Evidence map›Paper›PMID 24648523›Full record

ArticleThe Journal of biological chemistry2014

Stress-triggered activation of the metalloprotease Oma1 involves its C-terminal region and is important for mitochondrial stress protection in yeast.

Iryna Bohovych, Garrett Donaldson, Sara Christianson, Nataliya Zahayko, Oleh Khalimonchuk

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
–field-weighted citation impact
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

35 citing papers in PubMed.

  1. Article
  2. Proteolytic control of mitochondrial protein translocases.Protein science : a publication of the Protein Society · 2026
    Review
  3. Article
  4. Review
  5. Review
  6. Article
  7. Mitochondrial membrane potential and oxidative stress interact to regulate Oma1-dependent processing of Opa1 and mitochondrial dynamics.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2024
    Article
  8. Article
  9. Review
  10. Article
  11. Review
  12. Review
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. OMA1-An integral membrane protease?Biochimica et biophysica acta. Proteins and proteomics · 2021
    Review
  20. 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

5 authors.

Iryna BohovychFrom the Department of Biochemistry and Nebraska Redox Biology Center, University of Nebraska-Lincoln, Lincoln, Nebraska 68588.
Garrett Donaldson
Sara Christianson
Nataliya Zahayko
Oleh Khalimonchuk

Funding

THE REDOX-MEDIATED REGULATION OF IRON-RESPONSIVE GENE EXPRESSION IN LIVERP20RR017675 · NCRR · UNIVERSITY OF NEBRASKA LINCOLN · PI GRASS, GREGOR · 2002 to 2011
$20.4M
Redox Biology CenterP30GM103335 · NIGMS · UNIVERSITY OF NEBRASKA LINCOLN · PI BECKER, DONALD F · 2012 to 2016
$4.3M
METAL CHELATION IN PROTEINS WITH POLYMETALLIC CLUSTERSR37ES003817 · NIEHS · UNIVERSITY OF UTAH · PI WINGE, DENNIS R. · 1999 to 2008
$4.1M
METAL CHELATION IN PROTEINS WITH POLYMETALLIC CLUSTERSR01ES003817 · NIEHS · UNIVERSITY OF UTAH · PI WINGE, DENNIS R. · 1985 to 2013
$2.3M
A Conserved Metalloprotease Required for Mitochondrial Maintenance and ProtectionR01GM108975 · NIGMS · UNIVERSITY OF NEBRASKA LINCOLN · PI KHALIMONCHUK, OLEH · 2014 to 2018
$1.4M
NCRR NIH HHS P20 RR-017675NCRR NIH HHS P20 RR017675NIEHS NIH HHS ES03817NIEHS NIH HHS R01 ES003817NIEHS NIH HHS R37 ES003817NIGMS NIH HHS P30 GM103335NIGMS NIH HHS P30GM103335NIGMS NIH HHS R01 GM108975
6 · The paper itself

Abstract

Functional integrity of mitochondria is critical for optimal cellular physiology. A suite of conserved mitochondrial proteases known as intramitochondrial quality control represents one of the mechanisms assuring normal mitochondrial function. We previously demonstrated that ATP-independent metalloprotease Oma1 mediates degradation of hypohemylated Cox1 subunit of cytochrome c oxidase and is active in cytochrome c oxidase-deficient mitochondria. Here we show that Oma1 is important for adaptive responses to various homeostatic insults and preservation of normal mitochondrial function under damage-eliciting conditions. Changes in membrane potential, oxidative stress, or chronic hyperpolarization lead to increased Oma1-mediated proteolysis. The stress-triggered induction of Oma1 proteolytic activity appears to be associated with conformational changes within the Oma1 homo-oligomeric complex, and these alterations likely involve C-terminal residues of the protease. Substitutions in the conserved C-terminal region of Oma1 impair its ability to form a labile proteolytically active complex in response to stress stimuli. We demonstrate that Oma1 genetically interacts with other inner membrane-bound quality control proteases. These findings indicate that yeast Oma1 is an important player in IM protein homeostasis and integrity by acting in concert with other intramitochondrial quality control components.

Indexed as

ProteolysisElectron Transport Complex IVHomeostasisMetalloproteasesMitochondriaOxidative StressSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsCox1 protein, S cerevisiaeElectron Transport Complex IVMetalloproteasesOma1 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsGeneticsMetalloproteaseMitochondriaMitochondrial StressOma1Oxidative StressProteasesYeast

Identifiers

PMID24648523
PMCPMC4036336

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Registered trials

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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.