Evidence map›Paper›PMID 33596095›Full record

ArticleMolecular biology of the cell2021

The ER protein Ema19 facilitates the degradation of nonimported mitochondrial precursor proteins.

Janina Laborenz, Yury S Bykov, Katharina Knöringer, Markus Räschle, Sabine Filker, Cristina Prescianotto-Baschong, Anne Spang, Takashi Tatsuta, Thomas Langer, Zuzana Storchová and 2 more

Open access · bronzeAbstract read
In one paragraph

Article in Molecular biology of the cell, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

15 citing papers in PubMed, 24 citations in OpenAlex.

  1. The role of the nucleus in the control of mitochondrial precursor proteins in yeast.Protein science : a publication of the Protein Society · 2026
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  12. ER-SURF: Riding the Endoplasmic Reticulum Surface to Mitochondria.International journal of molecular sciences · 2021
    Review
  13. Article
  14. Article
  15. Protein Quality Control at the Mitochondrial Surface.Frontiers in cell and developmental biology · 2021
    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

12 authors at 4 institutions in 3 countries.

Janina LaborenzCell Biology, University of Kaiserslautern, 67663 Kaiserslautern, Germany.
Yury S BykovDepartment of Molecular Genetics, Weizmann Institute of Science, Rehovot 7610001, Israel.
Katharina KnöringerCell Biology, University of Kaiserslautern, 67663 Kaiserslautern, Germany.
Markus RäschleMolecular Genetics, University of Kaiserslautern, 67663 Kaiserslautern, Germany.
Sabine FilkerMolecular Ecology, University of Kaiserslautern, 67663 Kaiserslautern, Germany.
Cristina Prescianotto-BaschongBiozentrum, University of Basel, CH-4056 Basel, Switzerland.
Anne SpangBiozentrum, University of Basel, CH-4056 Basel, Switzerland.
Takashi TatsutaMax Planck Institute for Biology of Ageing, 50931 Cologne, Germany.
Thomas LangerMax Planck Institute for Biology of Ageing, 50931 Cologne, Germany.
Zuzana StorchováMolecular Genetics, University of Kaiserslautern, 67663 Kaiserslautern, Germany.
Maya SchuldinerDepartment of Molecular Genetics, Weizmann Institute of Science, Rehovot 7610001, Israel.
Johannes M HerrmannCell Biology, University of Kaiserslautern, 67663 Kaiserslautern, Germany.
University of Kaiserslautern · DEMax Planck Institute for Biology of Ageing · DEUniversity of Basel · CHWeizmann Institute of Science · IL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

For the biogenesis of mitochondria, hundreds of proteins need to be targeted from the cytosol into the various compartments of this organelle. The intramitochondrial targeting routes these proteins take to reach their respective location in the organelle are well understood. However, the early targeting processes, from cytosolic ribosomes to the membrane of the organelle, are still largely unknown. In this study, we present evidence that an integral membrane protein of the endoplasmic reticulum (ER), Ema19, plays a role in this process. Mutants lacking Ema19 show an increased stability of mitochondrial precursor proteins, indicating that Ema19 promotes the proteolytic degradation of nonproductive precursors. The deletion of Ema19 improves the growth of respiration-deficient cells, suggesting that Ema19-mediated degradation can compete with productive protein import into mitochondria. Ema19 is the yeast representative of a conserved protein family. The human Ema19 homologue is known as sigma 2 receptor or TMEM97. Though its molecular function is not known, previous studies suggested a role of the sigma 2 receptor as a quality control factor in the ER, compatible with our observations about Ema19. More globally, our data provide an additional demonstration of the important role of the ER in mitochondrial protein targeting.

Indexed as

CytosolEndoplasmic ReticulumMembrane ProteinsMitochondriaMitochondrial Membrane Transport ProteinsMitochondrial ProteinsProtein TransportProteolysisSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsMembrane ProteinsMitochondrial Membrane Transport ProteinsMitochondrial ProteinsSaccharomyces cerevisiae Proteins

Identifiers

PMID33596095
PMCPMC8108515
OpenAlexW3129815164

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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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.