Evidence map›Paper›PMID 29133406›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2017

Proteome-wide modulation of degradation dynamics in response to growth arrest.

Tian Zhang, Clara Wolfe, Andrew Pierle, Kevin A Welle, Jennifer R Hryhorenko, Sina Ghaemmaghami

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
2.2field-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

17 citing papers in PubMed, 32 citations in OpenAlex.

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  10. Fluorescent Protein-Based Autophagy Biosensors.Materials (Basel, Switzerland) · 2021
    Review
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  17. Cross-species Comparison of Proteome Turnover Kinetics.Molecular & cellular proteomics : MCP · 2018
    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

6 authors at 1 institution in 1 country.

Tian ZhangDepartment of Biology, University of Rochester, Rochester, NY 14627.
Clara WolfeDepartment of Biology, University of Rochester, Rochester, NY 14627.
Andrew PierleDepartment of Biology, University of Rochester, Rochester, NY 14627.
Kevin A WelleMass Spectrometry Resource Laboratory, University of Rochester, Rochester, NY 14627.
Jennifer R HryhorenkoMass Spectrometry Resource Laboratory, University of Rochester, Rochester, NY 14627.
Sina GhaemmaghamiDepartment of Biology, University of Rochester, Rochester, NY 14627; sghaemma@bio.rochester.edu.ORCID 0000-0002-8696-2950
University of Rochester · US

Funding

The prevalence and mechanism of selectivity in basal autophagyR35GM119502 · NIGMS · UNIVERSITY OF ROCHESTER · PI SINA GHAEMMAGHAMI · 2016 to 2026
$5.9M
QExactive for UR Proteomics ResearchS10OD021486 · OD · UNIVERSITY OF ROCHESTER · PI GHAEMMAGHAMI, SINA · 2016 to 2016
$309k
NIGMS NIH HHS R35 GM119502NIH HHS S10 OD021486
6 · The paper itself

Abstract

In dividing cells, cytoplasmic dilution is the dominant route of clearance for long-lived proteins whose inherent degradation is slower than the cellular growth rate. Thus, as cells transition from a dividing to a nondividing state, there is a propensity for long-lived proteins to become stabilized relative to short-lived proteins, leading to alterations in the abundance distribution of the proteome. However, it is not known if cells mount a compensatory response to counter this potentially deleterious proteostatic disruption. We used a proteomic approach to demonstrate that fibroblasts selectively increase degradation rates of long-lived proteins as they transition from a proliferating to a quiescent state. The selective degradation of long-lived proteins occurs by the concurrent activation of lysosomal biogenesis and up-regulation of macroautophagy. Through this mechanism, quiescent cells avoid the accumulation of aged long-lived proteins that would otherwise result from the absence of cytoplasmic dilution by cell division.

Indexed as

AutophagyAutophagy-Related Protein 5CathepsinsCell Cycle CheckpointsCycloheximideCytokinesisFibroblastsGene Expression RegulationGene OntologyHalf-LifeHomeostasisHumansKineticsLysosomesMolecular Sequence AnnotationMuscle ProteinsATG5 protein, humanAutophagy-Related Protein 5CathepsinsCycloheximideMTOR protein, humanMuscle ProteinsProteasome Endopeptidase ComplexProteomePSME1 protein, humanRNA, Small InterferingTOR Serine-Threonine Kinaseslysosomeprotein degradationprotein homeostasisquantitative proteomicsquiescence

Identifiers

PMID29133406
PMCPMC5715755
OpenAlexW2770351359

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.