ArticleEMBO reports2004
Membrane protein turnover by the m-AAA protease in mitochondria depends on the transmembrane domains of its subunits.
Article in EMBO reports, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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.
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.
Who cites it
22 citing papers in PubMed, 51 citations in OpenAlex.
- Molecular mechanisms of mitochondrial AAA+ proteases.The Journal of biological chemistry · 2026Review
- Membrane-embedded polar residues target membrane proteins for degradation by the quality control protease FtsH.Nature communications · 2026Article
- Bulk and selective autophagy cooperate to remodel a fungal proteome in response to changing nutrient availability.Cell reports · 2025Article
- Pharmacological Progress of Mitophagy Regulation.Current neuropharmacology · 2023Article
- Article
- The AAA ATPase Afg1 preserves mitochondrial fidelity and cellular health by maintaining mitochondrial matrix proteostasis.Journal of cell science · 2018Article
- Dissecting Substrate Specificities of the Mitochondrial AFG3L2 Protease.Biochemistry · 2018Article
- Molecular insights into theThe Journal of biological chemistry · 2017Article
- Msp1 Is a Membrane Protein Dislocase for Tail-Anchored Proteins.Molecular cell · 2017Article
- Multifunctional Mitochondrial AAA Proteases.Frontiers in molecular biosciences · 2017Review
- Mitochondrial protein quality control: the mechanisms guarding mitochondrial health.Antioxidants & redox signaling · 2015Review
- Mitochondrial protein quality control in health and disease.British journal of pharmacology · 2014Review
- NMR structure and MD simulations of the AAA protease intermembrane space domain indicates peripheral membrane localization within the hexaoligomer.FEBS letters · 2013Article
- Dislocation by the m-AAA protease increases the threshold hydrophobicity for retention of transmembrane helices in the inner membrane of yeast mitochondria.The Journal of biological chemistry · 2013Article
- Dissecting stop transfer versus conservative sorting pathways for mitochondrial inner membrane proteins in vivo.The Journal of biological chemistry · 2013Article
- A mitochondrial-focused genetic interaction map reveals a scaffold-like complex required for inner membrane organization in mitochondria.The Journal of cell biology · 2011Article
- Quality control of mitochondrial proteostasis.Cold Spring Harbor perspectives in biology · 2011Review
- Electron cryomicroscopy structure of a membrane-anchored mitochondrial AAA protease.The Journal of biological chemistry · 2011Article
- Identification and characterization of high molecular weight complexes formed by matrix AAA proteases and prohibitins in mitochondria of Arabidopsis thaliana.The Journal of biological chemistry · 2010Article
- Identification of novel oxidized protein substrates and physiological partners of the mitochondrial ATP-dependent Lon-like protease Pim1.The Journal of biological chemistry · 2010Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
AAA proteases are membrane-bound ATP-dependent proteases that are present in eubacteria, mitochondria and chloroplasts and that can degrade membrane proteins. Recent evidence suggests dislocation of membrane-embedded substrates for proteolysis to occur in a hydrophilic environment; however, next to nothing is known about the mechanism of this process. Here, we have analysed the role of the membrane-spanning domains of Yta10 and Yta12, which are conserved subunits of the hetero-oligomeric m-AAA protease in the mitochondria of Saccharomyces cerevisiae. We demonstrate that the m-AAA protease retains proteolytic activity after deletion of the transmembrane segments of either Yta10 or Yta12. Although the mutant m-AAA protease is still capable of processing cytochrome c peroxidase and degrading a peripheral membrane protein, proteolysis of integral membrane proteins is impaired. We therefore propose that transmembrane segments of m-AAA protease subunits have a direct role in the dislocation of membrane-embedded substrates.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.