Evidence map›Paper›PMID 30531974›Full record

ArticleScientific reports2018

Phosphorylation of nuclear Tau is modulated by distinct cellular pathways.

Giorgio Ulrich, Agnese Salvadè, Paul Boersema, Tito Calì, Chiara Foglieni, Martina Sola, Paola Picotti, Stéphanie Papin, Paolo Paganetti

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
2.6field-weighted citation impact, top 10% 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

32 citing papers in PubMed, 54 citations in OpenAlex.

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  8. Cellular and pathological functions of tau.Nature reviews. Molecular cell biology · 2024
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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

9 authors at 3 institutions in 2 countries.

Giorgio UlrichLaboratory for Biomedical Neurosciences, Neurocenter of Southern Switzerland, Ente Cantonale Ospedaliero, Torricella-Taverne, Switzerland.
Agnese SalvadèLaboratory for Biomedical Neurosciences, Neurocenter of Southern Switzerland, Ente Cantonale Ospedaliero, Torricella-Taverne, Switzerland.
Paul BoersemaInstitute of Molecular Systems Biology, Department of Biology, ETHZ, Zurich, Switzerland.
Tito CalìDepartment of Biomedical Sciences and Padova Neuroscience Center, University of Padova, Padova, Italy.ORCID http://orcid.org/0000-0002-8901-1659
Chiara FoglieniLaboratory for Biomedical Neurosciences, Neurocenter of Southern Switzerland, Ente Cantonale Ospedaliero, Torricella-Taverne, Switzerland.
Martina SolaLaboratory for Biomedical Neurosciences, Neurocenter of Southern Switzerland, Ente Cantonale Ospedaliero, Torricella-Taverne, Switzerland.
Paola PicottiInstitute of Molecular Systems Biology, Department of Biology, ETHZ, Zurich, Switzerland.
Stéphanie PapinLaboratory for Biomedical Neurosciences, Neurocenter of Southern Switzerland, Ente Cantonale Ospedaliero, Torricella-Taverne, Switzerland.
Paolo PaganettiLaboratory for Biomedical Neurosciences, Neurocenter of Southern Switzerland, Ente Cantonale Ospedaliero, Torricella-Taverne, Switzerland. paolo.paganetti@eoc.ch.ORCID http://orcid.org/0000-0003-1896-6324
Laboratory for Biomedical Neurosciences · CHETH Zurich · CHUniversity of Padua · IT

Funding

Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung (Swiss National Science Foundation) 31003A
6 · The paper itself

Abstract

Post-translational protein modification controls the function of Tau as a scaffold protein linking a variety of molecular partners. This is most studied in the context of microtubules, where Tau regulates their stability as well as the distribution of cellular components to defined compartments. However, Tau is also located in the cell nucleus; and is found to protect DNA. Quantitative assessment of Tau modification in the nucleus when compared to the cytosol may elucidate how subcellular distribution and function of Tau is regulated. We undertook an unbiased approach by combing bimolecular fluorescent complementation and mass spectrometry in order to show that Tau phosphorylation at specific residues is increased in the nucleus of proliferating pluripotent neuronal C17.2 and neuroblastoma SY5Y cells. These findings were validated with the use of nuclear targeted Tau and subcellular fractionation, in particular for the phosphorylation at T

Indexed as

Amino Acid SequenceAnimalsCell LineCell Line, TumorCell NucleusCell ProliferationCytosolHumansMiceNeuroblastomaNeurodegenerative DiseasesNeuronsPhosphorylationProtein Processing, Post-Translationaltau Proteinstau Proteins

Identifiers

PMID30531974
PMCPMC6286375
OpenAlexW2903165712

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.