Evidence map›Paper›PMID 23590695›Full record

ArticleJournal of proteome research2013

The liver connexin32 interactome is a novel plasma membrane-mitochondrial signaling nexus.

Stephanie L Fowler, Mark Akins, Hu Zhou, Daniel Figeys, Steffany A L Bennett

Open access · bronzeAbstract read
In one paragraph

Article in Journal of proteome research, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
2.7field-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

28 citing papers in PubMed, 62 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Review
  6. Mechanisms of Connexin Regulating Peptides.International journal of molecular sciences · 2021
    Review
  7. Article
  8. Article
  9. Article
  10. Shear stress augments mitochondrial ATP generation that triggers ATP release and CaAmerican journal of physiology. Heart and circulatory physiology · 2018
    Article
  11. Review
  12. A Cell Junctional Protein Network Associated with Connexin-26.International journal of molecular sciences · 2018
    Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Connexin-based signaling and drug-induced hepatotoxicity.Journal of clinical and translational research · 2017
    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

5 authors at 2 institutions in 2 countries.

Stephanie L FowlerNeural Regeneration Laboratory, Department of Biochemistry, Microbiology and Immunology, University of Ottawa, Ottawa, Ontario, Canada.
Mark Akins
Hu Zhou
Daniel Figeys
Steffany A L Bennett
Chinese Academy of Sciences · CNUniversity of Ottawa · CA

Funding

Canadian Institutes of Health Research MOP 62826Canadian Institutes of Health Research TGF 96121
6 · The paper itself

Abstract

Connexins are the structural subunits of gap junctions and act as protein platforms for signaling complexes. Little is known about tissue-specific connexin signaling nexuses, given significant challenges associated with affinity-purifying endogenous channel complexes to the level required for interaction analyses. Here, we used multiple subcellular fractionation techniques to isolate connexin32-enriched membrane microdomains from murine liver. We show, for the first time, that connexin32 localizes to both the plasma membrane and inner mitochondrial membrane of hepatocytes. Using a combination of immunoprecipitation-high throughput mass spectrometry, reciprocal co-IP, and subcellular fractionation methodologies, we report a novel interactome validated using null mutant controls. Eighteen connexin32 interacting proteins were identified. The majority represent resident mitochondrial proteins, a minority represent plasma membrane, endoplasmic reticulum, or cytoplasmic partners. In particular, connexin32 interacts with connexin26 and the mitochondrial protein, sideroflexin-1, at the plasma membrane. Connexin32 interaction enhances connexin26 stability. Converging bioinformatic, biochemical, and confocal analyses support a role for connexin32 in transiently tethering mitochondria to connexin32-enriched plasma membrane microdomains through interaction with proteins in the outer mitochondrial membrane, including sideroflexin-1. Complex formation increases the pool of sideroflexin-1 that is present at the plasma membrane. Together, these data identify a novel plasma membrane/mitochondrial signaling nexus in the connexin32 interactome.

Indexed as

Signal TransductionAnimalsCation Transport ProteinsCell FractionationCell MembraneConnexin 26ConnexinsGap Junction beta-1 ProteinGap JunctionsGene Expression RegulationHepatocytesLiverMiceMice, KnockoutMitochondria, LiverMitochondrial ProteinsCation Transport ProteinsConnexin 26ConnexinsGap Junction beta-1 ProteinMitochondrial ProteinsSfxn1 protein, mouse

Identifiers

PMID23590695
PMCPMC3714164
OpenAlexW1976134150

What OpenQuestion holds

Textmetadata
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.