Evidence map›Paper›PMID 23625917›Full record

ArticleThe Journal of biological chemistry2013

Role of phosphatidylethanolamine in the biogenesis of mitochondrial outer membrane proteins.

Thomas Becker, Susanne E Horvath, Lena Böttinger, Natalia Gebert, Günther Daum, Nikolaus Pfanner

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
2.5field-weighted citation impact, top 10% 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

44 citing papers in PubMed, 74 citations in OpenAlex.

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  6. Structures ofProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  7. Molecular insights into human phosphatidylserine synthase 2 and its regulation of SREBP pathways.Proceedings of the National Academy of Sciences of the United States of America · 2025
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  20. Structural basis of Tom20 and Tom22 cytosolic domains as the human TOM complex receptors.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
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

6 authors at 2 institutions in 2 countries.

Thomas BeckerInstitut für Biochemie und Molekularbiologie, ZBMZ, 79104 Freiburg, Germany; BIOSS Centre for Biological Signalling Studies, 79104 Freiburg, Germany.
Susanne E HorvathInstitut für Biochemie und Molekularbiologie, ZBMZ, 79104 Freiburg, Germany; Institut für Biochemie, Technische Universität Graz, A-8010 Graz, Austria.
Lena BöttingerInstitut für Biochemie und Molekularbiologie, ZBMZ, 79104 Freiburg, Germany; Fakultät für Biologie, Universität Freiburg, 79104 Freiburg, Germany.
Natalia GebertInstitut für Biochemie und Molekularbiologie, ZBMZ, 79104 Freiburg, Germany.
Günther DaumInstitut für Biochemie, Technische Universität Graz, A-8010 Graz, Austria. Electronic address: guenther.daum@tugraz.at.
Nikolaus PfannerInstitut für Biochemie und Molekularbiologie, ZBMZ, 79104 Freiburg, Germany; BIOSS Centre for Biological Signalling Studies, 79104 Freiburg, Germany. Electronic address: nikolaus.pfanner@biochemie.uni-freiburg.de.
University of Freiburg · DEGraz University of Technology · AT

Funding

Austrian Science Fund FWF P 21429
6 · The paper itself

Abstract

The mitochondrial outer membrane contains proteinaceous machineries for the import and assembly of proteins, including TOM (translocase of the outer membrane) and SAM (sorting and assembly machinery). It has been shown that the dimeric phospholipid cardiolipin is required for the stability of TOM and SAM complexes and thus for the efficient import and assembly of β-barrel proteins and some α-helical proteins of the outer membrane. Here, we report that mitochondria deficient in phosphatidylethanolamine (PE), the second non-bilayer-forming phospholipid, are impaired in the biogenesis of β-barrel proteins, but not of α-helical outer membrane proteins. The stability of TOM and SAM complexes is not disturbed by the lack of PE. By dissecting the import steps of β-barrel proteins, we show that an early import stage involving translocation through the TOM complex is affected. In PE-depleted mitochondria, the TOM complex binds precursor proteins with reduced efficiency. We conclude that PE is required for the proper function of the TOM complex.

Indexed as

Carrier ProteinsMembrane ProteinsMitochondriaMitochondrial Precursor Protein Import Complex ProteinsMitochondrial ProteinsPhosphatidylethanolaminesProtein Structure, SecondarySaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsCarrier ProteinsMembrane ProteinsMitochondrial Precursor Protein Import Complex ProteinsMitochondrial ProteinsphosphatidylethanolaminePhosphatidylethanolaminesSaccharomyces cerevisiae ProteinsMembrane BiogenesisMitochondriaPhospholipidProtein TargetingProtein Translocation

Identifiers

PMID23625917
PMCPMC3675581
OpenAlexW2092503084

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.