Evidence map›Paper›PMID 38565738›Full record

ArticleEMBO reports2024

The ER-SURF pathway uses ER-mitochondria contact sites for protein targeting to mitochondria.

Christian Koch, Svenja Lenhard, Markus Räschle, Cristina Prescianotto-Baschong, Anne Spang, Johannes M Herrmann

Open access · diamondAbstract read
In one paragraph

Article in EMBO reports, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
7.7field-weighted citation impact, top 2% 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

27 citing papers in PubMed, 34 citations in OpenAlex.

  1. Review
  2. Mass spectrometry proteomics for studying mitostasis.Protein science : a publication of the Protein Society · 2026
    Review
  3. The role of the nucleus in the control of mitochondrial precursor proteins in yeast.Protein science : a publication of the Protein Society · 2026
    Review
  4. Functions of J-domain proteins in mitochondrial protein biogenesis.Protein science : a publication of the Protein Society · 2026
    Review
  5. Review
  6. Mitochondrial presequences are more than just address labels.Protein science : a publication of the Protein Society · 2026
    Review
  7. Review
  8. Functional role ofVirulence · 2025
    Article
  9. Article
  10. Article
  11. Review
  12. Review
  13. Review
  14. Article
  15. Article
  16. Review
  17. Article
  18. Mitochondrial protein import stress.Nature cell biology · 2025
    Review
  19. Article
  20. Tissue-specific differences in CaPhysiological reports · 2024
    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

6 authors at 2 institutions in 2 countries.

Christian KochCell Biology, University of Kaiserslautern, Kaiserslautern, Germany.
Svenja LenhardCell Biology, University of Kaiserslautern, Kaiserslautern, Germany.
Markus RäschleMolecular Genetics, University of Kaiserslautern, Kaiserslautern, Germany.ORCID 0000-0002-6737-7203
Cristina Prescianotto-BaschongBiozentrum, University of Basel, 4056, Basel, Switzerland.
Anne SpangBiozentrum, University of Basel, 4056, Basel, Switzerland.ORCID 0000-0002-2387-6203
Johannes M HerrmannCell Biology, University of Kaiserslautern, Kaiserslautern, Germany. Hannes.herrmann@biologie.uni-kl.de.ORCID 0000-0003-2081-4506
University of Kaiserslautern · DEUniversity of Basel · CH

Funding

Deutsche Forschungsgemeinschaft (DFG) GRK2737Deutsche Forschungsgemeinschaft (DFG) HE2803/10-1EC | ERC | HORIZON EUROPE European Research Council (ERC) 101052639Landesforschungsinitiative Rheinland-Pfalz BioCompSchweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung (SNF) 310030_185127
6 · The paper itself

Abstract

Most mitochondrial proteins are synthesized on cytosolic ribosomes and imported into mitochondria in a post-translational reaction. Mitochondrial precursor proteins which use the ER-SURF pathway employ the surface of the endoplasmic reticulum (ER) as an important sorting platform. How they reach the mitochondrial import machinery from the ER is not known. Here we show that mitochondrial contact sites play a crucial role in the ER-to-mitochondria transfer of precursor proteins. The ER mitochondria encounter structure (ERMES) and Tom70, together with Djp1 and Lam6, are part of two parallel and partially redundant ER-to-mitochondria delivery routes. When ER-to-mitochondria transfer is prevented by loss of these two contact sites, many precursors of mitochondrial inner membrane proteins are left stranded on the ER membrane, resulting in mitochondrial dysfunction. Our observations support an active role of the ER in mitochondrial protein biogenesis.

Indexed as

MitochondriaSaccharomyces cerevisiae ProteinsEndoplasmic ReticulumMitochondrial MembranesMitochondrial Membrane Transport ProteinsMitochondrial ProteinsProtein TransportMitochondrial Membrane Transport ProteinsMitochondrial ProteinsSaccharomyces cerevisiae ProteinsContact sitesEndoplasmic reticulumERMESMitochondriaProtein import

Identifiers

PMID38565738
PMCPMC11014988
OpenAlexW4393431356

What OpenQuestion holds

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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.