Journal
SCIENCE
Volume 319, Issue 5866, Pages 1086-1089Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1152993
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Funding
- NIAMS NIH HHS [P01 AR051174, P01 AR051174-050002, P01-AR-051174] Funding Source: Medline
- NIGMS NIH HHS [GM-48661, R01 GM048661-16, R01 GM048661] Funding Source: Medline
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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.
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