Journal
NEUROSCIENCE
Volume 167, Issue 4, Pages 1044-1056Publisher
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.neuroscience.2010.02.077
Keywords
axoplasmic transport; glycogen synthase kinase-3 beta; cyclin dependent kinase 5; p25; mitochondrion transport
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Funding
- Belgian Federal Science Policy Office (BELSPO) [P6/43]
- Diane program (Wallon region)
- Fonds de la Recherche Scientifique Medicate
- Fondation pour la Recherche sur la maladie d'Alzheimer/Stichting voor Alzheimer Onderzoek
- Ligue Alzheimer
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The complex bi-directional axoplasmic transport of mitochondria is essential for proper metabolic functioning of neurons and is controlled by phosphorylation. We have investigated by time-lapse imaging the effects of increased expression of glycogen synthase kinase-3 beta (GSK-3 beta) and of the p25 activator of cyclin dependent kinase 5 on mitochondria movements in mammalian cortical neurons and in PC12 cells. Both GSK-3 beta and p25 increased the stationary behaviour of mitochondria in PC12 and in neurons, decreased their anterograde transport but did not affect the intrinsic velocities of mitochondria. The microtubule-associated tau proteins were more phosphorylated in GSK-3 beta and p25 transfected neurons, but ultrastructural observation showed that these cells still contained microtubules and nocodazole treatment further reduced residual mitochondria movements in GSK-3 beta or p25 transfected neurons, indicating that microtubule disruption was not the primary cause of increased mitochondrial stationary behaviour in GSK-3 beta or p25 transfected neurons. Our results suggest that increased expression of GSK-3 beta and p25 acted rather by decreasing the frequency of mitochondrial movements driven by molecular motors and that GSK-3 beta and p25 might regulate these transports by controlling the time that mitochondria spend pausing, rather than their velocities. (C) 2010 IBRO. Published by Elsevier Ltd. All rights reserved.
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