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Article

An acetylation-phosphorylation switch that regulates tau aggregation propensity and function.

The Journal of biological chemistry - 15 Sept 2017

Carlomagno Yari, Chung Dah-Eun Chloe, Yue Mei, Castanedes-Casey Monica, Madden Benjamin J, Dunmore Judy, Tong Jimei, DeTure Michael, Dickson Dennis W, Petrucelli Leonard, Cook Casey

Abstract excerpt

The aberrant accumulation of tau protein is a pathological hallmark of a class of neurodegenerative diseases known as tauopathies, including Alzheimer's disease and related dementias. On the basis of previous observations that tau is a direct substrate of histone deacetylase 6 (HDAC6), we sought to map all HDAC6-responsive sites in tau and determine how acetylation in a site-specific manner affects tau's...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

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Identifiers

PMID: 28760828
DOI: 10.1074/jbc.M117.794602
PMCID: PMC5602388

Genes

HDAC6

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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