Evidence map›Paper›PMID 28613034›Full record

ArticleAging cell2017

TORC1-mediated sensing of chaperone activity alters glucose metabolism and extends lifespan.

Matea Perić, Anita Lovrić, Ana Šarić, Marina Musa, Peter Bou Dib, Marina Rudan, Andrea Nikolić, Sandra Sobočanec, Ana-Matea Mikecin, Sven Dennerlein and 4 more

Open access · goldAbstract read
In one paragraph

Article in Aging cell, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.7field-weighted citation impact, top 18% 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

16 citing papers in PubMed, 25 citations in OpenAlex.

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  12. Editorial: Mitochondrial Communication in Physiology, Disease and Aging.Frontiers in cell and developmental biology · 2019
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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

14 authors at 5 institutions in 2 countries.

Matea PerićMediterranean Institute for Life Sciences, Mestrovicevo setaliste 45, 21000, Split, Croatia.
Anita LovrićMediterranean Institute for Life Sciences, Mestrovicevo setaliste 45, 21000, Split, Croatia.
Ana ŠarićDivision of Molecular Medicine, Rudjer Boskovic Institute, Bijenicka 54, 10000, Zagreb, Croatia.
Marina MusaMediterranean Institute for Life Sciences, Mestrovicevo setaliste 45, 21000, Split, Croatia.
Peter Bou DibInstitut für Zellbiochemie, Universitätsmedizin Göttingen, Humboldtallee 23, D-37073, Göttingen, Germany.
Marina RudanMediterranean Institute for Life Sciences, Mestrovicevo setaliste 45, 21000, Split, Croatia.
Andrea NikolićMediterranean Institute for Life Sciences, Mestrovicevo setaliste 45, 21000, Split, Croatia.
Sandra SobočanecDivision of Molecular Medicine, Rudjer Boskovic Institute, Bijenicka 54, 10000, Zagreb, Croatia.
Ana-Matea MikecinDivision of Molecular Medicine, Rudjer Boskovic Institute, Bijenicka 54, 10000, Zagreb, Croatia.
Sven DennerleinInstitut für Zellbiochemie, Universitätsmedizin Göttingen, Humboldtallee 23, D-37073, Göttingen, Germany.
Ira MiloševićEuropean Neuroscience Institute, Grisebachstraße 5, 37077, Göttingen, Germany.
Kristian VlahovičekBioinformatics Group, Division of Biology, Department of Molecular Biology, Faculty of Science, University of Zagreb, Zagreb, Croatia.
Nuno RaimundoInstitut für Zellbiochemie, Universitätsmedizin Göttingen, Humboldtallee 23, D-37073, Göttingen, Germany.
Anita KriškoMediterranean Institute for Life Sciences, Mestrovicevo setaliste 45, 21000, Split, Croatia.
Mediterranean Institute for Life Sciences · HRRudjer Boskovic Institute · HRUniversitätsmedizin Göttingen · DEEuropean Neuroscience Institute Göttingen · DEUniversity of Zagreb · HR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein quality control mechanisms, required for normal cellular functioning, encompass multiple functions related to protein production and maintenance. However, the existence of communication between proteostasis and metabolic networks and its underlying mechanisms remain elusive. Here, we report that enhanced chaperone activity and consequent improved proteostasis are sensed by TORC1 via the activity of Hsp82. Chaperone enrichment decreases the level of Hsp82, which deactivates TORC1 and leads to activation of Snf1/AMPK, regardless of glucose availability. This mechanism culminates in the extension of yeast replicative lifespan (RLS) that is fully reliant on both TORC1 deactivation and Snf1/AMPK activation. Specifically, we identify oxygen consumption increase as the downstream effect of Snf1 activation responsible for the entire RLS extension. Our results set a novel paradigm for the role of proteostasis in aging: modulation of the misfolded protein level can affect cellular metabolic features as well as mitochondrial activity and consequently modify lifespan. The described mechanism is expected to open new avenues for research of aging and age-related diseases.

Indexed as

Gene Expression Regulation, FungalAMP-Activated Protein KinasesCell DivisionGlucoseHSP90 Heat-Shock ProteinsMetabolic Networks and PathwaysMitochondriaOxygen ConsumptionProtein Serine-Threonine KinasesProteostasisSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSignal TransductionTranscription FactorsAMP-Activated Protein KinasesGlucoseHSP82 protein, S cerevisiaeHSP90 Heat-Shock ProteinsProtein Serine-Threonine KinasesSaccharomyces cerevisiae ProteinsSNF1-related protein kinasesTORC1 protein complex, S cerevisiaeTranscription Factorsageingglucose starvationmitochondriaprotein chaperonesreplicative lifespanSnf1/AMPKTORC1yeast

Identifiers

PMID28613034
PMCPMC5595670
OpenAlexW2626855925

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.