Evidence map›Paper›PMID 24508467›Full record

ReviewFEBS letters2014

Specific Cx43 phosphorylation events regulate gap junction turnover in vivo.

Joell L Solan, Paul D Lampe

Open access · bronzeAbstract readReview
In one paragraph

Review in FEBS letters, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 147 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
147citing papers in PubMed, 1 pooled it
13.1field-weighted citation impact, top 1% 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

147 citing papers in PubMed, 1 synthesis or guideline pooled it, 241 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Deceiving the gatekeepers: virus modulation of gap junctions.Microbiology and molecular biology reviews : MMBR · 2025
    Review
  11. Injury-induced connexin 43 expression regulates endothelial wound healing.American journal of physiology. Heart and circulatory physiology · 2025
    Article
  12. Article
  13. Review
  14. Cx45 regulation by kinases and impact of expression in heart failure.Journal of molecular and cellular cardiology · 2025
    Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. [RgpB contributes to chemoresistance in esophageal squamous cell carcinoma by preventing Cx43 degradationNan fang yi ke da xue xue bao = Journal of Southern Medical University · 2024
    Article
  20. Article

87 more citing papers are in PubMed but not listed here.

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

2 authors at 1 institution in 1 country.

Joell L SolanTranslational Research Program, Fred Hutchinson Cancer Research Center, Seattle, WA 98109, United States.
Paul D LampeTranslational Research Program, Fred Hutchinson Cancer Research Center, Seattle, WA 98109, United States. Electronic address: plampe@fhcrc.org.
Fred Hutch Cancer Center · US

Funding

PHOSPHORYLATION OF GAP JUNCTION PROTEINSR01GM055632 · NIGMS · FRED HUTCHINSON CANCER RESEARCH CENTER · PI LAMPE, PAUL D. · 1997 to 2017
$6.1M
NIGMS NIH HHS R01 GM055632NIGMS NIH HHS R01GM055632
6 · The paper itself

Abstract

Gap junctions, composed of proteins from the connexin gene family, are highly dynamic structures that are regulated by kinase-mediated signaling pathways and interactions with other proteins. Phosphorylation of Connexin43 (Cx43) at different sites controls gap junction assembly, gap junction size and gap junction turnover. Here we present a model describing how Akt, mitogen activated protein kinase (MAPK) and src kinase coordinate to regulate rapid turnover of gap junctions. Specifically, Akt phosphorylates Cx43 at S373 eliminating interaction with zona occludens-1 (ZO-1) allowing gap junctions to enlarge. Then MAPK and src phosphorylate Cx43 to initiate turnover. We integrate published data with new data to test and refine this model. Finally, we propose that differential coordination of kinase activation and Cx43 phosphorylation controls the specific routes of disassembly, e.g., annular junction formation or gap junctions can potentially "unzip" and be internalized/endocytosed into the cell that produced each connexin.

Indexed as

Protein Processing, Post-TranslationalAnimalsCell LineConnexin 43Gap JunctionsHumansMitogen-Activated Protein KinasesPhosphorylationZonula Occludens-1 ProteinConnexin 43Mitogen-Activated Protein KinasesZonula Occludens-1 ProteinConnexin43Gap junctionMitogen-activated protein kinasePhosphorylationProtein kinase CSrc

Identifiers

PMID24508467
PMCPMC3989505
OpenAlexW2132384646

What OpenQuestion holds

Textmetadata
LicenceTDM
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.