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Sabine Schipper-Krom Katrin Juenemann Anne H. Jansen Anne Wiemhoefer Rianne van den Nieuwendijk Donna L. Smith Mark A. Hink Gillian P. Bates Hermen Overkleeft Huib Ovaa Eric Reits 《FEBS letters》2014
Neurodegenerative disorders such as Huntington’s disease are hallmarked by neuronal intracellular inclusion body formation. Whether proteasomes are irreversibly recruited into inclusion bodies in these protein misfolding disorders is a controversial subject. In addition, it has been proposed that the proteasomes may become clogged by the aggregated protein fragments, leading to impairment of the ubiquitin–proteasome system. Here, we show by fluorescence pulse-chase experiments in living cells that proteasomes are dynamically and reversibly recruited into inclusion bodies. As these recruited proteasomes remain catalytically active and accessible to substrates, our results challenge the concept of proteasome sequestration and impairment in Huntington’s disease, and support the reported absence of proteasome impairment in mouse models of Huntington’s disease. 相似文献
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