Evidence map›Paper›PMID 23455769›Full record

ReviewPhysiology (Bethesda, Md.)2013

Proteins and mechanisms regulating gap-junction assembly, internalization, and degradation.

Anastasia F Thévenin, Tia J Kowal, John T Fong, Rachael M Kells, Charles G Fisher, Matthias M Falk

Open access · greenAbstract readReview
In one paragraph

Review in Physiology (Bethesda, Md.), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 78 papers.

0numbers the graph read from it
0cells of the map it votes in
78citing papers in PubMed
6.6field-weighted citation impact, top 2% 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

78 citing papers in PubMed, 152 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Cx45 regulation by kinases and impact of expression in heart failure.Journal of molecular and cellular cardiology · 2025
    Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Review
  10. Article
  11. Review
  12. Retinoic Acid InfluencesBioelectricity · 2023
    Article
  13. Endocytosis and Endocytic Motifs across the Connexin Gene Family.International journal of molecular sciences · 2023
    Article
  14. Review
  15. Cytomembrane Trafficking Pathways of Connexin 26, 30, and 43.International journal of molecular sciences · 2023
    Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

18 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

6 authors at 1 institution in 1 country.

Anastasia F ThéveninDepartment of Biological Sciences, Lehigh University, Bethlehem, Pennsylvania, USA.
Tia J Kowal
John T Fong
Rachael M Kells
Charles G Fisher
Matthias M Falk
Lehigh University · US

Funding

SYNTHESIS AND MATURATION OF OLIGOMERIC MEMBRANE PROTEINSR01GM055725 · NIGMS · SCRIPPS RESEARCH INSTITUTE · PI FALK, MATTHIAS M · 1998 to 2013
$2.5M
NIGMS NIH HHS GM-55725NIGMS NIH HHS R01 GM055725
6 · The paper itself

Abstract

Gap junctions (GJs) are the only known cellular structures that allow a direct cell-to-cell transfer of signaling molecules by forming densely packed arrays or "plaques" of hydrophilic channels that bridge the apposing membranes of neighboring cells. The crucial role of GJ-mediated intercellular communication (GJIC) for all aspects of multicellular life, including coordination of development, tissue function, and cell homeostasis, has been well documented. Assembly and degradation of these membrane channels is a complex process that includes biosynthesis of the connexin (Cx) subunit proteins (innexins in invertebrates) on endoplasmic reticulum (ER) membranes, oligomerization of compatible subunits into hexameric hemichannels (connexons), delivery of the connexons to the plasma membrane (PM), head-on docking of compatible connexons in the extracellular space at distinct locations, arrangement of channels into dynamic spatially and temporally organized GJ channel plaques, as well as internalization of GJs into the cytoplasm followed by their degradation. Clearly, precise modulation of GJIC, biosynthesis, and degradation are crucial for accurate function, and much research currently addresses how these fundamental processes are regulated. Here, we review posttranslational protein modifications (e.g., phosphorylation and ubiquitination) and the binding of protein partners (e.g., the scaffolding protein ZO-1) known to regulate GJ biosynthesis, internalization, and degradation. We also look closely at the atomic resolution structure of a GJ channel, since the structure harbors vital cues relevant to GJ biosynthesis and turnover.

Indexed as

AnimalsGap JunctionsHumansIon ChannelsProteinsProtein TransportProteolysisIon ChannelsProteins

Identifiers

PMID23455769
PMCPMC3768091
OpenAlexW2112161754

What Socratic 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 Socratic graph.