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000264175 1001_ $$0P:(DE-2719)2812532$$aChakraborty, Pijush$$b0$$eFirst author
000264175 245__ $$aAcetylation discriminates disease-specific tau deposition.
000264175 260__ $$a[London]$$bNature Publishing Group UK$$c2023
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000264175 520__ $$aPathogenic aggregation of the protein tau is a hallmark of Alzheimer's disease and several other tauopathies. Tauopathies are characterized by the deposition of specific tau isoforms as disease-related tau filament structures. The molecular processes that determine isoform-specific deposition of tau are however enigmatic. Here we show that acetylation of tau discriminates its isoform-specific aggregation. We reveal that acetylation strongly attenuates aggregation of four-repeat tau protein, but promotes amyloid formation of three-repeat tau. We further identify acetylation of lysine 298 as a hot spot for isoform-specific tau aggregation. Solid-state NMR spectroscopy demonstrates that amyloid fibrils formed by unmodified and acetylated three-repeat tau differ in structure indicating that site-specific acetylation modulates tau structure. The results implicate acetylation as a critical regulator that guides the selective aggregation of three-repeat tau and the development of tau isoform-specific neurodegenerative diseases.
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000264175 650_2 $$2MeSH$$aHumans
000264175 650_2 $$2MeSH$$a14-3-3 Proteins
000264175 650_2 $$2MeSH$$aAcetylation
000264175 650_2 $$2MeSH$$aAlzheimer Disease
000264175 650_2 $$2MeSH$$atau Proteins
000264175 650_2 $$2MeSH$$aTauopathies
000264175 650_7 $$2NLM Chemicals$$a14-3-3 Proteins
000264175 650_7 $$2NLM Chemicals$$atau Proteins
000264175 650_7 $$2NLM Chemicals$$aMAPT protein, human
000264175 7001_ $$0P:(DE-2719)9000723$$aRivière, Gwladys$$b1$$udzne
000264175 7001_ $$0P:(DE-2719)9001960$$aHebestreit, Alina$$b2$$udzne
000264175 7001_ $$0P:(DE-2719)2812657$$ade Opakua, Alain Ibáñez$$b3
000264175 7001_ $$0P:(DE-2719)2481765$$aVorberg, Ina M$$b4
000264175 7001_ $$aAndreas, Loren B$$b5
000264175 7001_ $$0P:(DE-2719)2810591$$aZweckstetter, Markus$$b6$$eLast author
000264175 773__ $$0PERI:(DE-600)2553671-0$$a10.1038/s41467-023-41672-1$$gVol. 14, no. 1, p. 5919$$n1$$p5919$$tNature Communications$$v14$$x2041-1723$$y2023
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