Evidence map›Paper›PMID 22461620›Full record

ArticleThe Journal of biological chemistry2012

Saccharomyces cerevisiae porin pore forms complexes with mitochondrial outer membrane proteins Om14p and Om45p.

Susann Lauffer, Katrin Mäbert, Cornelia Czupalla, Theresia Pursche, Bernard Hoflack, Gerhard Rödel, Udo Krause-Buchholz

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.2field-weighted citation impact, top 22% 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

15 citing papers in PubMed, 38 citations in OpenAlex.

  1. Nascent mitochondrial proteins initiate the localized condensation of cytosolic protein aggregates on the mitochondrial surface.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  2. Article
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  7. Article
  8. Article
  9. Review
  10. How lipids modulate mitochondrial protein import.Journal of bioenergetics and biomembranes · 2016
    Review
  11. Article
  12. Role of membrane contact sites in protein import into mitochondria.Protein science : a publication of the Protein Society · 2015
    Review
  13. Article
  14. Article
  15. The mitochondrial protein OM45 is exposed to the cytosol.The Journal of biological chemistry · 2012
    Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors at 1 institution in 1 country.

Susann LaufferInstitute of Genetics, Technische Universität Dresden, 01062 Dresden and. Electronic address: Susann.Lauffer@tu-dresden.de.
Katrin MäbertInstitute of Genetics, Technische Universität Dresden, 01062 Dresden and.
Cornelia CzupallaBiotechnology Center, Technische Universität Dresden, Tatzberg 47/49, 01307 Dresden, Germany.
Theresia PurscheBiotechnology Center, Technische Universität Dresden, Tatzberg 47/49, 01307 Dresden, Germany.
Bernard HoflackBiotechnology Center, Technische Universität Dresden, Tatzberg 47/49, 01307 Dresden, Germany.
Gerhard RödelInstitute of Genetics, Technische Universität Dresden, 01062 Dresden and.
Udo Krause-BuchholzInstitute of Genetics, Technische Universität Dresden, 01062 Dresden and.
TU Dresden · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Numerous transport processes occur between the two mitochondrial (mt) membranes due to the diverse functions and metabolic processes of the mt organelle. The metabolite and ion transport through the mt outer membrane (OM) is widely assumed to be mediated by the porin pore, whereas in the mt inner membrane (IM) specific carriers are responsible for transport processes. Here, we provide evidence by means of Blue Native (BN)-PAGE analysis, co-immunoprecipitation, and tandem affinity purification that the two mt OM proteins Om14p and Om45p associate with the porin pore. Porin molecules seem to assemble independently to build the core unit. A subpopulation of these core units interacts with Om14p and Om45p. With preparative tandem affinity purification followed by MS analysis, we could identify interaction partners of this OM complex, which are mainly localized within the mt IM and function as carriers for diverse molecules. We propose a model for the role of the two OM proteins in addressing the porin pore to bind to specific channels in the mt IM to facilitate transport of metabolites.

Indexed as

Models, BiologicalBiological TransportMitochondrial MembranesMitochondrial ProteinsPorinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsMitochondrial ProteinsPorinsSaccharomyces cerevisiae Proteins

Identifiers

PMID22461620
PMCPMC3366824
OpenAlexW2080852048

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.