Evidence map›Paper›PMID 24465968›Full record

ArticlePloS one2014

The Not4 E3 ligase and CCR4 deadenylase play distinct roles in protein quality control.

David Halter, Martine A Collart, Olesya O Panasenko

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
2.8field-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

32 citing papers in PubMed, 54 citations in OpenAlex.

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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

3 authors at 1 institution in 1 country.

David HalterDepartment of Microbiology and Molecular Medicine, Faculty of Medicine, Institute of Genetics and Genomics of Geneva, University of Geneva, Geneva, Switzerland.
Martine A CollartDepartment of Microbiology and Molecular Medicine, Faculty of Medicine, Institute of Genetics and Genomics of Geneva, University of Geneva, Geneva, Switzerland.
Olesya O PanasenkoDepartment of Microbiology and Molecular Medicine, Faculty of Medicine, Institute of Genetics and Genomics of Geneva, University of Geneva, Geneva, Switzerland.
University of Geneva · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Eukaryotic cells control their proteome by regulating protein production and protein clearance. Protein production is determined to a large extent by mRNA levels, whereas protein degradation depends mostly upon the proteasome. Dysfunction of the proteasome leads to the accumulation of non-functional proteins that can aggregate, be toxic for the cell, and, in extreme cases, lead to cell death. mRNA levels are controlled by their rates of synthesis and degradation. Recent evidence indicates that these rates have oppositely co-evolved to ensure appropriate mRNA levels. This opposite co-evolution has been correlated with the mutations in the Ccr4-Not complex. Consistently, the deadenylation enzymes responsible for the rate-limiting step in eukaryotic mRNA degradation, Caf1 and Ccr4, are subunits of the Ccr4-Not complex. Another subunit of this complex is a RING E3 ligase, Not4. It is essential for cellular protein solubility and has been proposed to be involved in co-translational quality control. An open question has been whether this role of Not4 resides strictly in the regulation of the deadenylation module of the Ccr4-Not complex. However, Not4 is important for proper assembly of the proteasome, and the Ccr4-Not complex may have multiple functional modules that participate in protein quality control in different ways. In this work we studied how the functions of the Caf1/Ccr4 and Not4 modules are connected. We concluded that Not4 plays a role in protein quality control independently of the Ccr4 deadenylase, and that it is involved in clearance of aberrant proteins at least in part via the proteasome.

Indexed as

Azetidinecarboxylic AcidCathepsin AEnzyme StabilityGene DeletionMutant ProteinsPhenotypePolyribosomesPolyubiquitinProteasome Endopeptidase ComplexProtein BiosynthesisProtein Structure, QuaternaryProteolysisRepressor ProteinsRibonucleasesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsAzetidinecarboxylic AcidCathepsin ACCR4 protein, S cerevisiaeMOT2 protein, S cerevisiaeMutant ProteinsPolyubiquitinProteasome Endopeptidase ComplexRepressor ProteinsRibonucleasesSaccharomyces cerevisiae ProteinsUbiquitin-Protein Ligases

Identifiers

PMID24465968
PMCPMC3895043
OpenAlexW2058757202

What OpenQuestion holds

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LicenceCC BY
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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.