Evidence map›Paper›PMID 19626334›Full record

ArticleHistochemistry and cell biology2009

Limiting transport steps and novel interactions of Connexin-43 along the secretory pathway.

Irina V Majoul, Daria Onichtchouk, Eugenia Butkevich, Dirk Wenzel, Levon M Chailakhyan, Rainer Duden

Open access · bronzeAbstract read
In one paragraph

Article in Histochemistry and cell biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
0.7field-weighted citation impact, top 30% 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

20 citing papers in PubMed, 30 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Connexins and Glucose Metabolism in Cancer.International journal of molecular sciences · 2022
    Review
  6. Intracellular trafficking pathways of Cx43 gap junction channels.Biochimica et biophysica acta. Biomembranes · 2018
    Review
  7. Article
  8. Article
  9. Review
  10. Article
  11. Review
  12. Article
  13. Review
  14. Article
  15. Review
  16. Fast structural responses of gap junction membrane domains to AB5 toxins.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  17. Article
  18. Article
  19. Gap junctions.Comprehensive Physiology · 2012
    Review
  20. Review
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 5 institutions in 2 countries.

Irina V MajoulInstitute of Biology, Center for Structural and Cell Biology in Medicine, University of Lübeck, Ratzeburger Allee 160, 23538, Lübeck, Germany. irina.majoul@bio.uni-luebeck.de
Daria Onichtchouk
Eugenia Butkevich
Dirk Wenzel
Levon M Chailakhyan
Rainer Duden
University of Lübeck · DEInstitute of Theoretical and Experimental Biophysics · RUMax Planck Institute for Biophysical Chemistry · DEUniversity of Freiburg · DEUniversity of Göttingen · DE

Funding

Wellcome TrustWellcome Trust 047578
6 · The paper itself

Abstract

Connexins are four-transmembrane-domain proteins expressed in all vertebrates which form permeable gap junction channels that connect cells. Here, we analysed Connexin-43 (Cx43) transport to the plasma membrane and studied the effects of small GTPases acting along the secretory pathway. We show that both GTP- and GDP-restricted Sar1 prevents exit of Cx43 from the endoplasmic reticulum (ER), but only GTP-restricted Sar1 arrests Cx43 in COP II-coated ER exit sites and accumulates 14-3-3 proteins in the ER fraction. FRET-FLIM data confirm that already in ER exit sites Cx43 exists in oligomeric form, suggesting an in vivo role for 14-3-3 in Cx43 oligomerization. Exit of Cx43 from the ER can be blocked by other factors--such as expression of the beta subunit of the COP I coat or p50/dynamitin that acts on the microtubule-based dynein motor complex. GTP-restricted Arf1 blocks Cx43 in the Golgi. Lastly, we show that GTP-restricted Arf6 removes Cx43 gap junction plaques from the cell-cell interface and targets them to degradation. These data provide a molecular explanation of how small GTPases act to regulate Cx43 transport through the secretory pathway, facilitating or abolishing cell-cell communication through gap junctions.

Indexed as

14-3-3 ProteinsAmino Acid SequenceAnimalsChlorocebus aethiopsConnexin 43Cryoelectron MicroscopyEndoplasmic ReticulumFluorescence Recovery After PhotobleachingGap JunctionsGolgi ApparatusMiceMicroscopy, ConfocalMolecular Sequence DataProtein TransportSecretory PathwayVero Cells14-3-3 ProteinsConnexin 43

Identifiers

PMID19626334
PMCPMC2756399
OpenAlexW2111114683

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.