The human form of tau exists in isoforms that contain either three (3R) or four (4R) microtubule-binding repeats. Tau can also form filamentous aggregates, which are a hallmark of Alzheimer disease and Pick disease. In this study, cryo-electron microscopy was used to investigate tau structure in these aggregates. The folded structure of tau that aggregates in patients with Pick disease was found to be distinct from that found in patients with Alzheimer disease, which might contribute to the distinct neuropathological phenotypes of these disorders.
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Falcon, B. et al. Structures of filaments from Pick’s disease reveal a novel tau protein fold. Nature 561, 137–140 (2018)
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Lewis, S. Untangling tau structure. Nat Rev Neurosci 19, 581 (2018). https://doi.org/10.1038/s41583-018-0063-7
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DOI: https://doi.org/10.1038/s41583-018-0063-7
