Coupling of kinesin ATP turnover to translocation and microtubule regulation: One engine, many machines

Friel, Claire T.; Howard, Jonathon

Abstract

The cycle of ATP turnover is integral to the action of motor proteins. Here we discuss how variation in this cycle leads to variation of function observed amongst members of the kinesin superfamily of microtubule associated motor proteins. Variation in the ATP turnover cycle among superfamily members can tune the characteristic kinesin motor to one of the range of microtubule-based functions performed by kinesins. The speed at which ATP is hydrolysed affects the speed of translocation. The ratio of rate constants of ATP turnover in relation to association and dissociation from the microtubule influence the processivity of translocation. Variation in the rate-limiting step of the cycle can reverse the way in which the motor domain interacts with the microtubule producing non-motile kinesins. Because the ATP turnover cycle is not fully understood for the majority of kinesins, much work remains to show how the kinesin engine functions in such a wide variety of molecular machines. © 2012 The Author(s).

Citation

Friel, C. T., & Howard, J. (2012). Coupling of kinesin ATP turnover to translocation and microtubule regulation: One engine, many machines. Journal of Muscle Research and Cell Motility, 33(6), 377-383. https://doi.org/10.1007/s10974-012-9289-6

• Journal Article Type: Review
• Acceptance Date: Mar 8, 2012
• Online Publication Date: Mar 24, 2012
• Publication Date: Mar 24, 2012
• Deposit Date: Aug 11, 2022
• Journal: Journal of Muscle Research and Cell Motility
• Print ISSN: 0142-4319
• Electronic ISSN: 1573-2657
• Publisher: Springer Verlag
• Peer Reviewed: Not Peer Reviewed
• Volume: 33
• Issue: 6
• Pages: 377-383
• DOI: https://doi.org/10.1007/s10974-012-9289-6
• Public URL: https://nottingham-repository.worktribe.com/output/3182569
• Publisher URL: https://link.springer.com/article/10.1007/s10974-012-9289-6#citeas