Evidence map›Paper›PMID 26857222›Full record

ArticleRNA (New York, N.Y.)2016

Cooling-induced SUMOylation of EXOSC10 down-regulates ribosome biogenesis.

John R P Knight, Amandine Bastide, Diego Peretti, Anne Roobol, Jo Roobol, Giovanna R Mallucci, C Mark Smales, Anne E Willis

Open access · bronzeAbstract read
In one paragraph

Article in RNA (New York, N.Y.), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
2.6field-weighted citation impact, top 10% 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

23 citing papers in PubMed, 35 citations in OpenAlex.

  1. Review
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  20. TAp73 contributes to the oxidative stress response by regulating protein synthesis.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
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

8 authors at 3 institutions in 1 country.

John R P KnightMedical Research Council Toxicology Unit, Hodgkin Building, Leicester, LE1 9HN, United Kingdom.ORCID http://orcid.org/0000-0002-8771-5484
Amandine BastideMedical Research Council Toxicology Unit, Hodgkin Building, Leicester, LE1 9HN, United Kingdom.
Diego PerettiMedical Research Council Toxicology Unit, Hodgkin Building, Leicester, LE1 9HN, United Kingdom Department of Clinical Neurosciences, Clifford Allbutt Building, Cambridge Biomedical Campus, University of Cambridge, Cambridge, CB2 0AH, United Kingdom.
Anne RoobolCentre for Molecular Processing and School of Biosciences, University of Kent, Canterbury, Kent, CT2 7NJ, United Kingdom.
Jo RoobolCentre for Molecular Processing and School of Biosciences, University of Kent, Canterbury, Kent, CT2 7NJ, United Kingdom.
Giovanna R MallucciMedical Research Council Toxicology Unit, Hodgkin Building, Leicester, LE1 9HN, United Kingdom Department of Clinical Neurosciences, Clifford Allbutt Building, Cambridge Biomedical Campus, University of Cambridge, Cambridge, CB2 0AH, United Kingdom.
C Mark SmalesCentre for Molecular Processing and School of Biosciences, University of Kent, Canterbury, Kent, CT2 7NJ, United Kingdom.
Anne E WillisMedical Research Council Toxicology Unit, Hodgkin Building, Leicester, LE1 9HN, United Kingdom.
Medical Research Council · GBUniversity of Kent · GBUniversity of Cambridge · GB

Funding

Biotechnology and Biological Sciences Research Council BB/F018738/1Biotechnology and Biological Sciences Research Council BB/F018908/1Biotechnology and Biological Sciences Research Council BB/I019790/1Biotechnology and Biological Sciences Research Council BB/I020055/1Medical Research Council MC_U123160654Medical Research Council MC_U132692719Medical Research Council MR/M501773/1
6 · The paper itself

Abstract

The RNA exosome is essential for 3' processing of functional RNA species and degradation of aberrant RNAs in eukaryotic cells. Recent reports have defined the substrates of the exosome catalytic domains and solved the multimeric structure of the exosome complex. However, regulation of exosome activity remains poorly characterized, especially in response to physiological stress. Following the observation that cooling of mammalian cells results in a reduction in 40S:60S ribosomal subunit ratio, we uncover regulation of the nuclear exosome as a result of reduced temperature. Using human cells and an in vivo model system allowing whole-body cooling, we observe reduced EXOSC10 (hRrp6, Pm/Scl-100) expression in the cold. In parallel, both models of cooling increase global SUMOylation, leading to the identification of specific conjugation of SUMO1 to EXOSC10, a process that is increased by cooling. Furthermore, we define the major SUMOylation sites in EXOSC10 by mutagenesis and show that overexpression of SUMO1 alone is sufficient to suppress EXOSC10 abundance. Reducing EXOSC10 expression by RNAi in human cells correlates with the 3' preribosomal RNA processing defects seen in the cold as well as reducing the 40S:60S ratio, a previously uncharacterized consequence of EXOSC10 suppression. Together, this work illustrates that EXOSC10 can be modified by SUMOylation and identifies a physiological stress where this regulation is prevalent both in vitro and in vivo.

Indexed as

Amino Acid SequenceAnimalsCold-Shock ResponseEnzyme RepressionExoribonucleasesExosome Multienzyme Ribonuclease ComplexHEK293 CellsHumansMiceMolecular Sequence DataProtein BiosynthesisRibosome Subunits, Large, EukaryoticRibosome Subunits, Small, EukaryoticRNA, RibosomalSUMO-1 ProteinSumoylationExoribonucleasesEXOSC10 protein, humanExosome Multienzyme Ribonuclease ComplexRNA, RibosomalSUMO-1 ProteinSUMO1 protein, human40S subunitscold shockRNA exosomerRNA processingSUMOylation

Identifiers

PMID26857222
PMCPMC4793216
OpenAlexW2300134937

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.