Evidence map›Paper›PMID 27280719›Full record

ArticlePloS one2016

Connexin43 Forms Supramolecular Complexes through Non-Overlapping Binding Sites for Drebrin, Tubulin, and ZO-1.

Cinzia Ambrosi, Cynthia Ren, Gaelle Spagnol, Gabriel Cavin, Angela Cone, Elena E Grintsevich, Gina E Sosinsky, Paul L Sorgen

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed, 2 pooled it
5.6field-weighted citation impact, top 4% 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

46 citing papers in PubMed, 2 syntheses or guidelines pooled it, 73 citations in OpenAlex.

  1. Pooled it
  2. Pooled it
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Cx45 regulation by kinases and impact of expression in heart failure.Journal of molecular and cellular cardiology · 2025
    Article
  9. Review
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Review
  16. Cytomembrane Trafficking Pathways of Connexin 26, 30, and 43.International journal of molecular sciences · 2023
    Review
  17. Article
  18. Article
  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

8 authors at 3 institutions in 1 country.

Cinzia AmbrosiNational Center for Microscopy and Imaging Research, Center for Research in Biological Systems, University of California La Jolla, La Jolla, California, United States of America.
Cynthia RenNational Center for Microscopy and Imaging Research, Center for Research in Biological Systems, University of California La Jolla, La Jolla, California, United States of America.
Gaelle SpagnolDepartment of Biochemistry and Molecular Biology, University of Nebraska Medical Center, Omaha, Nebraska, United States of America.
Gabriel CavinNational Center for Microscopy and Imaging Research, Center for Research in Biological Systems, University of California La Jolla, La Jolla, California, United States of America.
Angela ConeNational Center for Microscopy and Imaging Research, Center for Research in Biological Systems, University of California La Jolla, La Jolla, California, United States of America.
Elena E GrintsevichDepartment of Chemistry and Biochemistry, University of California Los Angeles, Los Angeles, California, United States of America.
Gina E SosinskyNational Center for Microscopy and Imaging Research, Center for Research in Biological Systems, University of California La Jolla, La Jolla, California, United States of America.
Paul L SorgenDepartment of Biochemistry and Molecular Biology, University of Nebraska Medical Center, Omaha, Nebraska, United States of America.
University of Nebraska Medical Center · USUniversity of California, Los Angeles · USUniversity of California, San Diego · US

Funding

Mechanisms of Gap Junction RegulationR01GM072631 · NIGMS · UNIVERSITY OF NEBRASKA MEDICAL CENTER · PI SORGEN, PAUL L · 2006 to 2025
$6.4M
Research Pilot Project ProgramP30GM106397 · NIGMS · UNIVERSITY OF NEBRASKA MEDICAL CENTER · PI JOHNSON, KEITH R · 2013 to 2017
$4.9M
STRUCTURE AND DYNAMICS OF CONNEXIN26 GAP JUNCTIONSR01GM065937 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI PERKINS, GUY A · 2003 to 2016
$3.9M
STRUCTURAL ANALYSIS OF GAP JUNCTION TRAFFICKINGR01GM072881 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI PERKINS, GUY A · 2005 to 2015
$2.6M
NIGMS NIH HHS P30 GM106397NIGMS NIH HHS R01 GM065937NIGMS NIH HHS R01 GM072631NIGMS NIH HHS R01 GM072881
6 · The paper itself

Abstract

Gap junctions are membrane specialization domains identified in most tissue types where cells abut each other. The connexin channels found in these membrane domains are conduits for direct cell-to-cell transfer of ions and molecules. Connexin43 (Cx43) is the most ubiquitous connexin, with critical roles in heart, skin, and brain. Several studies described the interaction between Cx43 and the cytoskeleton involving the actin binding proteins Zonula occludens (ZO-1) and drebrin, as well as with tubulin. However, a direct interaction has not been identified between drebrin and Cx43. In this study, co-IP and NMR experiments were used to demonstrate that the Cx43-CT directly interacts with the highly conserved N-terminus region of drebrin. Three Cx43-CT areas were found to be involved in drebrin binding, with residues 264-275 being critical for the interaction. Mimicking Src phosphorylation within this region (Y265) significantly disrupted the interaction between the Cx43-CT and drebrin. Immunofluorescence showed colocalization of Cx43, drebrin, and F-actin in astrocytes and Vero cells membrane, indicating that Cx43 forms a submembrane protein complex with cytoskeletal and scaffolding proteins. The co-IP data suggest that Cx43 indirectly interacts with F-actin through drebrin. Along with the known interaction of the Cx43-CT with ZO-1 and tubulin, the data presented here for drebrin indicate non-overlapping and separated binding sites for all three proteins for which simultaneous binding could be important in regulating cytoskeleton rearrangements, especially for neuronal migration during brain development.

Indexed as

Actin CytoskeletonAnimalsAstrocytesBinding SitesBrainCell MovementCells, CulturedChlorocebus aethiopsConnexin 43FemaleGap JunctionsHumansMultiprotein ComplexesNeuropeptidesPDZ DomainsPhosphorylationConnexin 43drebrinsMultiprotein ComplexesNeuropeptidesTubulinZonula Occludens-1 Protein

Identifiers

PMID27280719
PMCPMC4900556
OpenAlexW2418205215

What Socratic 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 Socratic graph.