Cargando…

Force Dependence of Velocity and Run Length of Kinesin-1, Kinesin-2 and Kinesin-5 Family Molecular Motors

Kinesin-1, kinesin-2 and kinesin-5 are three families of a superfamily of motor proteins; which can walk processively on microtubule filaments by hydrolyzing ATP. It was experimentally shown that while the three kinesin dimers show similar feature on the force dependence of velocity, they show rathe...

Descripción completa

Detalles Bibliográficos
Autores principales: Guo, Si-Kao, Wang, Wei-Chi, Wang, Peng-Ye, Xie, Ping
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6358798/
https://www.ncbi.nlm.nih.gov/pubmed/30646587
http://dx.doi.org/10.3390/molecules24020287
_version_ 1783392068388782080
author Guo, Si-Kao
Wang, Wei-Chi
Wang, Peng-Ye
Xie, Ping
author_facet Guo, Si-Kao
Wang, Wei-Chi
Wang, Peng-Ye
Xie, Ping
author_sort Guo, Si-Kao
collection PubMed
description Kinesin-1, kinesin-2 and kinesin-5 are three families of a superfamily of motor proteins; which can walk processively on microtubule filaments by hydrolyzing ATP. It was experimentally shown that while the three kinesin dimers show similar feature on the force dependence of velocity, they show rather different features on the force dependence of run length. However, why the three families of kinesins show these rather different features is unclear. Here, we computationally studied the movement dynamics of the three dimers based on our proposed model. The simulated results reproduce well the available experimental data on the force dependence of velocity and run length. Moreover, the simulated results on the velocity and run length for the three dimers with altered neck linker lengths are also in quantitative agreement with the available experimental data. The studies indicate that the three families of kinesins show much similar movement mechanism and the rather different features on the force dependence of run length arise mainly from the difference in rate constants of the ATPase activity and neck linker docking. Additionally, the asymmetric (limping) movement dynamics of the three families of homodimers with and without altered neck linker lengths are studied, providing predicted results.
format Online
Article
Text
id pubmed-6358798
institution National Center for Biotechnology Information
language English
publishDate 2019
publisher MDPI
record_format MEDLINE/PubMed
spelling pubmed-63587982019-02-06 Force Dependence of Velocity and Run Length of Kinesin-1, Kinesin-2 and Kinesin-5 Family Molecular Motors Guo, Si-Kao Wang, Wei-Chi Wang, Peng-Ye Xie, Ping Molecules Article Kinesin-1, kinesin-2 and kinesin-5 are three families of a superfamily of motor proteins; which can walk processively on microtubule filaments by hydrolyzing ATP. It was experimentally shown that while the three kinesin dimers show similar feature on the force dependence of velocity, they show rather different features on the force dependence of run length. However, why the three families of kinesins show these rather different features is unclear. Here, we computationally studied the movement dynamics of the three dimers based on our proposed model. The simulated results reproduce well the available experimental data on the force dependence of velocity and run length. Moreover, the simulated results on the velocity and run length for the three dimers with altered neck linker lengths are also in quantitative agreement with the available experimental data. The studies indicate that the three families of kinesins show much similar movement mechanism and the rather different features on the force dependence of run length arise mainly from the difference in rate constants of the ATPase activity and neck linker docking. Additionally, the asymmetric (limping) movement dynamics of the three families of homodimers with and without altered neck linker lengths are studied, providing predicted results. MDPI 2019-01-14 /pmc/articles/PMC6358798/ /pubmed/30646587 http://dx.doi.org/10.3390/molecules24020287 Text en © 2019 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Guo, Si-Kao
Wang, Wei-Chi
Wang, Peng-Ye
Xie, Ping
Force Dependence of Velocity and Run Length of Kinesin-1, Kinesin-2 and Kinesin-5 Family Molecular Motors
title Force Dependence of Velocity and Run Length of Kinesin-1, Kinesin-2 and Kinesin-5 Family Molecular Motors
title_full Force Dependence of Velocity and Run Length of Kinesin-1, Kinesin-2 and Kinesin-5 Family Molecular Motors
title_fullStr Force Dependence of Velocity and Run Length of Kinesin-1, Kinesin-2 and Kinesin-5 Family Molecular Motors
title_full_unstemmed Force Dependence of Velocity and Run Length of Kinesin-1, Kinesin-2 and Kinesin-5 Family Molecular Motors
title_short Force Dependence of Velocity and Run Length of Kinesin-1, Kinesin-2 and Kinesin-5 Family Molecular Motors
title_sort force dependence of velocity and run length of kinesin-1, kinesin-2 and kinesin-5 family molecular motors
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6358798/
https://www.ncbi.nlm.nih.gov/pubmed/30646587
http://dx.doi.org/10.3390/molecules24020287
work_keys_str_mv AT guosikao forcedependenceofvelocityandrunlengthofkinesin1kinesin2andkinesin5familymolecularmotors
AT wangweichi forcedependenceofvelocityandrunlengthofkinesin1kinesin2andkinesin5familymolecularmotors
AT wangpengye forcedependenceofvelocityandrunlengthofkinesin1kinesin2andkinesin5familymolecularmotors
AT xieping forcedependenceofvelocityandrunlengthofkinesin1kinesin2andkinesin5familymolecularmotors