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An HDAC6-dependent surveillance mechanism suppresses tau-mediated neurodegeneration and cognitive decline. | LitMetric

AI Article Synopsis

  • - Tauopathies, like Alzheimer's disease, involve harmful tau protein buildup, particularly acetylated tau, which contributes to neurodegeneration and memory loss.
  • - HDAC6 is a critical protein that helps modify tau; it not only removes acetylation but also prevents excessive phosphorylation of tau, which is important for maintaining neuron health.
  • - Research shows that HDAC6 interacts with tau in brain areas affected by Alzheimer's, and mice lacking HDAC6 experience faster tau-related damage and cognitive decline, suggesting that HDAC6 helps protect against these diseases.

Article Abstract

Tauopathies including Alzheimer's disease (AD) are marked by the accumulation of aberrantly modified tau proteins. Acetylated tau, in particular, has recently been implicated in neurodegeneration and cognitive decline. HDAC6 reversibly regulates tau acetylation, but its role in tauopathy progression remains unclear. Here, we identified an HDAC6-chaperone complex that targets aberrantly modified tau. HDAC6 not only deacetylates tau but also suppresses tau hyperphosphorylation within the microtubule-binding region. In neurons and human AD brain, HDAC6 becomes co-aggregated within focal tau swellings and human AD neuritic plaques. Using mass spectrometry, we identify a novel HDAC6-regulated tau acetylation site as a disease specific marker for 3R/4R and 3R tauopathies, supporting uniquely modified tau species in different neurodegenerative disorders. Tau transgenic mice lacking HDAC6 show reduced survival characterized by accelerated tau pathology and cognitive decline. We propose that a HDAC6-dependent surveillance mechanism suppresses toxic tau accumulation, which may protect against the progression of AD and related tauopathies.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7606452PMC
http://dx.doi.org/10.1038/s41467-020-19317-4DOI Listing

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