Evidence map›Paper›PMID 38279024›Full record

ArticleCellular and molecular life sciences : CMLS2024

Hypoxia-driven deSUMOylation of EXOSC10 promotes adaptive changes in the transcriptome profile.

Chrysa Filippopoulou, Chairini C Thomé, Sofia Perdikari, Evgenia Ntini, George Simos, Katherine E Bohnsack, Georgia Chachami

Open access · goldAbstract read
In one paragraph

Article in Cellular and molecular life sciences : CMLS, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
2.1field-weighted citation impact, top 14% 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

11 citing papers in PubMed, 9 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

7 authors at 3 institutions in 3 countries.

Chrysa FilippopoulouLaboratory of Biochemistry, Faculty of Medicine, University of Thessaly, Biopolis, 41500, Larissa, Greece.
Chairini C ThoméDepartment of Molecular Biology, University Medical Center Göttingen, 37073, Göttingen, Germany.
Sofia PerdikariInstitute of Molecular Biology and Biotechnology, Foundation for Research and Technology-Hellas (FORTH), 70013, Heraklion, Greece.
Evgenia NtiniInstitute of Molecular Biology and Biotechnology, Foundation for Research and Technology-Hellas (FORTH), 70013, Heraklion, Greece.
George SimosLaboratory of Biochemistry, Faculty of Medicine, University of Thessaly, Biopolis, 41500, Larissa, Greece.
Katherine E BohnsackDepartment of Molecular Biology, University Medical Center Göttingen, 37073, Göttingen, Germany.
Georgia ChachamiLaboratory of Biochemistry, Faculty of Medicine, University of Thessaly, Biopolis, 41500, Larissa, Greece. ghah@med.uth.gr.ORCID http://orcid.org/0000-0002-4771-4196
University of Thessaly · GRFoundation for Research and Technology Hellas · GRUniversitätsmedizin Göttingen · DE

Funding

HFRI 1460SFB 1565 469281184P12
6 · The paper itself

Abstract

Reduced oxygen availability (hypoxia) triggers adaptive cellular responses via hypoxia-inducible factor (HIF)-dependent transcriptional activation. Adaptation to hypoxia also involves transcription-independent processes like post-translational modifications; however, these mechanisms are poorly characterized. Investigating the involvement of protein SUMOylation in response to hypoxia, we discovered that hypoxia strongly decreases the SUMOylation of Exosome subunit 10 (EXOSC10), the catalytic subunit of the RNA exosome, in an HIF-independent manner. EXOSC10 is a multifunctional exoribonuclease enriched in the nucleolus that mediates the processing and degradation of various RNA species. We demonstrate that the ubiquitin-specific protease 36 (USP36) SUMOylates EXOSC10 and we reveal SUMO1/sentrin-specific peptidase 3 (SENP3) as the enzyme-mediating deSUMOylation of EXOSC10. Under hypoxia, EXOSC10 dissociates from USP36 and translocates from the nucleolus to the nucleoplasm concomitant with its deSUMOylation. Loss of EXOSC10 SUMOylation does not detectably affect rRNA maturation but affects the mRNA transcriptome by modulating the expression levels of hypoxia-related genes. Our data suggest that dynamic modulation of EXOSC10 SUMOylation and localization under hypoxia regulates the RNA degradation machinery to facilitate cellular adaptation to low oxygen conditions.

Indexed as

ExosomesTranscriptomeCysteine EndopeptidasesExoribonucleasesExosome Multienzyme Ribonuclease ComplexHumansHypoxiaHypoxia-Inducible Factor 1, alpha SubunitOxygenSumoylationTranscriptional ActivationUbiquitin ThiolesteraseCysteine EndopeptidasesExoribonucleasesEXOSC10 protein, humanExosome Multienzyme Ribonuclease ComplexHypoxia-Inducible Factor 1, alpha SubunitOxygenSENP3 protein, humanUbiquitin ThiolesteraseUSP36 protein, humanHIF-1αHypoxiaRNA exosomeSENP3SUMOUSP36

Identifiers

PMID38279024
PMCPMC10817850
OpenAlexW4391282715

What OpenQuestion holds

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LicenceCC BY
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Registered trials

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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.