Evidence map›Paper›PMID 30243024›Full record

ArticleAging2018

Sirt1 enhances tau exon 10 inclusion and improves spatial memory of Htau mice.

Shuo Qian, Jianlan Gu, Wufei Dai, Nana Jin, Dandan Chu, Qin Huang, Fei Liu, Wei Qian

Open access · greenAbstract read
In one paragraph

Article in Aging, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.5field-weighted citation impact, top 19% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

13 citing papers in PubMed, 16 citations in OpenAlex.

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  12. Updates on the epigenetic roles of sirtuins.Current opinion in chemical biology · 2019
    Review
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors at 2 institutions in 2 countries.

Shuo Qian *Department of Biochemistry and Molecular Biology, Medical School, Nantong University, Nantong, Jiangsu 226001, P. R. China.
Jianlan Gu *Department of Biochemistry and Molecular Biology, Medical School, Nantong University, Nantong, Jiangsu 226001, P. R. China.
Wufei DaiDepartment of Biochemistry and Molecular Biology, Medical School, Nantong University, Nantong, Jiangsu 226001, P. R. China.
Nana JinJiangsu Key Laboratory of Neuroregeneration of Jiangsu and Ministry of Education of China, Co-innovation Center of Neuroregeneration, Nantong University, Nantong, Jiangsu 226001, P. R. China.
Dandan ChuJiangsu Key Laboratory of Neuroregeneration of Jiangsu and Ministry of Education of China, Co-innovation Center of Neuroregeneration, Nantong University, Nantong, Jiangsu 226001, P. R. China.
Qin HuangJiangsu Key Laboratory of Neuroregeneration of Jiangsu and Ministry of Education of China, Co-innovation Center of Neuroregeneration, Nantong University, Nantong, Jiangsu 226001, P. R. China.
Fei LiuDepartment of Neurochemistry, Inge Grundke-Iqbal Research Floor, New York State Institute for Basic Research in Developmental Disabilities, Staten Island, NY 10314, USA.
Wei QianDepartment of Biochemistry and Molecular Biology, Medical School, Nantong University, Nantong, Jiangsu 226001, P. R. China.
Nantong University · CNNew York State Office for People With Developmental Disabilities · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Alternative splicing of tau exon 10 generates tau isoforms with three or four microtubule binding repeats, named 3R-tau and 4R-tau, respectively. Dysregulation of tau exon 10 splicing could cause neurofibrillary degeneration. Acetylation is one of the major post-translational protein modifications in the cell by attachment of the acetyl group to either the α-amino group of the N-terminus of proteins or to the ε-amino group of lysine residues. Sirt1, one member in mammalian Sirtuin family, deacetylates protein and is associated closely with age-related diseases including Alzheimer's disease. However, the role of Sirt1 in tau exon 10 splicing remains elusive. In the present study, we determined the role of Sirt1 in tau exon 10 splicing. We found that activation of Sirt1 by resveratrol enhanced tau exon 10 inclusion, leading to 4R-tau expression. Sirt1 interacted with splicing factor 9G8, deacetylated it at Lys24, and suppressed its function in promoting tau exon 10 exclusion. Moreover, resveratrol improved learning and spatial memory in Htau mice. These findings suggest that Sirt1 may serve as a new drug target for Alzheimer's Disease related tauopathies and resveratrol may be used to correct dysregulated tau exon 10 with 3R-tau > 4R-tau.

Indexed as

Spatial MemoryAcetylationAlternative SplicingAlzheimer DiseaseAnimalsExonsHEK293 CellsHeLa CellsHumansMiceResveratrolSirtuin 1tau ProteinsResveratrolSirt1 protein, mouseSirtuin 1tau Proteins9G8Alzheimer’s diseaseresveratrolSirt1tau exon 10 splicing

Identifiers

PMID30243024
PMCPMC6188499
OpenAlexW2894276058

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.