Evidence map›Paper›PMID 36253107›Full record

ArticleLife science alliance2023

The metabolite-controlled ubiquitin conjugase Ubc8 promotes mitochondrial protein import.

Saskia Rödl, Fabian den Brave, Markus Räschle, Büsra Kizmaz, Svenja Lenhard, Carina Groh, Hanna Becker, Jannik Zimmermann, Bruce Morgan, Elke Richling and 2 more

Open access · goldAbstract read
In one paragraph

Article in Life science alliance, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.9field-weighted citation impact, top 28% 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

6 citing papers in PubMed, 10 citations in OpenAlex.

  1. RANBP9 and RANBP10 cooperate in regulating non-small cell lung cancer proliferation.Journal of experimental & clinical cancer research : CR · 2025
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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

12 authors at 3 institutions in 1 country.

Saskia RödlCell Biology, University of Kaiserslautern, Kaiserslautern, Germany.
Fabian den BraveInstitute of Biochemistry and Molecular Biology, Faculty of Medicine, University of Bonn, Bonn, Germany.
Markus RäschleMolecular Genetics, University of Kaiserslautern, Kaiserslautern, Germany.
Büsra KizmazCell Biology, University of Kaiserslautern, Kaiserslautern, Germany.
Svenja LenhardCell Biology, University of Kaiserslautern, Kaiserslautern, Germany.
Carina GrohCell Biology, University of Kaiserslautern, Kaiserslautern, Germany.
Hanna BeckerFood Chemistry, University of Kaiserslautern, Kaiserslautern, Germany.ORCID 0000-0003-1749-6711
Jannik ZimmermannBiochemistry, Center for Human and Molecular Biology (ZHMB), Saarland University, Saarbrücken, Germany.ORCID 0000-0002-3336-042X
Bruce MorganBiochemistry, Center for Human and Molecular Biology (ZHMB), Saarland University, Saarbrücken, Germany.
Elke RichlingFood Chemistry, University of Kaiserslautern, Kaiserslautern, Germany.
Thomas BeckerInstitute of Biochemistry and Molecular Biology, Faculty of Medicine, University of Bonn, Bonn, Germany.
Johannes M HerrmannCell Biology, University of Kaiserslautern, Kaiserslautern, Germany hannes.herrmann@biologie.uni-kl.de.ORCID 0000-0003-2081-4506
University of Kaiserslautern · DESaarland University · DEUniversity of Bonn · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Mitochondria play a key role in cellular energy metabolism. Transitions between glycolytic and respiratory conditions induce considerable adaptations of the cellular proteome. These metabolism-dependent changes are particularly pronounced for the protein composition of mitochondria. Here, we show that the yeast cytosolic ubiquitin conjugase Ubc8 plays a crucial role in the remodeling process when cells transition from respiratory to fermentative conditions. Ubc8 is a conserved and well-studied component of the catabolite control system that is known to regulate the stability of gluconeogenic enzymes. Unexpectedly, we found that Ubc8 also promotes the assembly of the translocase of the outer membrane of mitochondria (TOM) and increases the levels of its cytosol-exposed receptor subunit Tom22. Ubc8 deficiency results in compromised protein import into mitochondria and reduced steady-state levels of mitochondrial proteins. Our observations show that Ubc8, which is controlled by the prevailing metabolic conditions, promotes the switch from glucose synthesis to glucose usage in the cytosol and induces the biogenesis of the mitochondrial TOM machinery to improve mitochondrial protein import during phases of metabolic transition.

Indexed as

Protein TransportSaccharomyces cerevisiae ProteinsUbiquitin-Conjugating Enzymesgamma-Glutamyl HydrolaseGlucoseMitochondrial ProteinsProteomeSaccharomyces cerevisiaeUbiquitingamma-Glutamyl HydrolaseGlucoseMitochondrial ProteinsProteomeSaccharomyces cerevisiae ProteinsUbiquitinUbiquitin-Conjugating Enzymesubiquitin-conjugating enzyme UBC8

Identifiers

PMID36253107
PMCPMC9579816
OpenAlexW4306660738

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.