期刊
NEUROSCIENCE
卷 167, 期 4, 页码 1044-1056出版社
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.neuroscience.2010.02.077
关键词
axoplasmic transport; glycogen synthase kinase-3 beta; cyclin dependent kinase 5; p25; mitochondrion transport
资金
- 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
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.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据