Acetylation of Tau Inhibits Its Degradation and Contributes to Tauopathy

Min, Sang-Won; Cho, Seo Hyun; Zhou, Yungui; Schroeder, Sebastian; Haroutunian, Vahram; Seeley, William W.; Huang, Eric J.; Shen, Yong; Masliah, Eliezer; Mukherjee, Chandrani; Meyers, David J.; Cole, Philip A.; Ott, Melanie; Gan, Li

doi:10.1016/j.neuron.2010.11.013

Cited by 19 publications

(23 citation statements)

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“…The non-histone substrates of SIRT1 include, but are not limited to, tumor suppressor P53, nuclear factor-kB (NF-kB), peroxisome proliferator-activated receptor gamma coactivator-1alpha (PGC-1a), fork-head box protein O (FOXO) transcription factors, liver X receptor (LXR), PARP, Ku70, and hypoxia-inducible factor (HIF)-1a, making SIRT1 a promising candidate for targeted therapies to halt disease progression. A recent study by Min et al showed that SIRT1 transgenic Alzheimer's disease mice were protected from memory loss [13]. Other work indicates that SIRT1 has tumor suppression activity in cancer [14].…”

Section: Introductionmentioning

confidence: 99%

SIRT1 activator ameliorates the renal tubular injury induced by hyperglycemia in vivo and in vitro via inhibiting apoptosis

Wang

Zhao

et al. 2016

Biomedicine & Pharmacotherapy

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Section: Introductionmentioning

confidence: 99%

SIRT1 activator ameliorates the renal tubular injury induced by hyperglycemia in vivo and in vitro via inhibiting apoptosis

Wang

Zhao

et al. 2016

Biomedicine & Pharmacotherapy

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“…Studies related to neurodegeneration strongly suggest that intracellular increase of p-tau is cytotoxic to neurons (reviewed in [70,77]). Recently, it has been reported that in AD brain p-tau is hyperacetylated due to deficiency of SIRT1 [78]. That modification was reported to impair p-tau degradation by the 26S proteasome [78].…”

Section: Phosphorylated Taumentioning

confidence: 99%

Sporadic inclusion-body myositis: A degenerative muscle disease associated with aging, impaired muscle protein homeostasis and abnormal mitophagy

Askanas

Engel

Nogalska

2015

Biochimica et Biophysica Acta (BBA) - Molecular Basis of Diseas

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Sporadic inclusion-body myositis (s-IBM) is the most common degenerative muscle disease in which aging appears to be a key risk factor. In this review we focus on several cellular molecular mechanisms responsible for multiprotein aggregation and accumulations within s-IBM muscle fibers, and their possible consequences. Those include mechanisms leading to: a) accumulation in the form of aggregates within the muscle fibers, of several proteins, including amyloid-β42 and its oligomers, and phosphorylated tau in the form of paired helical filaments, and we consider their putative detrimental influence; and b) protein misfolding and aggregation, including evidence of abnormal myoproteostasis, such as increased protein transcription, inadequate protein disposal, and abnormal posttranslational modifications of proteins. Pathogenic importance of our recently demonstrated abnormal mitophagy is also discussed. The intriguing phenotypic similarities between s-IBM muscle fibers and the brains of Alzheimer and Parkinson's disease patients, the two most common neurodegenerative diseases associated with aging, are also discussed. This article is part of a Special Issue entitled: Neuromuscular Diseases: Pathology and Molecular Pathogenesis.

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“…1). Some post-translational modifications such as glycosylation, O-GlcNAcylation, acetylation and abnormal truncations [120][121][122][123] will not be covered in details here. This is not meant to imply that these aspects of tau modifications are unimportant.…”

Section: Animal Models Of Tauopathiesmentioning

confidence: 99%

Behind the curtain of tauopathy: a show of multiple players orchestrating tau toxicity

Huang

Zhou

2015

Cell. Mol. Life Sci.

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tau, a microtubule-associated protein, directly binds with microtubules to dynamically regulate the organization of cellular cytoskeletons, and is especially abundant in neurons of the central nervous system. Under disease conditions such as Pick's disease, progressive supranuclear palsy, frontotemporal dementia, parkinsonism linked to chromosome 17 and Alzheimer's disease, tau proteins can self-assemble to paired helical filaments progressing to neurofibrillary tangles. In these diseases, collectively referred to as "tauopathies", alterations of diverse tau modifications including phosphorylation, metal ion binding, glycosylation, as well as structural changes of tau proteins have all been observed, indicating the complexity and variability of factors in the regulation of tau toxicity. Here, we review our current knowledge and hypotheses from relevant studies on tau toxicity, emphasizing the roles of phosphorylations, metal ions, folding and clearance control underlining tau etiology and their regulations. A summary of clinical efforts and associated findings of drug candidates under development is also presented. It is hoped that a more comprehensive understanding of tau regulation will provide us with a better blueprint of tau networking in neuronal cells and offer hints for the design of more efficient strategies to tackle tau-related diseases in the future.

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Acetylation of Tau Inhibits Its Degradation and Contributes to Tauopathy

Cited by 19 publications

References 0 publications

SIRT1 activator ameliorates the renal tubular injury induced by hyperglycemia in vivo and in vitro via inhibiting apoptosis

SIRT1 activator ameliorates the renal tubular injury induced by hyperglycemia in vivo and in vitro via inhibiting apoptosis

Sporadic inclusion-body myositis: A degenerative muscle disease associated with aging, impaired muscle protein homeostasis and abnormal mitophagy

Behind the curtain of tauopathy: a show of multiple players orchestrating tau toxicity

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