Evidence map›Paper›PMID 24133065›Full record

ArticleAmerican journal of physiology. Cell physiology2013

Carboxy terminus and pore-forming domain properties specific to Cx37 are necessary for Cx37-mediated suppression of insulinoma cell proliferation.

Tasha K Nelson, Paul L Sorgen, Janis M Burt

Abstract read
In one paragraph

Article in American journal of physiology. Cell physiology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.2field-weighted citation impact, top 21% 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

19 citing papers in PubMed, 29 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Connexin43 Carboxyl-Terminal Domain Directly Interacts with β-Catenin.International journal of molecular sciences · 2018
    Article
  10. Protein⁻Protein Interactions with Connexin 43: Regulation and Function.International journal of molecular sciences · 2018
    Review
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. 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

3 authors at 2 institutions in 1 country.

Tasha K NelsonDepartment of Physiology, University of Arizona, Tucson, Arizona; and.
Paul L Sorgen
Janis M Burt
University of Arizona · USUniversity of Nebraska Medical Center · US

Funding

Mechanisms of Gap Junction RegulationR01GM072631 · NIGMS · UNIVERSITY OF NEBRASKA MEDICAL CENTER · PI SORGEN, PAUL L · 2006 to 2025
$6.4M
GAP JUNCTIONS IN VASCULAR SMOOTH MUSCLE--GROWTH CONTROLR01HL058732 · NHLBI · UNIVERSITY OF ARIZONA · PI BURT, JANIS M · 1997 to 2014
$4.2M
NHLBI NIH HHS 5R01-HL-058732NHLBI NIH HHS R01 HL058732NIGMS NIH HHS 5R01-GM-072631NIGMS NIH HHS R01 GM072631
6 · The paper itself

Abstract

Connexin 37 (Cx37) suppresses cell proliferation when expressed in rat insulinoma (Rin) cells, an effect also manifest in vivo during vascular development and in response to tissue injury. Mutant forms of Cx37 with nonfunctional channels but normally localized, wild-type carboxy termini are not growth suppressive. Here we determined whether the carboxy-terminal (CT) domain is required for Cx37-mediated growth suppression and whether the Cx37 pore-forming domain can be replaced with the Cx43 pore-forming domain and still retain growth-suppressive properties. We show that despite forming functional gap junction channels and hemichannels, Cx37 with residues subsequent to 273 replaced with a V5-epitope tag (Cx37-273tr*V5) had no effect on the proliferation of Rin cells, did not facilitate G1-cell cycle arrest with serum deprivation, and did not prolong cell cycle time comparably to the wild-type protein. The chimera Cx43*CT37, comprising the pore-forming domain of Cx43 and CT of Cx37, also did not suppress proliferation, despite forming functional gap junctions with a permselective profile similar to wild-type Cx37. Differences in channel behavior of both Cx37-273tr*V5 and Cx43*CT37 relative to their wild-type counterparts and failure of the Cx37-CT to interact as the Cx43-CT does with the Cx43 cytoplasmic loop suggest that the Cx37-CT and pore-forming domains are both essential to growth suppression by Cx37.

Indexed as

AnimalsCell Line, TumorConnexinsElectrophysiological PhenomenaGap Junction alpha-4 ProteinGene Expression Regulation, NeoplasticInsulinomaMutationPancreatic NeoplasmsProtein ConformationProtein Structure, TertiaryRatsRecombinant Fusion ProteinsConnexinsGap Junction alpha-4 ProteinRecombinant Fusion Proteinsconnexinendotheliumgap junction channelgrowth suppressionprotein interactome

Identifiers

PMID24133065
PMCPMC3882364
OpenAlexW2327959705

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.