NE40CH09-Goedert ARI 8 June 2017 10:53 Propagation of Tau Aggregates and Neurodegeneration Michel Goedert,1 David S. Eisenberg,2 and R. Anthony Crowther1 1MRC Laboratory of Molecular Biology, Cambridge CB2 0QH, United Kingdom; email:
[email protected] 2Department of Biological Chemistry and Howard Hughes Medical Institute, University of California, Los Angeles, California 90095 Annu. Rev. Neurosci. 2017. 40:189–210 Keywords The Annual Review of Neuroscience is online at Alzheimer’s disease, amyloid, cell-to-cell spreading, disease propagation, neuro.annualreviews.org Pick’s disease, prion-like, protein strains, Tau, Tauopathies, toxicity https://doi.org/10.1146/annurev-neuro-072116- 031153 Abstract Copyright c 2017 by Annual Reviews. A pathway from the natively unfolded microtubule-associated protein Tau All rights reserved to a highly structured amyloid fibril underlies human Tauopathies. This ordered assembly causes disease and represents the gain of toxic function. In recent years, evidence has accumulated to suggest that Tau inclusions form first in a small number of brain cells, from where they propagate to other regions, resulting in neurodegeneration and disease. Propagation of ANNUAL pathology is often called prion-like, which refers to the capacity of an as- REVIEWS Further Annu. Rev. Neurosci. 2017.40:189-210. Downloaded from www.annualreviews.org Access provided by Occidental College Library on 11/13/18. For personal use only. sembled protein to induce the same abnormal conformation in a protein of Click here to view this article's online features: the same kind, initiating a self-amplifying cascade. In addition, prion-like • Download figures as PPT slides • Navigate linked references encompasses the release of protein aggregates from brain cells and their • Download citations • Explore related articles uptake by neighboring cells.