Evidence map›Paper›PMID 28076789›Full record

ArticleCell reports2017

Reduced Insulin/IGF-1 Signaling Restores the Dynamic Properties of Key Stress Granule Proteins during Aging.

Marie C Lechler, Emily D Crawford, Nicole Groh, Katja Widmaier, Raimund Jung, Janine Kirstein, Jonathan C Trinidad, Alma L Burlingame, Della C David

Open access · goldAbstract read
In one paragraph

Article in Cell reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed, 1 pooled it
3.4field-weighted citation impact, top 7% 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

44 citing papers in PubMed, 1 synthesis or guideline pooled it, 79 citations in OpenAlex.

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  19. Chaotic aging: intrinsically disordered proteins in aging-related processes.Cellular and molecular life sciences : CMLS · 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

9 authors at 4 institutions in 2 countries.

Marie C LechlerGerman Center for Neurodegenerative Diseases, 72076 Tübingen, Germany; Graduate Training Centre of Neuroscience, 72074 Tübingen, Germany.
Emily D CrawfordGerman Center for Neurodegenerative Diseases, 72076 Tübingen, Germany.
Nicole GrohGerman Center for Neurodegenerative Diseases, 72076 Tübingen, Germany; Graduate Training Centre of Neuroscience, 72074 Tübingen, Germany.
Katja WidmaierGerman Center for Neurodegenerative Diseases, 72076 Tübingen, Germany.
Raimund JungGerman Center for Neurodegenerative Diseases, 72076 Tübingen, Germany.
Janine KirsteinLeibniz-Institut für Molekulare Pharmakologie im Forschungsverbund Berlin, 13125 Berlin, Germany.
Jonathan C TrinidadMass Spectrometry Facility, Department of Pharmaceutical Chemistry, University of California, San Francisco, San Francisco, CA 94158, USA.
Alma L BurlingameMass Spectrometry Facility, Department of Pharmaceutical Chemistry, University of California, San Francisco, San Francisco, CA 94158, USA.
Della C DavidGerman Center for Neurodegenerative Diseases, 72076 Tübingen, Germany. Electronic address: della.david@dzne.de.
German Center for Neurodegenerative Diseases · DEUniversity of California, San Francisco · USBernstein Center for Computational Neuroscience Tübingen · DEForschungsverbund Berlin · DE

Funding

Rewiring Therapeutic Cells: User-Controlled T Cells and Stem CellsP50GM081879 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI LIM, WENDELL A · 2010 to 2017
$19.0M
Bio-Organic Biomedical Mass Spectromy ResourceP41GM103481 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI BURLINGAME, ALMA L · 2012 to 2015
$6.4M
NIGMS NIH HHS P41 GM103481NIGMS NIH HHS P50 GM081879
6 · The paper itself

Abstract

Low-complexity "prion-like" domains in key RNA-binding proteins (RBPs) mediate the reversible assembly of RNA granules. Individual RBPs harboring these domains have been linked to specific neurodegenerative diseases. Although their aggregation in neurodegeneration has been extensively characterized, it remains unknown how the process of aging disturbs RBP dynamics. We show that a wide variety of RNA granule components, including stress granule proteins, become highly insoluble with age in C. elegans and that reduced insulin/insulin-like growth factor 1 (IGF-1) daf-2 receptor signaling efficiently prevents their aggregation. Importantly, stress-granule-related RBP aggregates are associated with reduced fitness. We show that heat shock transcription factor 1 (HSF-1) is a main regulator of stress-granule-related RBP aggregation in both young and aged animals. During aging, increasing DAF-16 activity restores dynamic stress-granule-related RBPs, partly by decreasing the buildup of other misfolded proteins that seed RBP aggregation. Longevity-associated mechanisms found to maintain dynamic RBPs during aging could be relevant for neurodegenerative diseases.

Indexed as

Signal TransductionAgingAnimalsCaenorhabditis elegansCaenorhabditis elegans ProteinsCytoplasmic GranulesHeat-Shock ProteinsInsulinInsulin-Like Growth Factor ILongevityMutationProtein AggregatesReceptor, InsulinRNARNA-Binding ProteinsSolubilityCaenorhabditis elegans ProteinsDAF-2 protein, C elegansHeat-Shock ProteinsInsulinInsulin-Like Growth Factor IProtein AggregatesReceptor, InsulinRNARNA-Binding ProteinsagingCaenorhabditis elegansDAF-2HSF-1longevityneurodegenerative diseasesprotein aggregationRNA-binding proteinsstress granules

Identifiers

PMID28076789
PMCPMC5263236
OpenAlexW2569733750

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.