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Cellular polyamines condense hyperphosphorylated Tau, triggering Alzheimer’s disease
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Cellular polyamines condense hyperphosphorylated Tau, triggering Alzheimer’s disease
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Journal Article
Cellular polyamines condense hyperphosphorylated Tau, triggering Alzheimer’s disease
2020
Overview
Many gaps in our understanding of Alzheimer’s disease remain despite intense research efforts. One such prominent gap is the mechanism of Tau condensation and fibrillization. One viewpoint is that positively charged Tau is condensed by cytosolic polyanions. However, this hypothesis is likely based on an overestimation of the abundance and stability of cytosolic polyanions and an underestimation of crucial intracellular constituents – the cationic polyamines. Here, we propose an alternative mechanism grounded in cellular biology. We describe extensive molecular dynamics simulations and analysis on physiologically relevant model systems, which suggest that it is not positively charged, unmodified Tau that is condensed by cytosolic polyanions but negatively charged, hyperphosphorylated Tau that is condensed by cytosolic polycations. Our work has broad implications for anti-Alzheimer’s research and drug development and the broader field of tauopathies in general, potentially paving the way to future etiologic therapies.
Publisher
Nature Publishing Group UK,Nature Publishing Group
Subject
/ Alzheimer Disease - metabolism
/ Biogenic Polyamines - adverse effects
/ Biogenic Polyamines - chemistry
/ Humanities and Social Sciences
/ Humans
/ Molecular Dynamics Simulation
/ Polyelectrolytes - metabolism
/ Protein Aggregation, Pathological - etiology
/ Protein Aggregation, Pathological - metabolism
/ Science
