Evidence map›Paper›PMID 28916712›Full record

ArticleThe Journal of cell biology2017

Identification of new channels by systematic analysis of the mitochondrial outer membrane.

Vivien Krüger, Thomas Becker, Lars Becker, Malayko Montilla-Martinez, Lars Ellenrieder, F-Nora Vögtle, Helmut E Meyer, Michael T Ryan, Nils Wiedemann, Bettina Warscheid and 3 more

Abstract read
In one paragraph

Article in The Journal of cell biology, 2017. 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
–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

36 citing papers in PubMed.

  1. Redox signals and oxidative stress in the control of mitochondrial protein import.Protein science : a publication of the Protein Society · 2026
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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

13 authors.

Vivien KrügerDivision of Biophysics, School of Biology/Chemistry, University of Osnabrück, Osnabrück, Germany.
Thomas BeckerInstitute of Biochemistry and Molecular Biology, ZBMZ, Faculty of Medicine, University of Freiburg, Freiburg, Germany.
Lars BeckerDivision of Biophysics, School of Biology/Chemistry, University of Osnabrück, Osnabrück, Germany.
Malayko Montilla-MartinezDivision of Biophysics, School of Biology/Chemistry, University of Osnabrück, Osnabrück, Germany.
Lars EllenriederInstitute of Biochemistry and Molecular Biology, ZBMZ, Faculty of Medicine, University of Freiburg, Freiburg, Germany.
F-Nora VögtleInstitute of Biochemistry and Molecular Biology, ZBMZ, Faculty of Medicine, University of Freiburg, Freiburg, Germany.
Helmut E MeyerLeibniz-Institut für Analytische Wissenschaften-ISAS-e.V., Dortmund, Germany.ORCID 0000-0003-4442-457X
Michael T RyanDepartment of Biochemistry and Molecular Biology, Monash Biomedicine Discovery Institute, Monash University, Melbourne, Australia.ORCID 0000-0003-2586-8829
Nils WiedemannInstitute of Biochemistry and Molecular Biology, ZBMZ, Faculty of Medicine, University of Freiburg, Freiburg, Germany.
Bettina WarscheidBIOSS Centre for Biological Signalling Studies, University of Freiburg, Freiburg, Germany.
Nikolaus PfannerInstitute of Biochemistry and Molecular Biology, ZBMZ, Faculty of Medicine, University of Freiburg, Freiburg, Germany nikolaus.pfanner@biochemie.uni-freiburg.de.ORCID 0000-0003-2136-2046
Richard WagnerDivision of Biophysics, School of Biology/Chemistry, University of Osnabrück, Osnabrück, Germany ri.wagner@jacobs-university.de.
Chris MeisingerInstitute of Biochemistry and Molecular Biology, ZBMZ, Faculty of Medicine, University of Freiburg, Freiburg, Germany.

Funding

European Research Council 648235
6 · The paper itself

Abstract

The mitochondrial outer membrane is essential for communication between mitochondria and the rest of the cell and facilitates the transport of metabolites, ions, and proteins. All mitochondrial outer membrane channels known to date are β-barrel membrane proteins, including the abundant voltage-dependent anion channel and the cation-preferring protein-conducting channels Tom40, Sam50, and Mdm10. We analyzed outer membrane fractions of yeast mitochondria and identified four new channel activities: two anion-preferring channels and two cation-preferring channels. We characterized the cation-preferring channels at the molecular level. The mitochondrial import component Mim1 forms a channel that is predicted to have an α-helical structure for protein import. The short-chain dehydrogenase-related protein Ayr1 forms an NADPH-regulated channel. We conclude that the mitochondrial outer membrane contains a considerably larger variety of channel-forming proteins than assumed thus far. These findings challenge the traditional view of the outer membrane as an unspecific molecular sieve and indicate a higher degree of selectivity and regulation of metabolite fluxes at the mitochondrial boundary.

Indexed as

Biological TransportCarboxylic Ester HydrolasesMembrane ProteinsMitochondriaMitochondrial MembranesNADPProtein Conformation, alpha-HelicalSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsAyr1 protein, S cerevisiaeCarboxylic Ester HydrolasesMembrane ProteinsMIM1 protein, S cerevisiaeNADPSaccharomyces cerevisiae Proteins

Identifiers

PMID28916712
PMCPMC5674900

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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.