Evidence map›Paper›PMID 29497115›Full record

ArticleScientific reports2018

Loss of mRNA surveillance pathways results in widespread protein aggregation.

Nur Hidayah Jamar, Paraskevi Kritsiligkou, Chris M Grant

Erratum issuedOpen access · goldAbstract read
In one paragraph

Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

22 citing papers in PubMed, 48 citations in OpenAlex.

  1. Article
  2. RAN Translation-Coupled Decay of theInternational journal of molecular sciences · 2026
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  13. Emerging Roles of RNA-Binding Proteins in Neurodevelopment.Journal of developmental biology · 2022
    Review
  14. Review
  15. Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

3 authors at 1 institution in 2 countries.

Nur Hidayah Jamar *Division of Molecular and Cellular Function, School of Biological Sciences, Faculty of Biology Medicine and Health, Manchester Academic Health Science Centre, The University of Manchester, Manchester, M13 9PT, UK.
Paraskevi Kritsiligkou *Division of Molecular and Cellular Function, School of Biological Sciences, Faculty of Biology Medicine and Health, Manchester Academic Health Science Centre, The University of Manchester, Manchester, M13 9PT, UK.ORCID http://orcid.org/0000-0003-2452-141X
Chris M GrantDivision of Molecular and Cellular Function, School of Biological Sciences, Faculty of Biology Medicine and Health, Manchester Academic Health Science Centre, The University of Manchester, Manchester, M13 9PT, UK. chris.grant@manchester.ac.uk.ORCID http://orcid.org/0000-0002-0616-6576
Manchester Academic Health Science Centre · GB

Funding

Biotechnology and Biological Sciences Research Council BB/M020770/1Wellcome Trust
6 · The paper itself

Abstract

Eukaryotic cells contain translation-associated mRNA surveillance pathways which prevent the production of potentially toxic proteins from aberrant mRNA translation events. We found that loss of mRNA surveillance pathways in mutants deficient in nonsense-mediated decay (NMD), no-go decay (NGD) and nonstop decay (NSD) results in increased protein aggregation. We have isolated and identified the proteins that aggregate and our bioinformatic analyses indicates that increased aggregation of aggregation-prone proteins is a general occurrence in mRNA surveillance mutants, rather than being attributable to specific pathways. The proteins that aggregate in mRNA surveillance mutants tend to be more highly expressed, more abundant and more stable proteins compared with the wider proteome. There is also a strong correlation with the proteins that aggregate in response to nascent protein misfolding and an enrichment for proteins that are substrates of ribosome-associated Hsp70 chaperones, consistent with susceptibility for aggregation primarily occurring during translation/folding. We also identified a significant overlap between the aggregated proteins in mRNA surveillance mutants and ageing yeast cells suggesting that translation-dependent protein aggregation may be a feature of the loss of proteostasis that occurs in aged cell populations.

Indexed as

Biochemical PhenomenaEndoribonucleasesEukaryotic CellsHSP70 Heat-Shock ProteinsNonsense Mediated mRNA DecayProtein AggregatesProtein BiosynthesisRibosomesRNA, MessengerRNA StabilitySaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsEndoribonucleasesHSP70 Heat-Shock ProteinsProtein AggregatesRNA, MessengerSaccharomyces cerevisiae Proteins

Identifiers

PMID29497115
PMCPMC5832753
OpenAlexW2806045028

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.