Evidence map›Paper›PMID 22993211›Full record

ArticleMolecular biology of the cell2012

Role of the AAA protease Yme1 in folding of proteins in the intermembrane space of mitochondria.

Bernadette Schreiner, Heike Westerburg, Ignasi Forné, Axel Imhof, Walter Neupert, Dejana Mokranjac

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

36 citing papers in PubMed, 71 citations in OpenAlex.

  1. mtHsp70 chaperone converts mitochondrial proteostasis stress into impaired protein import.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  2. Article
  3. Review
  4. Elucidation of molecular mechanisms by which amyloid βBiochimica et biophysica acta. Molecular and cell biology of lipids · 2024
    Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Review
  13. Article
  14. Review
  15. Quality control of the mitochondrial proteome.Nature reviews. Molecular cell biology · 2021
    Review
  16. Protein Quality Control at the Mitochondrial Surface.Frontiers in cell and developmental biology · 2021
    Review
  17. Review
  18. Article
  19. Article
  20. 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 1 country.

Bernadette SchreinerAdolf Butenandt Institute, Physiological Chemistry, University of Munich, 81377 Munich, Germany.
Heike Westerburg
Ignasi Forné
Axel Imhof
Walter Neupert
Dejana Mokranjac
Ludwig-Maximilians-Universität München · DEMax Planck Society · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The vast majority of mitochondrial proteins are synthesized in the cytosol and transported into the organelle in a largely, if not completely, unfolded state. The proper function of mitochondria thus depends on folding of several hundreds of proteins in the various subcompartments of the organelle. Whereas folding of proteins in the mitochondrial matrix is supported by members of several chaperone families, very little is known about folding of proteins in the intermembrane space (IMS). We targeted dihydrofolate reductase (DHFR) as a model substrate to the IMS of yeast mitochondria and analyzed its folding. DHFR can fold in this compartment, and its aggregation upon heat shock can be prevented in an ATP-dependent manner. Yme1, an AAA (ATPases associated with diverse cellular activities) protease of the IMS, prevented aggregation of DHFR. Analysis of protein aggregates in mitochondria lacking Yme1 revealed the presence of a number of proteins involved in the establishment of mitochondrial ultrastructure, lipid metabolism, protein import, and respiratory growth. These findings explain the pleiotropic effects of deletion of YME1 and suggest an important role for Yme1 as a folding assistant, in addition to its proteolytic function, in the protein homeostasis of mitochondria.

Indexed as

Protein FoldingAnimalsATP-Dependent ProteasesMiceMitochondriaMitochondrial ProteinsSaccharomyces cerevisiae ProteinsTetrahydrofolate DehydrogenaseATP-Dependent ProteasesMitochondrial ProteinsMpm1 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsTetrahydrofolate DehydrogenaseYME1 protein, S cerevisiae

Identifiers

PMID22993211
PMCPMC3496608
OpenAlexW2117108451

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.