Abstract
Multiple neurodegenerative conditions including Alzheimer's disease and frontotemporal dementia are characterized by the accumulation of tau in the brain, associated with synapse loss and cognitive decline. Currently, the molecular events that lead to tau aggregation, and the pathological effects of the tau protein, are incompletely understood. Recent work has highlighted aberrant acetylation of tau as a key to understanding the pathophysiological roles of this protein. Specific acetylation sites regulate the formation of tau aggregates, synaptic signaling and long-term potentiation. Unraveling the details of this emerging story may offer novel insights into potential therapeutic approaches for devastating neurodegenerative diseases.
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