Evidence map›Paper›PMID 32826315›Full record

ArticleThe Journal of biological chemistry2020

The intermembrane space protein Mix23 is a novel stress-induced mitochondrial import factor.

Eva Zöller, Janina Laborenz, Lena Krämer, Felix Boos, Markus Räschle, R Todd Alexander, Johannes M Herrmann

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.2field-weighted citation impact, top 22% 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

13 citing papers in PubMed, 21 citations in OpenAlex.

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  7. Methods to Study the Biogenesis of Mitoribosomal Proteins in Yeast.Methods in molecular biology (Clifton, N.J.) · 2023
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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 2 institutions in 2 countries.

Eva ZöllerDepartment of Cell Biology, University of Kaiserslautern, Kaiserslautern, Germany.
Janina LaborenzDepartment of Cell Biology, University of Kaiserslautern, Kaiserslautern, Germany.
Lena KrämerDepartment of Cell Biology, University of Kaiserslautern, Kaiserslautern, Germany.
Felix BoosDepartment of Cell Biology, University of Kaiserslautern, Kaiserslautern, Germany.
Markus RäschleDepartment of Molecular Genetics, University of Kaiserslautern, Kaiserslautern, Germany.
R Todd AlexanderDepartment of Pediatrics, University of Alberta, Edmonton, Alberta, Canada.
Johannes M HerrmannDepartment of Cell Biology, University of Kaiserslautern, Kaiserslautern, Germany. Electronic address: hannes.herrmann@biologie.uni-kl.de.
University of Kaiserslautern · DEUniversity of Alberta · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The biogenesis of mitochondria requires the import of hundreds of precursor proteins. These proteins are transported post-translationally with the help of chaperones, meaning that the overproduction of mitochondrial proteins or the limited availability of chaperones can lead to the accumulation of cytosolic precursor proteins. This imposes a severe challenge to cytosolic proteostasis and triggers a specific transcription program called the mitoprotein-induced stress response, which activates the proteasome system. This coincides with the repression of mitochondrial proteins, including many proteins of the intermembrane space. In contrast, herein we report that the so-far-uncharacterized intermembrane space protein Mix23 is considerably up-regulated when mitochondrial import is perturbed. Mix23 is evolutionarily conserved and a homolog of the human protein CCDC58. We found that, like the subunits of the proteasome, Mix23 is under control of the transcription factor Rpn4. It is imported into mitochondria by the mitochondrial disulfide relay. Mix23 is critical for the efficient import of proteins into the mitochondrial matrix, particularly if the function of the translocase of the inner membrane 23 is compromised such as in temperature-sensitive mutants of Tim17. Our observations identify Mix23 as a novel regulator or stabilizer of the mitochondrial protein import machinery that is specifically up-regulated upon mitoprotein-induced stress conditions.

Indexed as

Gene Expression Regulation, FungalMitochondriaMitochondrial ProteinsProtein TransportProteostasisSaccharomyces cerevisiaeStress, PhysiologicalUp-RegulationMitochondrial Proteinsdisulfideintermembrane spacemitochondriaproteasomeprotein importprotein translocationproteostasisstress response

Identifiers

PMID32826315
PMCPMC7586232
OpenAlexW3081388452

What OpenQuestion 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 OpenQuestion graph.