Acetylation of tau inhibits its degradation and contributes to tauopathy.

By Sang-Won Min, Seo-hyun Cho, Yungui Zhou, S. Schroeder, V. Haroutunian, William W. Seeley, E. Huang, Yong Shen, E. Masliah, Chandrani Mukherjee and 4 more. Neuron, 2010

725 citations recorded by the source corpus.

Subfields: Geriatrics and Gerontology, Molecular Biology, Physiology

View Paper: https://www.semanticscholar.org/paper/73aba8a38cf2c6402dfd457a20c4bb9f462d577f

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Geriatrics and Gerontology

1. T. Arnesen
2. Rasmus Ree
3. Adrian Drazic
4. Line M. Myklebust

In Molecular Biology

1. John Q. Trojanowski
2. V. Lee
3. E. Mandelkow
4. L. Mucke

In Physiology

1. E. Mandelkow
2. V. Lee
3. Jing L Guo
4. John Q. Trojanowski
5. L. Mucke
6. Huaxi Xu
7. D. Selkoe
8. D. Holtzman

Citations in the corpus

• Alzheimer Disease: An Update on Pathobiology and Treatment Strategies (2019, neutral): “Tau acetylation has been shown to reduce degradation of phosphorylated tau and increase tau pathology (Min et al., 2010) but has also been shown to inhibit tau phosphorylation at certain residues and limit further aggregation (Cook et al.”
• Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease (2020, background): “Acetylation may affect other PTMs in tau: since both acetylation and ubiquitination are modifications on Lys residues, acetylation may decrease proteasome-mediated tau degradation by competitively attenuating tau ubiquitination [153, 161].”
• The Many Faces of Tau (2011, background): “In AD brains, tau is hyperacetylated, which should increase its half-life (Min et al., 2010), alter its microtubule binding and enhance aggregation (Cohen et al., 2011).”
• The world of protein acetylation. (2016, background): “Tau is also acetylated by p300, and deacetylated by SIRT1 [443].”
• The acetylation of tau inhibits its function and promotes pathological tau aggregation (2011, background): “Notably, reversible lysine acetylation has emerged as a potential regulatory modification implicated in AD and other neurodegenerative disorders, and a recent study demonstrated that tau is modified by lysine acetylatio”
• Biochemistry and cell biology of tau protein in neurofibrillary degeneration. (2012, background): “Acetylation of lysines affects predominantly K280, impairs MT binding of Tau, promotes aggregation and potentially interferes with ubiquitination and thus degradation of Tau (Cohen et al. 2011; Min et al. 2010).”