Evidence map›Paper›PMID 26915330›Full record

ArticleJournal of cellular and molecular medicine2016

New protein-protein interactions of mitochondrial connexin 43 in mouse heart.

Amanda Denuc, Estefanía Núñez, Enrique Calvo, Marta Loureiro, Elisabet Miro-Casas, Adela Guarás, Jesús Vázquez, David Garcia-Dorado

Open access · goldAbstract read
In one paragraph

Article in Journal of cellular and molecular medicine, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
3.8field-weighted citation impact, top 7% 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

36 citing papers in PubMed, 62 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Review
  7. Review
  8. Article
  9. Role of astrocytes connexins - pannexins in acute brain injury.Neurotherapeutics : the journal of the American Society for Experimental NeuroTherapeutics · 2025
    Review
  10. Review
  11. Review
  12. Article
  13. Review
  14. Review
  15. Article
  16. Intercellular delivery of therapeutic oligonucleotides.Journal of drug delivery science and technology · 2022
    Article
  17. Article
  18. Article
  19. Review
  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

8 authors at 2 institutions in 1 country.

Amanda DenucVall d'Hebron University Hospital and Reseach Institute, Universitat Autònoma de Barcelona, Barcelona, Spain.
Estefanía NúñezCentro Nacional de Investigaciones Cardiovasculares Carlos III, Madrid, Spain.
Enrique CalvoCentro Nacional de Investigaciones Cardiovasculares Carlos III, Madrid, Spain.
Marta LoureiroCentro Nacional de Investigaciones Cardiovasculares Carlos III, Madrid, Spain.
Elisabet Miro-CasasVall d'Hebron University Hospital and Reseach Institute, Universitat Autònoma de Barcelona, Barcelona, Spain.
Adela GuarásCentro Nacional de Investigaciones Cardiovasculares Carlos III, Madrid, Spain.
Jesús VázquezCentro Nacional de Investigaciones Cardiovasculares Carlos III, Madrid, Spain.
David Garcia-DoradoVall d'Hebron University Hospital and Reseach Institute, Universitat Autònoma de Barcelona, Barcelona, Spain.
Spanish National Centre for Cardiovascular Research · ESUniversitat Autònoma de Barcelona · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Connexin 43 (Cx43), the gap junction protein involved in cell-to-cell coupling in the heart, is also present in the subsarcolemmal fraction of cardiomyocyte mitochondria. It has been described to regulate mitochondrial potassium influx and respiration and to be important for ischaemic preconditioning protection, although the molecular effectors involved are not fully characterized. In this study, we looked for potential partners of mitochondrial Cx43 in an attempt to identify new molecular pathways for cardioprotection. Mass spectrometry analysis of native immunoprecipitated mitochondrial extracts showed that Cx43 interacts with several proteins related with mitochondrial function and metabolism. Among them, we selected for further analysis only those present in the subsarcolemmal mitochondrial fraction and known to be related with the respiratory chain. Apoptosis-inducing factor (AIF) and the beta-subunit of the electron-transfer protein (ETFB), two proteins unrelated to date with Cx43, fulfilled these conditions, and their interaction with Cx43 was proven by direct and reverse co-immunoprecipitation. Furthermore, a previously unknown molecular interaction between AIF and ETFB was established, and protein content and sub-cellular localization appeared to be independent from the presence of Cx43. Our results identify new protein-protein interactions between AIF-Cx43, ETFB-Cx43 and AIF-ETFB as possible players in the regulation of the mitochondrial redox state.

Indexed as

AnimalsApoptosis Inducing FactorConnexin 43Electron-Transferring FlavoproteinsFemaleGene Expression RegulationImmunoprecipitationMaleMiceMice, TransgenicMitochondria, HeartMyocytes, CardiacOxidation-ReductionProtein BindingProtein Interaction MappingProtein SubunitsAIFM1 protein, mouseApoptosis Inducing FactorConnexin 43Electron-Transferring FlavoproteinsGJA1 protein, mouseProtein Subunitsapoptosis-inducing factorcardiomyocyteconnexin 43electron-transfer proteinmitochondria

Identifiers

PMID26915330
PMCPMC4831365
OpenAlexW2275210540

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.