Evidence map›Paper›PMID 26416881›Full record

ArticleMolecular and cellular biology2015

The Oxidation Status of Mic19 Regulates MICOS Assembly.

Paulina Sakowska, Daniel C Jans, Karthik Mohanraj, Dietmar Riedel, Stefan Jakobs, Agnieszka Chacinska

Open access · bronzeAbstract read
In one paragraph

Article in Molecular and cellular biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
2.6field-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

33 citing papers in PubMed, 57 citations in OpenAlex.

  1. Review
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  8. Molecular machineries shaping the mitochondrial inner membrane.Nature reviews. Molecular cell biology · 2025
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  11. HThe Journal of biological chemistry · 2025
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  20. Mechanisms of mitochondrial respiratory adaptation.Nature reviews. Molecular cell biology · 2022
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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

6 authors at 4 institutions in 2 countries.

Paulina SakowskaInternational Institute of Molecular and Cell Biology, Warsaw, Poland.
Daniel C JansDepartment of NanoBiophotonics, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany Department of Neurology, University Medical Center, Göttingen, Germany.
Karthik MohanrajInternational Institute of Molecular and Cell Biology, Warsaw, Poland.
Dietmar RiedelElectron Microscopy Facility, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany.
Stefan JakobsDepartment of NanoBiophotonics, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany Department of Neurology, University Medical Center, Göttingen, Germany.
Agnieszka ChacinskaInternational Institute of Molecular and Cell Biology, Warsaw, Poland achacinska@iimcb.gov.pl.
International Institute of Molecular and Cell Biology · PLMax Planck Institute for Biophysical Chemistry · DEUniversitätsmedizin Göttingen · DEUniversity of Göttingen · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The function of mitochondria depends on the proper organization of mitochondrial membranes. The morphology of the inner membrane is regulated by the recently identified mitochondrial contact site and crista organizing system (MICOS) complex. MICOS mutants exhibit alterations in crista formation, leading to mitochondrial dysfunction. However, the mechanisms that underlie MICOS regulation remain poorly understood. MIC19, a peripheral protein of the inner membrane and component of the MICOS complex, was previously reported to be required for the proper function of MICOS in maintaining the architecture of the inner membrane. Here, we show that human and Saccharomyces cerevisiae MIC19 proteins undergo oxidation in mitochondria and require the mitochondrial intermembrane space assembly (MIA) pathway, which couples the oxidation and import of mitochondrial intermembrane space proteins for mitochondrial localization. Detailed analyses identified yeast Mic19 in two different redox forms. The form that contains an intramolecular disulfide bond is bound to Mic60 of the MICOS complex. Mic19 oxidation is not essential for its integration into the MICOS complex but plays a role in MICOS assembly and the maintenance of the proper inner membrane morphology. These findings suggest that Mic19 is a redox-dependent regulator of MICOS function.

Indexed as

Cell LineHEK293 CellsHumansMembrane ProteinsMitochondriaMitochondrial MembranesMitochondrial ProteinsMultiprotein ComplexesOxidation-ReductionProtein BindingRNA InterferenceRNA, Small InterferingSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsCHCHD3 protein, humanMembrane ProteinsMIC19 protein, S cerevisiaeMitochondrial ProteinsMultiprotein ComplexesRNA, Small InterferingSaccharomyces cerevisiae Proteins

Identifiers

PMID26416881
PMCPMC4648825
OpenAlexW2179054579

What OpenQuestion holds

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LicenceCC BY-NC-SA
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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.