Coupling of Kinesin ATP Turnover to Translocation and Microtubule Regulation: One Engine, Many Machines

Overview

Journal J Muscle Res Cell Motil

Specialties Cell Biology
Physiology

Date 2012 Mar 27

PMID 22447431

Citations 13

Authors

Claire T Friel

Jonathon Howard

Affiliations

Soon will be listed here.

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.

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