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p(HGNC:MAPT, pmod(Ac))

Equivalencies: 0 | Classes: 0 | Children: 11 | Explore

Entity

Name
MAPT
Namespace
hgnc
Namespace Version
20180906
Namespace URL
https://raw.githubusercontent.com/pharmacome/terminology/b46b65c3da259b6e86026514dfececab7c22a11b/external/hgnc-names.belns

Appears in Networks 2

Tau clearance mechanisms and their possible role in the pathogenesis of Alzheimer disease v1.0.0

Tau Modifications v1.9.5

Tau Modifications Sections of NESTOR

In-Edges 21

p(HGNC:MAPT) hasVariant p(HGNC:MAPT, pmod(Ac)) View Subject | View Object

Appears in Networks:

path(MESH:"Neurofibrillary Tangles") association p(HGNC:MAPT, pmod(Ac)) View Subject | View Object

The predominant post-translational modification of tau in the NFTs is phosphorylation; however numerous modifications have been noted including truncation, acetylation, nitration, and several others (2–4). PubMed:24027553

Appears in Networks:
Annotations
Text Location
Review

a(CHEBI:"methylene blue") decreases p(HGNC:MAPT, pmod(Ac)) View Subject | View Object

Thus, K → Q substitutions within the critical PHF6* motif, in the apparent absence of other tau PTMs, appears sufficient to accelerate tau aggregation in vitro. PubMed:28287136

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a(CHEBI:"trichostatin A") increases p(HGNC:MAPT, pmod(Ac)) View Subject | View Object

Although low-level tau acetylation was observed in untreated HEK-T40 cells, treatment with the pan histone deacetylase (HDAC) inhibitor trichostatin A (TSA), but not the Sir2 class inhibitor nicotinamide, resulted in a dramatic increase in acetylated tau levels. PubMed:21427723

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a(HBP:"cystein-dependent auto-acetylation") increases p(HGNC:MAPT, pmod(Ac)) View Subject | View Object

Similar to tau, MAP2 acetylation can occur in a cysteine-dependent auto-regulatory manner in the presence of acetyl-CoA. Tubulin reduced MAP2 acetylation, suggesting tubulin binding dictates MAP acetylation status. PubMed:28002468

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a(HBP:C646) decreases p(HGNC:MAPT, pmod(Ac)) View Subject | View Object

Next, we treated primary neurons with C646, a pyrazolone-containing small-molecule inhibitor of p300 with a Ki of 400 nM (Bowers et al., 2010). Under cell-free conditions, C646 at 10 μM inhibits p300 in a highly selective manner (86% inhibition vs. <10% for the six other acetyltransferases) (Bowers et al., 2010). Inhibition of p300 with C646 (20 μM) drastically reduced levels of ac-tau in primary neurons within 8 h. PubMed:20869593

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p(HGNC:MAPT, pmod(Ac, Lys, 280)) isA p(HGNC:MAPT, pmod(Ac)) View Subject | View Object

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p(HGNC:MAPT, pmod(Ac, Lys, 163)) isA p(HGNC:MAPT, pmod(Ac)) View Subject | View Object

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p(HGNC:MAPT, pmod(Ac, Lys, 369)) isA p(HGNC:MAPT, pmod(Ac)) View Subject | View Object

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act(p(FPLX:HDAC)) decreases p(HGNC:MAPT, pmod(Ac)) View Subject | View Object

Although low-level tau acetylation was observed in untreated HEK-T40 cells, treatment with the pan histone deacetylase (HDAC) inhibitor trichostatin A (TSA), but not the Sir2 class inhibitor nicotinamide, resulted in a dramatic increase in acetylated tau levels. PubMed:21427723

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p(HBP:"Tau epitope, AT8") positiveCorrelation p(HGNC:MAPT, pmod(Ac)) View Subject | View Object

Thus, the increase in ac-tau induced by SIRT1 deficiency is accompanied by accumulation of pathogenic p-tau in primary neurons. In mouse brains, deleting SIRT1, which elevated ac-tau, also increased AT8-positive p-tau. PubMed:20869593

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p(HGNC:MAPT, pmod(Ac, Lys, 225)) isA p(HGNC:MAPT, pmod(Ac)) View Subject | View Object

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p(HGNC:MAPT, pmod(Ac, Lys, 259)) isA p(HGNC:MAPT, pmod(Ac)) View Subject | View Object

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p(HGNC:MAPT, pmod(Ac, Lys, 317)) isA p(HGNC:MAPT, pmod(Ac)) View Subject | View Object

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p(HGNC:MAPT, pmod(Ac, Lys, 321)) isA p(HGNC:MAPT, pmod(Ac)) View Subject | View Object

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p(HGNC:MAPT, pmod(Ac, Lys, 331)) isA p(HGNC:MAPT, pmod(Ac)) View Subject | View Object

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p(HGNC:MAPT, pmod(Ac, Lys, 343)) isA p(HGNC:MAPT, pmod(Ac)) View Subject | View Object

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p(HGNC:MAPT, pmod(Ac, Lys, 347)) isA p(HGNC:MAPT, pmod(Ac)) View Subject | View Object

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p(HGNC:MAPT, pmod(Ac, Lys, 385)) isA p(HGNC:MAPT, pmod(Ac)) View Subject | View Object

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act(p(HGNC:SIRT1)) negativeCorrelation p(HGNC:MAPT, pmod(Ac)) View Subject | View Object

Thus, the increase in ac-tau induced by SIRT1 deficiency is accompanied by accumulation of pathogenic p-tau in primary neurons. In mouse brains, deleting SIRT1, which elevated ac-tau, also increased AT8-positive p-tau. PubMed:20869593

Appears in Networks:

p(MGI:Sirt3) negativeCorrelation p(HGNC:MAPT, pmod(Ac)) View Subject | View Object

After pretreating hTau neurons with oligo Aβ-42 (1000 ng/ml), Sirt3 levels were reduced (Fig. 6b and e). This reduction in Sirt3 was translated into an increase in total tau and Ac-tau. PubMed:29540553

Appears in Networks:

Out-Edges 5

p(HGNC:MAPT, pmod(Ac)) association path(MESH:"Neurofibrillary Tangles") View Subject | View Object

The predominant post-translational modification of tau in the NFTs is phosphorylation; however numerous modifications have been noted including truncation, acetylation, nitration, and several others (2–4). PubMed:24027553

Appears in Networks:
Annotations
Text Location
Review

p(HGNC:MAPT, pmod(Ac)) negativeCorrelation p(MGI:Sirt3) View Subject | View Object

After pretreating hTau neurons with oligo Aβ-42 (1000 ng/ml), Sirt3 levels were reduced (Fig. 6b and e). This reduction in Sirt3 was translated into an increase in total tau and Ac-tau. PubMed:29540553

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p(HGNC:MAPT, pmod(Ac)) decreases p(HGNC:WWC1) View Subject | View Object

Here we report abnormal acetylation of K274 and K281 on tau, identified in AD brains, promotes memory loss and disrupts synaptic plasticity by reducing postsynaptic KIdney/BRAin (KIBRA) protein, a memory-associated protein.Transgenic mice expressing human tau with lysine-to-glutamine mutations to mimic K274 and K281 acetylation (tauKQ) exhibit AD-related memory deficits and impaired hippocampal long-term potentiation (LTP). TauKQ reduces synaptic KIBRA levels and disrupts activity-induced postsynaptic actin remodeling and AMPA receptor insertion. The LTP deficit was rescued by promoting actin polymerization or by KIBRA expression. In AD patients with dementia, we found enhanced tau acetylation is linked to loss of KIBRA. PubMed:27041503

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p(HGNC:MAPT, pmod(Ac)) negativeCorrelation act(p(HGNC:SIRT1)) View Subject | View Object

Thus, the increase in ac-tau induced by SIRT1 deficiency is accompanied by accumulation of pathogenic p-tau in primary neurons. In mouse brains, deleting SIRT1, which elevated ac-tau, also increased AT8-positive p-tau. PubMed:20869593

Appears in Networks:

p(HGNC:MAPT, pmod(Ac)) positiveCorrelation p(HBP:"Tau epitope, AT8") View Subject | View Object

Thus, the increase in ac-tau induced by SIRT1 deficiency is accompanied by accumulation of pathogenic p-tau in primary neurons. In mouse brains, deleting SIRT1, which elevated ac-tau, also increased AT8-positive p-tau. PubMed:20869593

Appears in Networks:

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If you find BEL Commons useful in your work, please consider citing: Hoyt, C. T., Domingo-Fernández, D., & Hofmann-Apitius, M. (2018). BEL Commons: an environment for exploration and analysis of networks encoded in Biological Expression Language. Database, 2018(3), 1–11.