A new study shows that aggregated forms of tau that cause frontotemporal dementia impair proteasome activity. Furthermore, proteasome inhibition can be alleviated by a small molecule that leads to proteasome phosphorylation and activation, thereby reducing tau accumulation.
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References
Spillantini, M.G. & Goedert, M. Lancet Neurol. 12, 609–622 (2013).
Lee, M.J., Lee, J.H. & Rubinsztein, D.C. Prog. Neurobiol. 105, 49–59 (2013).
Myeku, N. et al. Nat. Med. 22, 46–53 (2016).
Goldberg, A.L. Biochem. Soc. Trans. 35, 12–17 (2007).
Asai, M. et al. J. Mol. Cell. Cardiol. 46, 452–462 (2009).
Zhang, F. et al. J. Biol. Chem. 282, 22460–22471 (2007).
Myeku, N., Wang, H. & Figueiredo-Pereira, M.E. Neurosci. Lett. 527, 126–131 (2012).
Deriziotis, P. et al. EMBO J. 30, 3065–3077 (2011).
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Rubinsztein, D. Tau toxicity feeds forward in frontotemporal dementia. Nat Med 22, 24–25 (2016). https://doi.org/10.1038/nm.4029
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DOI: https://doi.org/10.1038/nm.4029
