Evidence map›Paper›PMID 29062069›Full record

ArticleScientific reports2017

Resveratrol induces dephosphorylation of Tau by interfering with the MID1-PP2A complex.

Susann Schweiger, Frank Matthes, Karen Posey, Eva Kickstein, Stephanie Weber, Moritz M Hettich, Sandra Pfurtscheller, Dan Ehninger, Rainer Schneider, Sybille Krauß

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
52citing papers in PubMed, 1 pooled it
6.0field-weighted citation impact, top 3% 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

52 citing papers in PubMed, 1 synthesis or guideline pooled it, 89 citations in OpenAlex.

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  20. Role of Tau protein in long COVID and potential therapeutic targets.Frontiers in cellular and infection microbiology · 2023
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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

10 authors at 5 institutions in 3 countries.

Susann SchweigerInstitute for Human Genetics, University of Mainz, Langenbeckstr. 1, 55131, Mainz, Germany. susann.schweiger@unimedizin-mainz.de.
Frank MatthesGerman Center for Neurodegenerative Diseases (DZNE), Sigmund-Freud-Str.27, 53127, Bonn, Germany.
Karen PoseyMcGovern Medical School at University of Texas in Houston, Department of Pediatrics, 6431 Fannin Street, Houston, Texas, 77030, USA.
Eva KicksteinMax-Planck Institute for Molecular Genetics, Department of Human Molecular Genetics, Ihnestr. 73, 14195, Berlin, Germany.
Stephanie WeberGerman Center for Neurodegenerative Diseases (DZNE), Sigmund-Freud-Str.27, 53127, Bonn, Germany.
Moritz M HettichGerman Center for Neurodegenerative Diseases (DZNE), Sigmund-Freud-Str.27, 53127, Bonn, Germany.
Sandra PfurtschellerInstitute of Biochemistry and Center for Molecular Biosciences Innsbruck (CMBI), Innrain 80/82, 6020, Innsbruck, Austria.
Dan EhningerGerman Center for Neurodegenerative Diseases (DZNE), Sigmund-Freud-Str.27, 53127, Bonn, Germany.
Rainer SchneiderInstitute of Biochemistry and Center for Molecular Biosciences Innsbruck (CMBI), Innrain 80/82, 6020, Innsbruck, Austria.
Sybille KraußGerman Center for Neurodegenerative Diseases (DZNE), Sigmund-Freud-Str.27, 53127, Bonn, Germany. sybille.krauss@dzne.de.
German Center for Neurodegenerative Diseases · DEUniversität Innsbruck · ATJohannes Gutenberg University Mainz · DEMax Planck Institute for Molecular Genetics · DEThe University of Texas Health Science Center at Houston · US

Funding

Consequences of Mutant COMP Expression and Therapeutic Approaches in Transgenic MiceR01AR057117 · NIAMS · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI HECHT, JACQUELINE T, POSEY, KAREN LASHEA · 2010 to 2020
$4.2M
NIAMS NIH HHS R01 AR057117
6 · The paper itself

Abstract

The formation of paired helical filaments (PHF), which are composed of hyperphosphorylated Tau protein dissociating from microtubules, is one of the pathological hallmarks of Alzheimer's disease (AD) and other tauopathies. The most important phosphatase that is capable of dephosphorylating Tau at AD specific phospho-sites is protein phosphatase 2 A (PP2A). Here we show that resveratrol, a polyphenol, significantly induces PP2A activity and reduces Tau phosphorylation at PP2A-dependent epitopes. The increase in PP2A activity is caused by decreased expression of the MID1 ubiquitin ligase that mediates ubiquitin-specific modification and degradation of the catalytic subunit of PP2A when bound to microtubules. Interestingly, we further show that MID1 expression is elevated in AD tissue. Our data suggest a key role of MID1 in the pathology of AD and related tauopathies. Together with previous studies showing that resveratrol reduces β-amyloid toxicity they also give evidence of a promising role for resveratrol in the prophylaxis and therapy of AD.

Indexed as

Alzheimer DiseaseAnimalsAnti-Inflammatory Agents, Non-SteroidalCells, CulturedEmbryo, MammalianFibroblastsHEK293 CellsHumansMiceMicrotubule ProteinsMicrotubulesNeurofibrillary TanglesNeuronsNuclear ProteinsPhosphorylationProtein Interaction MapsAnti-Inflammatory Agents, Non-SteroidalMicrotubule ProteinsMID1 protein, humanMid1 protein, mouseNuclear ProteinsProtein Phosphatase 2ProteinsResveratroltau ProteinsTranscription FactorsUbiquitin-Protein Ligases

Identifiers

PMID29062069
PMCPMC5653760
OpenAlexW2765816988

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.