Evidence map›Paper›PMID 25260631›Full record

ArticleThe Journal of physiology2014

Charge at the 46th residue of connexin 50 is crucial for the gap-junctional unitary conductance and transjunctional voltage-dependent gating.

Xiaoling Tong, Hiroshi Aoyama, Tomitake Tsukihara, Donglin Bai

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of physiology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.4field-weighted citation impact, top 20% 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

14 citing papers in PubMed, 29 citations in OpenAlex.

  1. Article
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  10. Review
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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 3 institutions in 2 countries.

Xiaoling TongDepartment of Physiology and Pharmacology, Western University, London, Ontario, Canada.
Hiroshi AoyamaGraduate School of Pharmaceutical Sciences, Osaka University, Osaka, Japan.
Tomitake TsukiharaInstitutes for Protein Research, Osaka University, Osaka, Japan Department of Life Science, University of Hyogo, 3-2-1 Koto, Kamighori, Akoh, Hyogo 678-1297, Japan.
Donglin BaiDepartment of Physiology and Pharmacology, Western University, London, Ontario, Canada donglin.bai@schulich.uwo.ca.
Western University · CAOsaka University of Pharmaceutical Sciences · JPUniversity of Hyogo · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Gap-junction (GJ) channels are twice the length of most membrane channels, yet they often have large unitary channel conductance (γj). What factors make this possibly the longest channel so efficient in passing ions are not fully clear. Here we studied the lens connexin (Cx) 50 GJs, which display one of the largest γj and the most sensitive transjunctional voltage-dependent gating (Vj gating) among all GJ channels. Introduction of charged residues into a putative pore-lining domain (the first transmembrane and the first extracellular loop border) drastically altered the apparent γj. Specifically, G46D and G46E increased the Cx50 γj from 201 to 256 and 293 pS, respectively and the G46K channel showed an apparent γj of only 20 pS. G46K also drastically altered Vj gating properties in homotypic G46K and heterotypic Cx50/G46K channels, causing an apparent loss of fast Vj-dependent gating transitions and leaving only loop gating transitions at the single channel current records. Both macroscopic and single channel currents of heterotypic Cx50/G46K channels showed a prominent rectification. Our homology structural models indicate that the pore surface electrostatic potentials are a dictating factor in determining the γj. Our data demonstrate, at the whole GJ channel level, a crucial role of the surface charge properties in the first transmembrane/first extracellular border domain in determining the efficiency of ion permeation and the Vj gating of Cx50 and possibly other GJ channels.

Indexed as

Amino Acid SubstitutionAnimalsCell LineConnexin 50ConnexinsEye ProteinsGap JunctionsHumansIon Channel GatingMiceModels, MolecularMutagenesis, Site-DirectedMutant ProteinsProtein Structure, TertiaryRecombinant ProteinsStatic ElectricityConnexin 50ConnexinsEye ProteinsMutant ProteinsRecombinant Proteins

Identifiers

PMID25260631
PMCPMC4262333
OpenAlexW1529175255

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.