Evidence map›Paper›PMID 42315289›Full record

ArticleRNA (New York, N.Y.)2026

Puf3 contributes to changes in mRNA solubility, translation elongation dynamics at rare arginine codons and loss of protein homeostasis in cells lacking Not4.

Léna Audebert, George E Allen, Siyu Chen, Olesya O Panasenko, Susanne Huch, Christine Polte, Zoya Ignatova, Vicent Pelechano, Martine A Collart

Abstract read
In one paragraph

Article in RNA (New York, N.Y.), 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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0cells of the map it votes in
0citing papers in PubMed
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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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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.

Léna AudebertDepartment of Microbiology and Molecular Medicine, Faculty of Medicine and Institute of Genetics and Genomics Geneva, University of Geneva, 1211 Geneva 4, Switzerland.
George E AllenDepartment of Microbiology and Molecular Medicine, Faculty of Medicine and Institute of Genetics and Genomics Geneva, University of Geneva, 1211 Geneva 4, Switzerland.
Siyu ChenDepartment of Microbiology and Molecular Medicine, Faculty of Medicine and Institute of Genetics and Genomics Geneva, University of Geneva, 1211 Geneva 4, Switzerland.
Olesya O PanasenkoDepartment of Microbiology and Molecular Medicine, Faculty of Medicine and Institute of Genetics and Genomics Geneva, University of Geneva, 1211 Geneva 4, Switzerland.
Susanne HuchSciLifeLab, Department of Microbiology, Tumor and Cell Biology, Karolinska Institutet, 17165 Solna, Sweden.
Christine PolteBiochemistry and Molecular Biology, University of Hamburg, 20146 Hamburg, Germany.
Zoya IgnatovaBiochemistry and Molecular Biology, University of Hamburg, 20146 Hamburg, Germany.
Vicent PelechanoSciLifeLab, Department of Microbiology, Tumor and Cell Biology, Karolinska Institutet, 17165 Solna, Sweden.
Martine A CollartDepartment of Microbiology and Molecular Medicine, Faculty of Medicine and Institute of Genetics and Genomics Geneva, University of Geneva, 1211 Geneva 4, Switzerland martine.collart@unige.ch.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The Not proteins of the Ccr4-Not complex regulate translation elongation dynamics, essential for proper folding and assembly of new proteins. In yeast, ribosomes with nonoptimal codons in the A-site are enriched within the pool of ribosomes bound by Not4 and Not5. Such ribosomes accumulate in cells lacking Not4 or Not5 that show defects in co-translational assembly and aggregation of new proteins. Recently, we observed that depletion of Not1 and Not4 inversely regulate changes in mRNA solubility, correlating with inverse codon-specific changes in A-site ribosome dwelling occupancies (RDOs). Here we describe that mRNAs less soluble upon Not4 depletion are enriched for targets of the RNA-binding protein Puf3. We determine that Puf3 contributes to differential changes of A-site RDOs upon Not1 and Not4 depletion, in particular at rare arginine codons, and it contributes to changes in mRNA solubility in

Indexed as

ArginineCodonPeptide Chain Elongation, TranslationalProteostasisRNA-Binding ProteinsRNA, MessengerSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTranscription FactorsHomeostasisRibosomesSolubilityArginineCodonRNA-Binding ProteinsRNA, MessengerSaccharomyces cerevisiae ProteinsTranscription FactorsmRNA solubilityNot4protein homeostasisPuf3rare arginine codonsribosome dwelling

Identifiers

PMID42315289
PMCPMC13492119

What Socratic 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 Socratic graph.