Evidence map›Paper›PMID 29183993›Full record

ArticleThe Journal of biological chemistry2018

Failed mitochondrial import and impaired proteostasis trigger SUMOylation of mitochondrial proteins.

Florian Paasch, Fabian den Brave, Ivan Psakhye, Boris Pfander, Stefan Jentsch

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2018. 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
0.8field-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

15 citing papers in PubMed, 27 citations in OpenAlex.

  1. Article
  2. The role of the nucleus in the control of mitochondrial precursor proteins in yeast.Protein science : a publication of the Protein Society · 2026
    Review
  3. Function and regulation of the mitochondrial stress response.Nature structural & molecular biology · 2026
    Review
  4. Article
  5. Article
  6. Article
  7. Mitochondrial protein import stress.Nature cell biology · 2025
    Review
  8. ULP-2 SUMO protease regulates UPRFree radical biology & medicine · 2024
    Article
  9. Article
  10. Review
  11. Common Principles and Specific Mechanisms of Mitophagy from Yeast to Humans.International journal of molecular sciences · 2021
    Review
  12. Article
  13. Review
  14. Review
  15. 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

5 authors at 3 institutions in 3 countries.

Florian PaaschFrom the Department of Molecular Cell Biology and.
Fabian den BraveFrom the Department of Molecular Cell Biology and denbrave@biochem.mpg.de.
Ivan PsakhyeFrom the Department of Molecular Cell Biology and.
Boris Pfanderthe Research Group DNA Replication and Genome Integrity, Max Planck Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany bpfander@biochem.mpg.de.ORCID 0000-0003-2180-5054
Stefan JentschFrom the Department of Molecular Cell Biology and.
Institute of Molecular and Cell Biology · RUBioChem Technology (United States) · USMax Planck Institute of Biochemistry · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Modification by the ubiquitin-like protein SUMO affects hundreds of cellular substrate proteins and regulates a wide variety of physiological processes. While the SUMO system appears to predominantly target nuclear proteins and, to a lesser extent, cytosolic proteins, hardly anything is known about the SUMOylation of proteins targeted to membrane-enclosed organelles. Here, we identify a large set of structurally and functionally unrelated mitochondrial proteins as substrates of the SUMO pathway in yeast. We show that SUMO modification of mitochondrial proteins does not rely on mitochondrial targeting and, in fact, is strongly enhanced upon import failure, consistent with the modification occurring in the cytosol. Moreover, SUMOylated forms of mitochondrial proteins particularly accumulate in HSP70- and proteasome-deficient cells, suggesting that SUMOylation participates in cellular protein quality control. We therefore propose that SUMO serves as a mark for nonfunctional mitochondrial proteins, which only sporadically arise in unstressed cells but strongly accumulate upon defective mitochondrial import and impaired proteostasis. Overall, our findings provide support for a role of SUMO in the cytosolic response to aberrant proteins.

Indexed as

Biological TransportMicroscopy, FluorescenceMitochondriaMitochondrial ProteinsProteostasisSaccharomyces cerevisiaeSumoylationMitochondrial Proteins70-kilodalton heat shock protein (HSP70)mitochondriamitochondrial proteinsproteasomeprotein quality controlproteostasissmall ubiquitin-like modifier (SUMO)SUMOylation

Identifiers

PMID29183993
PMCPMC5767865
OpenAlexW2770297849

What OpenQuestion holds

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LicenceCC BY
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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.