ArticleACS chemical neuroscience2025
Impact of Lysine Acetylation Mutations on the Structure of Full-Length Tau Fibrils.
Article in ACS chemical neuroscience, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
The tau protein aggregates into amyloid fibrils in Alzheimer's disease and other neurodegenerative diseases. In these tauopathies, tau is decorated with posttranslational modifications, including phosphorylation and acetylation, suggesting that these modifications may cause tau to aggregate into specific pathological structures. Here, we investigate how pseudoacetylation of three lysine residues, K311Q, K321Q, and K369Q, affects the fibrilization and fibril structure of full-length four-repeat tau. These acetyl mimics are in addition to four phospho-mimetic glutamate mutations at the PHF1 epitope (4E tau). The joint mutant 4E3Q tau formed well-ordered amyloid fibrils without anionic cofactors. The 4E3Q tau fibrils lack twists, preventing structure determination by cryoelectron microscopy and necessitating characterization by solid-state NMR.
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