Evidence map›Paper›PMID 33121519›Full record

ArticleBMC biology2020

The selectivity filter of the mitochondrial protein import machinery.

Sebastian Kreimendahl, Jan Schwichtenberg, Kathrin Günnewig, Lukas Brandherm, Joachim Rassow

Open access · goldAbstract read
In one paragraph

Article in BMC biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.3field-weighted citation impact, top 19% 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

17 citing papers in PubMed, 24 citations in OpenAlex.

  1. From the cytosol to the inner membrane: biogenesis of the mitochondrial carrier family.Protein science : a publication of the Protein Society · 2026
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  7. Mechanisms of mitochondrial respiratory adaptation.Nature reviews. Molecular cell biology · 2022
    Review
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  10. Article
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  12. Article
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  14. Targeting and Insertion of Membrane Proteins in Mitochondria.Frontiers in cell and developmental biology · 2021
    Review
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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

5 authors at 2 institutions in 1 country.

Sebastian KreimendahlInstitute for Biochemistry and Pathobiochemistry, Ruhr-University Bochum, 44780, Bochum, Germany.
Jan SchwichtenbergInstitute for Biochemistry and Pathobiochemistry, Ruhr-University Bochum, 44780, Bochum, Germany.
Kathrin GünnewigInstitute for Biochemistry and Pathobiochemistry, Ruhr-University Bochum, 44780, Bochum, Germany.
Lukas BrandhermInstitute for Biochemistry and Pathobiochemistry, Ruhr-University Bochum, 44780, Bochum, Germany.
Joachim RassowInstitute for Biochemistry and Pathobiochemistry, Ruhr-University Bochum, 44780, Bochum, Germany. joachim.rassow@rub.de.ORCID 0000-0002-1219-2623
Ruhr University Bochum · DEUniversity Hospitals of the Ruhr-University of Bochum · DE

Funding

Deutsche Forschungsgemeinschaft RA 702/4-1Medizinische Fakultät, Ruhr-Universität Bochum FoRUM-Program (F813R2-2014)
6 · The paper itself

Abstract

backgroundThe uptake of newly synthesized nuclear-encoded mitochondrial proteins from the cytosol is mediated by a complex of mitochondrial outer membrane proteins comprising a central pore-forming component and associated receptor proteins. Distinct fractions of proteins initially bind to the receptor proteins and are subsequently transferred to the pore-forming component for import. The aim of this study was the identification of the decisive elements of this machinery that determine the specific selection of the proteins that should be imported.

resultsWe identified the essential internal targeting signal of the members of the mitochondrial metabolite carrier proteins, the largest protein family of the mitochondria, and we investigated the specific recognition of this signal by the protein import machinery at the mitochondrial outer surface. We found that the outer membrane import receptors facilitated the uptake of these proteins, and we identified the corresponding binding site, marked by cysteine C141 in the receptor protein Tom70. However, in tests both in vivo and in vitro, the import receptors were neither necessary nor sufficient for specific recognition of the targeting signals. Although these signals are unrelated to the amino-terminal presequences that mediate the targeting of other mitochondrial preproteins, they were found to resemble presequences in their strict dependence on a content of positively charged residues as a prerequisite of interactions with the import pore.

conclusionsThe general import pore of the mitochondrial outer membrane appears to represent not only the central channel of protein translocation but also to form the decisive general selectivity filter in the uptake of the newly synthesized mitochondrial proteins.

Indexed as

Protein TransportFungal ProteinsMitochondrial ADP, ATP TranslocasesMitochondrial ProteinsNeurospora crassaFungal ProteinsMitochondrial ADP, ATP TranslocasesMitochondrial ProteinsChaperonesIon channelMitochondriaProtein targetingSelectivity filterTom40Tom70TOM complex

Identifiers

PMID33121519
PMCPMC7596997
OpenAlexW3096795536

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.