Article
FTD-tau S320F mutation stabilizes local structure and allosterically promotes amyloid motif-dependent aggregation.
Nature communications - 23 Mar 2023
Chen Dailu, Bali Sofia, Singh Ruhar, Wosztyl Aleksandra, Mullapudi Vishruth, Vaquer-Alicea Jaime, Jayan Parvathy, Melhem Shamiram, Seelaar Harro, van Swieten John C, Diamond Marc I, Joachimiak Lukasz A
Abstract excerpt
Amyloid deposition of the microtubule-associated protein tau is associated with neurodegenerative diseases. In frontotemporal dementia with abnormal tau (FTD-tau), missense mutations in tau enhance its aggregation propensity. Here we describe the structural mechanism for how an FTD-tau S320F mutation drives spontaneous aggregation, integrating data from in vitro, in silico and cellular experiments. We find that...
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