processive walking and slipping of kinesin-8 molecular motors
description	Abstract Kinesin-8 molecular motor can move with superprocessivity on microtubules towards the plus end by hydrolyzing ATP molecules, depolymerizing microtubules. The available single molecule data for yeast kinesin-8 (Kip3) motor showed that its superprocessive movement is frequently interrupted by brief stick–slip motion. Here, a model is presented for the chemomechanical coupling of the kinesin-8 motor. On the basis of the model, the dynamics of Kip3 motor is studied analytically. The analytical results reproduce quantitatively the available single molecule data on velocity without including the slip and that with including the slip versus external load at saturating ATP as well as slipping velocity versus external load at saturating ADP and no ATP. Predicted results on load dependence of stepping ratio at saturating ATP and load dependence of velocity at non-saturating ATP are provided. Similarities and differences between dynamics of kinesin-8 and that of kinesin-1 are discussed.
format	article
author	Ping Xie
author_facet	Ping Xie
author_sort	Ping Xie
title	A model of processive walking and slipping of kinesin-8 molecular motors
title_short	A model of processive walking and slipping of kinesin-8 molecular motors
title_full	A model of processive walking and slipping of kinesin-8 molecular motors
title_fullStr	A model of processive walking and slipping of kinesin-8 molecular motors
title_full_unstemmed	A model of processive walking and slipping of kinesin-8 molecular motors
title_sort	model of processive walking and slipping of kinesin-8 molecular motors
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/68027f252c5549bf94e615b5806b255b
work_keys_str_mv	AT pingxie amodelofprocessivewalkingandslippingofkinesin8molecularmotors AT pingxie modelofprocessivewalkingandslippingofkinesin8molecularmotors
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A model of processive walking and slipping of kinesin-8 molecular motors

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