Evidence map›Paper›PMID 25124039›Full record

ArticleThe Journal of biological chemistry2014

The mitochondrial ADP/ATP carrier associates with the inner membrane presequence translocase in a stoichiometric manner.

Carola S Mehnert, Heike Rampelt, Michael Gebert, Silke Oeljeklaus, Sandra G Schrempp, Lioba Kochbeck, Bernard Guiard, Bettina Warscheid, Martin van der Laan

Open access · hybridAbstract 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 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.7field-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

16 citing papers in PubMed, 31 citations in OpenAlex.

  1. Review
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  7. Mitochondrial proteins: from biogenesis to functional networks.Nature reviews. Molecular cell biology · 2019
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  16. Role of membrane contact sites in protein import into mitochondria.Protein science : a publication of the Protein Society · 2015
    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

9 authors at 2 institutions in 2 countries.

Carola S MehnertInstitut für Biochemie und Molekularbiologie, ZBMZ, Universität Freiburg, 79104 Freiburg, Germany; Fakultät für Biologie, Universität Freiburg, 79104 Freiburg, Germany.
Heike RampeltInstitut für Biochemie und Molekularbiologie, ZBMZ, Universität Freiburg, 79104 Freiburg, Germany.
Michael GebertInstitut für Biochemie und Molekularbiologie, ZBMZ, Universität Freiburg, 79104 Freiburg, Germany; Fakultät für Biologie, Universität Freiburg, 79104 Freiburg, Germany.
Silke OeljeklausInstitut für Biologie II, Fakultät für Biologie, Funktionelle Proteomik, and Universität Freiburg, 79104 Freiburg, Germany; BIOSS Centre for Biological Signaling Studies, Universität Freiburg, 79104 Freiburg, Germany and.
Sandra G SchremppInstitut für Biochemie und Molekularbiologie, ZBMZ, Universität Freiburg, 79104 Freiburg, Germany; Fakultät für Biologie, Universität Freiburg, 79104 Freiburg, Germany.
Lioba KochbeckInstitut für Biochemie und Molekularbiologie, ZBMZ, Universität Freiburg, 79104 Freiburg, Germany.
Bernard GuiardCentre de Génétique Moléculaire, CNRS, 91190 Gif-sur-Yvette, France.
Bettina WarscheidInstitut für Biologie II, Fakultät für Biologie, Funktionelle Proteomik, and Universität Freiburg, 79104 Freiburg, Germany; BIOSS Centre for Biological Signaling Studies, Universität Freiburg, 79104 Freiburg, Germany and.
Martin van der LaanInstitut für Biochemie und Molekularbiologie, ZBMZ, Universität Freiburg, 79104 Freiburg, Germany; BIOSS Centre for Biological Signaling Studies, Universität Freiburg, 79104 Freiburg, Germany and. Electronic address: martin.van.der.laan@biochemie.uni-freiburg.de.
University of Freiburg · DECentre de Génétique Moléculaire · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The majority of mitochondrial proteins are synthesized with amino-terminal signal sequences. The presequence translocase of the inner membrane (TIM23 complex) mediates the import of these preproteins. The essential TIM23 core complex closely cooperates with partner protein complexes like the presequence translocase-associated import motor and the respiratory chain. The inner mitochondrial membrane also contains a large number of metabolite carriers, but their association with preprotein translocases has been controversial. We performed a comprehensive analysis of the TIM23 interactome based on stable isotope labeling with amino acids in cell culture. Subsequent biochemical studies on identified partner proteins showed that the mitochondrial ADP/ATP carrier associates with the membrane-embedded core of the TIM23 complex in a stoichiometric manner, revealing an unexpected connection of mitochondrial protein biogenesis to metabolite transport. Our data indicate that direct TIM23-AAC coupling may support preprotein import into mitochondria when respiratory activity is low.

Indexed as

Membrane Transport ProteinsMitochondrial MembranesMitochondrial Precursor Protein Import Complex ProteinsMitochondrial ProteinsMultiprotein ComplexesProtein TransportSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsMembrane Transport ProteinsMitochondrial Precursor Protein Import Complex ProteinsMitochondrial ProteinsMultiprotein ComplexesSaccharomyces cerevisiae ProteinsTIM23 protein, S cerevisiaeenergy MetabolismMembrane ProteinMetabolite CarrierMitochondriaMitochondrial Protein ImportProtein TranslocationRespiratory ChainSILACTIM23 Complex

Identifiers

PMID25124039
PMCPMC4175365
OpenAlexW1963822045

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.