Evidence map›Paper›PMID 24500206›Full record

ArticleNucleic acids research2014

Sumoylation of the THO complex regulates the biogenesis of a subset of mRNPs.

Hugo Bretes, Jérôme O Rouviere, Thibaut Leger, Marlene Oeffinger, Frédéric Devaux, Valérie Doye, Benoit Palancade

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 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
3.3field-weighted citation impact, top 7% 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, 53 citations in OpenAlex.

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  17. When SUMO met splicing.RNA biology · 2018
    Review
  18. Review
  19. Article
  20. Roles of Sumoylation in mRNA Processing and Metabolism.Advances in experimental medicine and biology · 2017
    Review
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 4 institutions in 2 countries.

Hugo BretesInstitut Jacques Monod, CNRS, UMR 7592, Univ Paris Diderot, Sorbonne Paris Cité, F-75205 Paris, France, Ecole Doctorale Gènes Génomes Cellules, Université Paris Sud-11, Orsay, France, Proteomics facility, Institut Jacques Monod, CNRS, UMR 7592, Univ Paris Diderot, Sorbonne Paris Cité, F-75205 Paris, France, Department for Systems Biology, Institut de recherches cliniques de Montréal (IRCM), Montreal, Québec, Canada H2W 1R7, Département de Biochimie et Médecine Moléculaire, Faculté de Médecine, Université de Montréal, Montréal, Québec, Canada H3T 1J4, Division of Experimental Medicine, Faculty of Medicine, McGill University, Montréal, Québec, Canada H3A 1A3, Université Pierre et Marie Curie, UMR7238, 15, rue de l'Ecole de Médecine, 75006 Paris, France and CNRS, UMR7238, Laboratoire de Génomique des Microorganismes, 75006 Paris, France.
Jérôme O Rouviere
Thibaut Leger
Marlene Oeffinger
Frédéric Devaux
Valérie Doye
Benoit Palancade
Centre National de la Recherche Scientifique · FRMontreal Clinical Research Institute · CAUniversité Paris Cité · FRUniversité Paris-Sud · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Assembly of messenger ribonucleoparticles (mRNPs) is a pivotal step in gene expression, but only a few molecular mechanisms contributing to its regulation have been described. Here, through a comprehensive proteomic survey of mRNP assembly, we demonstrate that the SUMO pathway specifically controls the association of the THO complex with mRNPs. We further show that the THO complex, a key player in the interplay between gene expression, mRNA export and genetic stability, is sumoylated on its Hpr1 subunit and that this modification regulates its association with mRNPs. Altered recruitment of the THO complex onto mRNPs in sumoylation-defective mutants does not affect bulk mRNA export or genetic stability, but impairs the expression of acidic stress-induced genes and, consistently, compromises viability in acidic stress conditions. Importantly, inactivation of the nuclear exosome suppresses the phenotypes of the hpr1 non-sumoylatable mutant, showing that SUMO-dependent mRNP assembly is critical to allow a specific subset of mRNPs to escape degradation. This article thus provides the first example of a SUMO-dependent mRNP-assembly event allowing a refined tuning of gene expression, in particular under specific stress conditions.

Indexed as

SumoylationCysteine EndopeptidasesExosome Multienzyme Ribonuclease ComplexGene ExpressionNuclear ProteinsProteomeRibonucleoproteinsRNA, MessengerRNA TransportSaccharomyces cerevisiae ProteinsStress, PhysiologicalSUMO-1 ProteinUbiquitinationCysteine EndopeptidasesExosome Multienzyme Ribonuclease ComplexHPR1 protein, S cerevisiaemessenger ribonucleoproteinNuclear ProteinsProteomeRibonucleoproteinsRNA, MessengerSaccharomyces cerevisiae ProteinsSUMO-1 ProteinUlp1 protease

Identifiers

PMID24500206
PMCPMC4005672
OpenAlexW2097647525

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.