Evidence map›Paper›PMID 36528685›Full record

ArticleScientific reports2022

A conserved MTMR lipid phosphatase increasingly suppresses autophagy in brain neurons during aging.

Tibor Kovács, Janka Szinyákovics, Viktor Billes, Gábor Murányi, Virginia B Varga, Annamária Bjelik, Ádám Légrádi, Melinda Szabó, Sára Sándor, Enikő Kubinyi and 10 more

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
2.3field-weighted citation impact, top 11% 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

9 citing papers in PubMed, 16 citations in OpenAlex.

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  9. The Small-Molecule Enhancers of Autophagy AUTEN-67 and -99 Delay Ageing inInternational journal of molecular sciences · 2023
    Article
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

20 authors at 7 institutions in 3 countries.

Tibor Kovács *Department of Genetics, ELTE Eötvös Loránd University, Pázmány Péter Stny. 1/C, Budapest, 1117, Hungary.
Janka Szinyákovics *Department of Genetics, ELTE Eötvös Loránd University, Pázmány Péter Stny. 1/C, Budapest, 1117, Hungary.
Viktor BillesDepartment of Genetics, ELTE Eötvös Loránd University, Pázmány Péter Stny. 1/C, Budapest, 1117, Hungary.
Gábor MurányiDepartment of Genetics, ELTE Eötvös Loránd University, Pázmány Péter Stny. 1/C, Budapest, 1117, Hungary.
Virginia B VargaDepartment of Genetics, ELTE Eötvös Loránd University, Pázmány Péter Stny. 1/C, Budapest, 1117, Hungary.
Annamária BjelikDepartment of Cell Biology and Molecular Medicine, University of Szeged, Szeged, 6720, Hungary.
Ádám LégrádiDepartment of Cell Biology and Molecular Medicine, University of Szeged, Szeged, 6720, Hungary.
Melinda SzabóDepartment of Cell Biology and Molecular Medicine, University of Szeged, Szeged, 6720, Hungary.
Sára SándorDepartment of Ethology, ELTE Eötvös Loránd University, Budapest, 1117, Hungary.
Enikő KubinyiDepartment of Ethology, ELTE Eötvös Loránd University, Budapest, 1117, Hungary.
Cecília Szekeres-ParackyHuman Brain Research Laboratory, Institute of Experimental Medicine, ELKH, Budapest, 1085, Hungary.
Péter SzocsicsHuman Brain Research Laboratory, Institute of Experimental Medicine, ELKH, Budapest, 1085, Hungary.
János LőkeDepartment of Psychiatry, Saint Borbala Hospital, Tatabánya, 2800, Hungary.
Jun MulderScience for Life Laboratory, Department of Neuroscience, Karolinska Institute, 171 77, Stockholm, Sweden.
Balázs GulyásLee Kong Chian School of Medicine, Nanyang Technological University, Singapore, 636921, Singapore.
Éva RennerHuman Brain Tissue Bank and Laboratory, Semmelweis University, Budapest, 1085, Hungary.
Miklós PalkovitsHuman Brain Tissue Bank and Laboratory, Semmelweis University, Budapest, 1085, Hungary.
Károly GulyaDepartment of Cell Biology and Molecular Medicine, University of Szeged, Szeged, 6720, Hungary. gulyak@bio.u-szeged.hu.
Zsófia MaglóczkyHuman Brain Research Laboratory, Institute of Experimental Medicine, ELKH, Budapest, 1085, Hungary. magloczky.zsofia@koki.mta.hu.
Tibor VellaiDepartment of Genetics, ELTE Eötvös Loránd University, Pázmány Péter Stny. 1/C, Budapest, 1117, Hungary. vellai@falco.elte.hu.
Eötvös Loránd University · HUUniversity of Szeged · HUSemmelweis University · HUHUN-REN Institute of Experimental Medicine · HUKarolinska Institutet · SENanyang Technological University · SGSzent Borbála Kórház · HU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Ageing is driven by the progressive, lifelong accumulation of cellular damage. Autophagy (cellular self-eating) functions as a major cell clearance mechanism to degrade such damages, and its capacity declines with age. Despite its physiological and medical significance, it remains largely unknown why autophagy becomes incapable of effectively eliminating harmful cellular materials in many cells at advanced ages. Here we show that age-associated defects in autophagic degradation occur at both the early and late stages of the process. Furthermore, in the fruit fly Drosophila melanogaster, the myotubularin-related (MTMR) lipid phosphatase egg-derived tyrosine phosphatase (EDTP) known as an autophagy repressor gradually accumulates in brain neurons during the adult lifespan. The age-related increase in EDTP activity is associated with a growing DNA N6-adenine methylation at EDTP locus. MTMR14, the human counterpart of EDTP, also tends to accumulate with age in brain neurons. Thus, EDTP, and presumably MTMR14, promotes brain ageing by increasingly suppressing autophagy throughout adulthood. We propose that EDTP and MTMR14 phosphatases operate as endogenous pro-ageing factors setting the rate at which neurons age largely independently of environmental factors, and that autophagy is influenced by DNA N6-methyladenine levels in insects.

Indexed as

Drosophila melanogasterDrosophila ProteinsAdultAgingAnimalsAutophagyBrainDrosophilaHumansLipidsNeuronsProtein Tyrosine PhosphatasesProtein Tyrosine Phosphatases, Non-ReceptorDrosophila ProteinsEDTP protein, DrosophilaLipidsmyotubularinProtein Tyrosine PhosphatasesProtein Tyrosine Phosphatases, Non-Receptor

Identifiers

PMID36528685
PMCPMC9759524
OpenAlexW4311715238

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LicenceCC BY
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Registered trials

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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.