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Originally published in Science Express on 17 January 2008
Science 22 February 2008:
Vol. 319. no. 5866, pp. 1086 - 1089
DOI: 10.1126/science.1152993
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Reports

Differential Regulation of Dynein and Kinesin Motor Proteins by Tau

Ram Dixit, Jennifer L. Ross,* Yale E. Goldman, Erika L. F. Holzbaur{dagger}

Dynein and kinesin motor proteins transport cellular cargoes toward opposite ends of microtubule tracks. In neurons, microtubules are abundantly decorated with microtubule-associated proteins (MAPs) such as tau. Motor proteins thus encounter MAPs frequently along their path. To determine the effects of tau on dynein and kinesin motility, we conducted single-molecule studies of motor proteins moving along tau-decorated microtubules. Dynein tended to reverse direction, whereas kinesin tended to detach at patches of bound tau. Kinesin was inhibited at about a tenth of the tau concentration that inhibited dynein, and the microtubule-binding domain of tau was sufficient to inhibit motor activity. The differential modulation of dynein and kinesin motility suggests that MAPs can spatially regulate the balance of microtubule-dependent axonal transport.

Department of Physiology and Pennsylvania Muscle Institute, University of Pennsylvania, Philadelphia, PA 19104, USA.

* Present address: 302 Hasbrouck Laboratory, Department of Physics, University of Massachusetts at Amherst, Amherst, MA 01003, USA.

{dagger} To whom correspondence should be addressed. E-mail: holzbaur{at}mail.med.upenn.edu

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