Evidence map›Paper›PMID 20157544›Full record

ArticleAging2009

The mitochondrial ribosomal protein of the large subunit, Afo1p, determines cellular longevity through mitochondrial back-signaling via TOR1.

Gino Heeren, Mark Rinnerthaler, Peter Laun, Phyllis von Seyerl, Sonja Kössler, Harald Klinger, Matthias Hager, Edith Bogengruber, Stefanie Jarolim, Birgit Simon-Nobbe and 9 more

Open access · hybridAbstract read
In one paragraph

Article in Aging, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.

0numbers the graph read from it
0cells of the map it votes in
50citing papers in PubMed
4.7field-weighted citation impact, top 4% 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

50 citing papers in PubMed, 85 citations in OpenAlex.

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  15. Mitonuclear communication in homeostasis and stress.Nature reviews. Molecular cell biology · 2016
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

19 authors at 5 institutions in 2 countries.

Gino HeerenDepartment of Cell Biology, Division of Genetics, University of Salzburg, 5020 Salzburg, Austria.
Mark Rinnerthaler
Peter Laun
Phyllis von Seyerl
Sonja Kössler
Harald Klinger
Matthias Hager
Edith Bogengruber
Stefanie Jarolim
Birgit Simon-Nobbe
Christoph Schüller
Didac Carmona-Gutierrez
Lore Breitenbach-Koller
Christoph Mück
Pidder Jansen-Dürr
Alfredo Criollo
Guido Kroemer
Frank Madeo
Michael Breitenbach
University of Salzburg · ATAustrian Academy of Sciences · ATInserm · FRUniversity of Graz · ATMax Perutz Labs · AT

Funding

Austrian Science Fund FWF P 19966Austrian Science Fund FWF S 9302
6 · The paper itself

Abstract

Yeast mother cell-specific aging constitutes a model of replicative aging as it occurs in stem cell populations of higher eukaryotes. Here, we present a new long-lived yeast deletion mutation,afo1 (for aging factor one), that confers a 60% increase in replicative lifespan. AFO1/MRPL25 codes for a protein that is contained in the large subunit of the mitochondrial ribosome. Double mutant experiments indicate that the longevity-increasing action of the afo1 mutation is independent of mitochondrial translation, yet involves the cytoplasmic Tor1p as well as the growth-controlling transcription factor Sfp1p. In their final cell cycle, the long-lived mutant cells do show the phenotypes of yeast apoptosis indicating that the longevity of the mutant is not caused by an inability to undergo programmed cell death. Furthermore, the afo1 mutation displays high resistance against oxidants. Despite the respiratory deficiency the mutant has paradoxical increase in growth rate compared to generic petite mutants. A comparison of the single and double mutant strains for afo1 and fob1 shows that the longevity phenotype of afo1 is independent of the formation of ERCs (ribosomal DNA minicircles). AFO1/MRPL25 function establishes a new connection between mitochondria, metabolism and aging.

Indexed as

Active Transport, Cell NucleusApoptosisCell ProliferationCell SizeCrosses, GeneticDNA-Binding ProteinsDNA, CircularDNA, RibosomalGene DeletionHydrogen PeroxideMitochondriaMitochondrial ProteinsMutationOxidantsOxidative StressPhosphatidylinositol 3-KinasesDNA-Binding ProteinsDNA, CircularDNA, RibosomalFOB1 protein, S cerevisiaeHydrogen PeroxideMitochondrial ProteinsMRP17 protein, S cerevisiaeMRPL25 protein, S cerevisiaeOxidantsPhosphatidylinositol 3-KinasesRibosomal ProteinsSaccharomyces cerevisiae ProteinsSFP1 protein, S cerevisiaeSirolimustert-ButylhydroperoxideTOR1 protein, S cerevisiaerapamycinSaccharomyces cerevisiaeTOR complexyeast mother cell-specific ageing

Identifiers

PMID20157544
PMCPMC2806038
OpenAlexW1564604840

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

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.