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Science. 2008 Feb 22;319(5866):1086-9. doi: 10.1126/science.1152993. Epub 2008 Jan 17.

Differential regulation of dynein and kinesin motor proteins by tau.

Author information

1
Department of Physiology and Pennsylvania Muscle Institute, University of Pennsylvania, Philadelphia, PA 19104, USA.

Abstract

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.

PMID:
18202255
PMCID:
PMC2866193
DOI:
10.1126/science.1152993
[Indexed for MEDLINE]
Free PMC Article

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