Evidence map›Paper›PMID 27229925›Full record

ReviewBMC cell biology2016

Regulation of gap junction channels and hemichannels by phosphorylation and redox changes: a revision.

Kristin Pogoda, Petra Kameritsch, Mauricio A Retamal, José L Vega

Open access · goldAbstract readReview
In one paragraph

Review in BMC cell biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 84 papers.

0numbers the graph read from it
0cells of the map it votes in
84citing papers in PubMed
9.2field-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

84 citing papers in PubMed, 150 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Review
  5. Review
  6. Article
  7. Review
  8. Review
  9. Oxidative stress and atrial fibrillation.Journal of molecular and cellular cardiology · 2024
    Review
  10. Article
  11. Article
  12. Article
  13. Gap Junctions in Ctenophora.Methods in molecular biology (Clifton, N.J.) · 2024
    Article
  14. Evaluation of Connexin Hemichannel Activity In Vivo.Methods in molecular biology (Clifton, N.J.) · 2024
    Article
  15. Review
  16. Review
  17. Article
  18. Article
  19. Review
  20. Article

24 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

4 authors at 4 institutions in 2 countries.

Kristin PogodaWalter Brendel Centre of Experimental Medicine, Ludwig-Maximilians-Universität München and Munich University Hospital, München, Germany. kristin.pogoda@lrz.uni-muenchen.de.
Petra KameritschWalter Brendel Centre of Experimental Medicine, Ludwig-Maximilians-Universität München and Munich University Hospital, München, Germany.
Mauricio A RetamalCentro de Fisiología Celular e Integrativa, Facultad de Medicina, Clínica Alemana Universidad del Desarrollo, Santiago, Chile.
José L VegaExperimental Physiology Laboratory (EPhyL), Antofagasta Institute, Universidad de Antofagasta, Antofagasta, Chile.
Clínica Alemana · CLGerman Centre for Cardiovascular Research · DELudwig-Maximilians-Universität München · DEUniversidad de Antofagasta · CL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Post-translational modifications of connexins play an important role in the regulation of gap junction and hemichannel permeability. The prerequisite for the formation of functional gap junction channels is the assembly of connexin proteins into hemichannels and their insertion into the membrane. Hemichannels can affect cellular processes by enabling the passage of signaling molecules between the intracellular and extracellular space. For the intercellular communication hemichannels from one cell have to dock to its counterparts on the opposing membrane of an adjacent cell to allow the transmission of signals via gap junctions from one cell to the other. The controlled opening of hemichannels and gating properties of complete gap junctions can be regulated via post-translational modifications of connexins. Not only channel gating, but also connexin trafficking and assembly into hemichannels can be affected by post-translational changes. Recent investigations have shown that connexins can be modified by phosphorylation/dephosphorylation, redox-related changes including effects of nitric oxide (NO), hydrogen sulfide (H2S) or carbon monoxide (CO), acetylation, methylation or ubiquitination. Most of the connexin isoforms are known to be phosphorylated, e.g. Cx43, one of the most studied connexin at all, has 21 reported phosphorylation sites. In this review, we provide an overview about the current knowledge and relevant research of responsible kinases, connexin phosphorylation sites and reported effects on gap junction and hemichannel regulation. Regarding the effects of oxidants we discuss the role of NO in different cell types and tissues and recent studies about modifications of connexins by CO and H2S.

Indexed as

Amino Acid SequenceAnimalsCarbon MonoxideGap JunctionsHumansHydrogen SulfideIon ChannelsOxidation-ReductionPhosphorylationProtein KinasesCarbon MonoxideHydrogen SulfideIon ChannelsProtein KinasesChannelsGap junctionHemichannelNitric OxidePhosphorylationRedox

Identifiers

PMID27229925
PMCPMC4896245
OpenAlexW2397975465

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.