Evidence map›Paper›PMID 25971775›Full record

ArticleThe EMBO journal2015

Not4-dependent translational repression is important for cellular protein homeostasis in yeast.

Steffen Preissler, Julia Reuther, Miriam Koch, Annika Scior, Michael Bruderek, Tancred Frickey, Elke Deuerling

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
2.9field-weighted citation impact, top 9% 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

36 citing papers in PubMed, 58 citations in OpenAlex.

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  8. A ubiquitin language communicates ribosomal distress.Seminars in cell & developmental biology · 2024
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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

7 authors at 1 institution in 1 country.

Steffen PreisslerMolecular Microbiology, University of Konstanz, Konstanz, Germany Konstanz Research School Chemical Biology, University of Konstanz, Konstanz, Germany sp693@cam.ac.uk elke.deuerling@uni-konstanz.de.
Julia ReutherMolecular Microbiology, University of Konstanz, Konstanz, Germany Konstanz Research School Chemical Biology, University of Konstanz, Konstanz, Germany.
Miriam KochMolecular Microbiology, University of Konstanz, Konstanz, Germany Konstanz Research School Chemical Biology, University of Konstanz, Konstanz, Germany.
Annika SciorMolecular Microbiology, University of Konstanz, Konstanz, Germany Konstanz Research School Chemical Biology, University of Konstanz, Konstanz, Germany.
Michael BruderekMolecular Microbiology, University of Konstanz, Konstanz, Germany.
Tancred FrickeyApplied Bioinformatics, University of Konstanz, Konstanz, Germany.
Elke DeuerlingMolecular Microbiology, University of Konstanz, Konstanz, Germany sp693@cam.ac.uk elke.deuerling@uni-konstanz.de.
University of Konstanz · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Translation of aberrant or problematic mRNAs can cause ribosome stalling which leads to the production of truncated or defective proteins. Therefore, cells evolved cotranslational quality control mechanisms that eliminate these transcripts and target arrested nascent polypeptides for proteasomal degradation. Here we show that Not4, which is part of the multifunctional Ccr4-Not complex in yeast, associates with polysomes and contributes to the negative regulation of protein synthesis. Not4 is involved in translational repression of transcripts that cause transient ribosome stalling. The absence of Not4 affected global translational repression upon nutrient withdrawal, enhanced the expression of arrested nascent polypeptides and caused constitutive protein folding stress and aggregation. Similar defects were observed in cells with impaired mRNA decapping protein function and in cells lacking the mRNA decapping activator and translational repressor Dhh1. The results suggest a role for Not4 together with components of the decapping machinery in the regulation of protein expression on the mRNA level and emphasize the importance of translational repression for the maintenance of proteome integrity.

Indexed as

Protein BiosynthesisDEAD-box RNA HelicasesEndoribonucleasesGene Expression Regulation, FungalHomeostasisPolylysinePolyribosomesRepressor ProteinsRibonucleasesRibosomesRNA Cap-Binding ProteinsRNA, MessengerSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsUbiquitin-Protein LigasesCCR4 protein, S cerevisiaeDCP1 protein, S cerevisiaeDEAD-box RNA HelicasesDHH1 protein, S cerevisiaeEndoribonucleasesMOT2 protein, S cerevisiaePolylysineRepressor ProteinsRibonucleasesRNA Cap-Binding ProteinsRNA, MessengerSaccharomyces cerevisiae ProteinsUbiquitin-Protein LigasesCcr4–Not complexNot4protein homeostasisribosome stallingtranslational repression

Identifiers

PMID25971775
PMCPMC4547895
OpenAlexW2140717971

What OpenQuestion holds

Textmetadata
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.