Evidence map›Paper›PMID 25956655›Full record

ArticleNucleic acids research2015

Mitochondrial translocation of APE1 relies on the MIA pathway.

Arianna Barchiesi, Michal Wasilewski, Agnieszka Chacinska, Gianluca Tell, Carlo Vascotto

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
3.0field-weighted citation impact, top 9% 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

35 citing papers in PubMed, 63 citations in OpenAlex.

  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

5 authors at 2 institutions in 2 countries.

Arianna BarchiesiDepartment of Medical and Biological Sciences, University of Udine, Udine 33100, Italy.
Michal WasilewskiInternational Institute of Molecular and Cell Biology, Warsaw, 02-109, Poland.
Agnieszka ChacinskaInternational Institute of Molecular and Cell Biology, Warsaw, 02-109, Poland.
Gianluca TellDepartment of Medical and Biological Sciences, University of Udine, Udine 33100, Italy.
Carlo VascottoDepartment of Medical and Biological Sciences, University of Udine, Udine 33100, Italy carlo.vascotto@uniud.it.
University of Udine · ITInternational Institute of Molecular and Cell Biology · PL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

APE1 is a multifunctional protein with a fundamental role in repairing nuclear and mitochondrial DNA lesions caused by oxidative and alkylating agents. Unfortunately, comprehensions of the mechanisms regulating APE1 intracellular trafficking are still fragmentary and contrasting. Recent data demonstrate that APE1 interacts with the mitochondrial import and assembly protein Mia40 suggesting the involvement of a redox-assisted mechanism, dependent on the disulfide transfer system, to be responsible of APE1 trafficking into the mitochondria. The MIA pathway is an import machinery that uses a redox system for cysteine enriched proteins to drive them in this compartment. It is composed by two main proteins: Mia40 is the oxidoreductase that catalyzes the formation of the disulfide bonds in the substrate, while ALR reoxidizes Mia40 after the import. In this study, we demonstrated that: (i) APE1 and Mia40 interact through disulfide bond formation; and (ii) Mia40 expression levels directly affect APE1's mitochondrial translocation and, consequently, play a role in the maintenance of mitochondrial DNA integrity. In summary, our data strongly support the hypothesis of a redox-assisted mechanism, dependent on Mia40, in controlling APE1 translocation into the mitochondrial inner membrane space and thus highlight the role of this protein transport pathway in the maintenance of mitochondrial DNA stability and cell survival.

Indexed as

Cell Line, TumorCysteineDisulfidesDNA-(Apurinic or Apyrimidinic Site) LyaseDNA DamageDNA, MitochondrialDNA RepairHumansMitochondriaMitochondrial Membrane Transport ProteinsMitochondrial Precursor Protein Import Complex ProteinsMutationProtein StabilityProtein TransportAPEX1 protein, humanCHCHD4 protein, humanCysteineDisulfidesDNA-(Apurinic or Apyrimidinic Site) LyaseDNA, MitochondrialMitochondrial Membrane Transport ProteinsMitochondrial Precursor Protein Import Complex Proteins

Identifiers

PMID25956655
PMCPMC4477663
OpenAlexW1559246450

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Registered trials

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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.