Evidence map›Paper›PMID 17245427›Full record

ArticleThe EMBO journal2007

m-AAA protease-driven membrane dislocation allows intramembrane cleavage by rhomboid in mitochondria.

Takashi Tatsuta, Steffen Augustin, Mark Nolden, Björn Friedrichs, Thomas Langer

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing papers in PubMed
4.7field-weighted citation impact, top 4% 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

48 citing papers in PubMed, 118 citations in OpenAlex.

  1. Molecular mechanisms of mitochondrial AAA+ proteases.The Journal of biological chemistry · 2026
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  15. Molecular insights into theThe Journal of biological chemistry · 2017
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  19. Multifunctional Mitochondrial AAA Proteases.Frontiers in molecular biosciences · 2017
    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 at 1 institution in 1 country.

Takashi TatsutaInstitute for Genetics and Center for Molecular Medicine (CMMC), University of Cologne, Cologne, Germany.
Steffen Augustin
Mark Nolden
Björn Friedrichs
Thomas Langer
University of Cologne · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Maturation of cytochrome c peroxidase (Ccp1) in mitochondria occurs by the subsequent action of two conserved proteases in the inner membrane: the m-AAA protease, an ATP-dependent protease degrading misfolded proteins and mediating protein processing, and the rhomboid protease Pcp1, an intramembrane cleaving peptidase. Neither the determinants preventing complete proteolysis of certain substrates by the m-AAA protease, nor the obligatory requirement of the m-AAA protease for rhomboid cleavage is currently understood. Here, we describe an intimate and unexpected functional interplay of both proteases. The m-AAA protease mediates the ATP-dependent membrane dislocation of Ccp1 independent of its proteolytic activity. It thereby ensures the correct positioning of Ccp1 within the membrane bilayer allowing intramembrane cleavage by rhomboid. Decreasing the hydrophobicity of the Ccp1 transmembrane segment facilitates its dislocation from the membrane and renders rhomboid cleavage m-AAA protease-independent. These findings reveal for the first time a non-proteolytic function of the m-AAA protease during mitochondrial biogenesis and rationalise the requirement of a preceding step for intramembrane cleavage by rhomboid.

Indexed as

Protein Processing, Post-TranslationalAmino Acid SequenceConserved SequenceCytochrome-c PeroxidaseFungal ProteinsMembrane FluidityMetalloendopeptidasesMitochondriaModels, BiologicalMolecular Sequence DataMutant ProteinsProtein FoldingProtein Structure, TertiaryProtein TransportSaccharomyces cerevisiae ProteinsSerine EndopeptidasesCytochrome-c PeroxidaseFungal Proteinsm-AAA proteasesMetalloendopeptidasesMutant ProteinsPcp1 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsSerine Endopeptidases

Identifiers

PMID17245427
PMCPMC1783466
OpenAlexW2127967647

What OpenQuestion holds

Textmetadata
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.