Evidence map›Paper›PMID 26745416›Full record

ArticleBiophysical journal2016

Determinants of Cx43 Channel Gating and Permeation: The Amino Terminus.

José F Ek Vitorín, Tasha K Pontifex, Janis M Burt

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2016. 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
1.7field-weighted citation impact, top 16% 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, 28 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. The Anti-Epileptic Effects of Carbenoxolone In Vitro and In Vivo.International journal of molecular sciences · 2022
    Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Calmodulin-Mediated Regulation of Gap Junction Channels.International journal of molecular sciences · 2020
    Review
  13. Review
  14. Review
  15. Article
  16. Article
  17. Article
  18. The NHAmerican journal of physiology. Cell physiology · 2017
    Article
  19. Mechanism of gating by calcium in connexin hemichannels.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  20. 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 1 institution in 1 country.

José F Ek VitorínDepartment of Physiology, University of Arizona, Tucson, Arizona. Electronic address: ekvitori@email.arizona.edu.
Tasha K PontifexDepartment of Physiology, University of Arizona, Tucson, Arizona.
Janis M BurtDepartment of Physiology, University of Arizona, Tucson, Arizona.
University of Arizona · US

Funding

GAP JUNCTIONS IN VASCULAR SMOOTH MUSCLE--GROWTH CONTROLR01HL058732 · NHLBI · UNIVERSITY OF ARIZONA · PI BURT, JANIS M · 1997 to 2014
$4.2M
Phosphorylation and gating of cardiac connexin channelsR01HL131712 · NHLBI · UNIVERSITY OF ARIZONA · PI BURT, JANIS M, SORGEN, PAUL L · 2016 to 2019
$1.5M
Design of virucidal lectins targeting HIV.R01GM086199 · NIGMS · STATE UNIVERSITY NEW YORK STONY BROOK · PI GREEN, DAVID F · 2009 to 2013
$1.4M
NHLBI NIH HHS R01 HL058732NHLBI NIH HHS R01 HL131712NIGMS NIH HHS GM086199
6 · The paper itself

Abstract

Separate connexin domains partake in proposed gating mechanisms of gap junction channels. The amino-terminus (NT) domains, which contribute to voltage sensing, may line the channel's cytoplasmic-facing funnel surface, stabilize the channel's overall structure through interactions with the transmembrane domains and each other, and integrate to form a compound particle to gate the channel closed. Interactions of the carboxyl-terminus (CT) and cytoplasmic loop (CL) domains underlie voltage- and low pH-triggered channel closure. To elucidate potential cooperation of these gating mechanisms, we replaced the Cx43NT with the Cx37NT (chimera Cx43(∗)NT37), leaving the remainder of the Cx43 sequence, including the CT and CL, unchanged. Compared to wild-type Cx43 (Cx43WT), Cx43(∗)NT37 junctions exhibited several functional alterations: extreme resistance to halothane- and acidification-induced uncoupling, absence of voltage-dependent fast inactivation, longer channel open times, larger unitary channel conductances, low junctional dye permeability/permselectivity, and an overall cation selectivity more typical of Cx37WT than Cx43WT junctions. Together, these results suggest a cohesive model of channel function wherein: 1) channel conductance and size selectivity are largely determined by pore diameter, whereas charge selectivity results from the NT domains, and 2) transition between fully open and (multiple) closed states involves global changes in structure of the pore-forming domains transduced by interactions of the pore-forming domains with either the NT, CT, or both, with the NT domains forming the gate of the completely closed channel.

Indexed as

Ion Channel GatingAmino Acid SequenceCell LineConnexin 43Electrophysiological PhenomenaHalothaneHydrogen-Ion ConcentrationMolecular Sequence DataPermeabilityProtein StabilityConnexin 43Halothane

Identifiers

PMID26745416
PMCPMC4805864
OpenAlexW2222154559

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.