Evidence map›Paper›PMID 26760765›Full record

ArticleOncotarget2016

VDAC3 as a sensor of oxidative state of the intermembrane space of mitochondria: the putative role of cysteine residue modifications.

Simona Reina, Vanessa Checchetto, Rosaria Saletti, Ankit Gupta, Deepti Chaturvedi, Carlo Guardiani, Francesca Guarino, Mariano Andrea Scorciapino, Andrea Magrì, Salvatore Foti and 5 more

Open access · diamondAbstract read
In one paragraph

Article in Oncotarget, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.

0numbers the graph read from it
0cells of the map it votes in
59citing papers in PubMed
6.6field-weighted citation impact, top 3% 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

59 citing papers in PubMed, 84 citations in OpenAlex.

  1. Review
  2. Article
  3. Pathogens (Basel, Switzerland) · 2026
    Article
  4. Article
  5. Article
  6. Review
  7. Review
  8. Developing a Novel and Optimized Yeast Model for Human VDAC Research.International journal of molecular sciences · 2024
    Article
  9. Review
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Mitochondrial quality control in health and cardiovascular diseases.Frontiers in cell and developmental biology · 2023
    Review
  16. Review
  17. Article
  18. Review
  19. Article
  20. 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

15 authors at 4 institutions in 2 countries.

Simona ReinaDepartment of Biomedicine and Biotechnology BIOMETEC, Section of Biology and Genetics, University of Catania, Catania, Italy.
Vanessa ChecchettoDepartment of Biology, University of Padova, Padova, Italy.
Rosaria SalettiDepartment of Biomedical Sciences, University of Padova, Padova, Italy.
Ankit GuptaDepartment of Chemical Sciences, Mass Spectrometry Unit, University of Catania, Catania, Italy.
Deepti ChaturvediDepartment of Chemical Sciences, Mass Spectrometry Unit, University of Catania, Catania, Italy.
Carlo GuardianiMolecular Biophysics Laboratory, Department of Biological Sciences, Indian Institute of Science Education and Research, Bhopal, India.
Francesca GuarinoDepartment of Biomedicine and Biotechnology BIOMETEC, Section of Biology and Genetics, University of Catania, Catania, Italy.
Mariano Andrea ScorciapinoMolecular Biophysics Laboratory, Department of Biological Sciences, Indian Institute of Science Education and Research, Bhopal, India.
Andrea MagrìDepartment of Biomedicine and Biotechnology BIOMETEC, Section of Biology and Genetics, University of Catania, Catania, Italy.
Salvatore FotiCNR Institute of Neurosciences, Padova, Italy.
Matteo CeccarelliDepartment of Chemical Sciences, Mass Spectrometry Unit, University of Catania, Catania, Italy.
Angela Anna MessinaDepartment of Biomedical Sciences, Biochemistry Unit, University of Cagliari, Cagliari, Italy.
Radhakrishnan MahalakshmiDepartment of Biomedical Sciences, University of Padova, Padova, Italy.
Ildiko SzaboNational Institute for Biomembranes and Biosystems, Section of Catania, Catania, Italy.
Vito De PintoDepartment of Biomedicine and Biotechnology BIOMETEC, Section of Biology and Genetics, University of Catania, Catania, Italy.
University of Catania · ITIndian Institute of Science Education and Research, Bhopal · INUniversity of Cagliari · ITNeuroscience Institute · IT

Funding

DBT-Wellcome Trust India Alliance IA/I/14/1/501305
6 · The paper itself

Abstract

Voltage-Dependent Anion selective Channels (VDAC) are pore-forming mitochondrial outer membrane proteins. In mammals VDAC3, the least characterized isoform, presents a set of cysteines predicted to be exposed toward the intermembrane space. We find that cysteines in VDAC3 can stay in different oxidation states. This was preliminary observed when, in our experimental conditions, completely lacking any reducing agent, VDAC3 presented a pattern of slightly different electrophoretic mobilities. This observation holds true both for rat liver mitochondrial VDAC3 and for recombinant and refolded human VDAC3. Mass spectroscopy revealed that cysteines 2 and 8 can form a disulfide bridge in native VDAC3. Single or combined site-directed mutagenesis of cysteines 2, 8 and 122 showed that the protein mobility in SDS-PAGE is influenced by the presence of cysteine and by the redox status. In addition, cysteines 2, 8 and 122 are involved in the stability control of the pore as shown by electrophysiology, complementation assays and chemico-physical characterization. Furthermore, a positive correlation between the pore conductance of the mutants and their ability to complement the growth of porin-less yeast mutant cells was found. Our work provides evidence for a complex oxidation pattern of a mitochondrial protein not directly involved in electron transport. The most likely biological meaning of this behavior is to buffer the ROS load and keep track of the redox level in the inter-membrane space, eventually signaling it through conformational changes.

Indexed as

Amino Acid SequenceAnimalsCysteineElectron TransportElectrophoresis, Polyacrylamide GelEscherichia coliHumansLiverMass SpectrometryMitochondriaMitochondrial Membrane Transport ProteinsMolecular Dynamics SimulationMolecular Sequence DataOxidation-ReductionProtein IsoformsRatsCysteineMitochondrial Membrane Transport ProteinsProtein IsoformsVdac3 protein, ratVoltage-Dependent Anion Channelscysteine oxidationdisulfide bridgemass spectrometrymitochondrial intermembrane spaceVDACs

Identifiers

PMID26760765
PMCPMC4823033
OpenAlexW2236703262

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.